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Volumn 14, Issue 3, 2015, Pages 167-182

Erratum: Advances in the development of influenza virus vaccines (Nature Reviews Drug Discovery (2015) 14 (167-182) DOI: 10.1038/nrd4529);Advances in the development of influenza virus vaccines

Author keywords

[No Author keywords available]

Indexed keywords

DNA VACCINE; EPITOPE; GLYCAN; HEMAGGLUTININ; INACTIVATED VIRUS VACCINE; INFLUENZA VACCINE; PROTEIN M2; TRIPLE VACCINE; VIRUS SIALIDASE; VIRUS ANTIGEN;

EID: 84924060844     PISSN: 14741776     EISSN: 14741784     Source Type: Journal    
DOI: 10.1038/nrd4595     Document Type: Erratum
Times cited : (487)

References (232)
  • 1
    • 84924065775 scopus 로고    scopus 로고
    • Influenza (seasonal) fact sheet
    • World Health Organization
    • World Health Organization. Influenza (seasonal) fact sheet. World Health Organization [online], http://www.who.int/mediacentre/factsheets/fs211/en (2014).
    • (2014) World Health Organization
  • 2
    • 0037402228 scopus 로고    scopus 로고
    • The annual production cycle for influenza vaccine
    • Gerdil, C. The annual production cycle for influenza vaccine. Vaccine 21, 1776-1779 (2003).
    • (2003) Vaccine , vol.21 , pp. 1776-1779
    • Gerdil, C.1
  • 3
    • 10944240992 scopus 로고    scopus 로고
    • Influenza: Old and new threats
    • Palese, P. Influenza: old and new threats. Nature Med. 10, S82-S87 (2004).
    • (2004) Nature Med. , vol.10 , pp. S82-S87
    • Palese, P.1
  • 4
    • 0036514779 scopus 로고    scopus 로고
    • Updating the accounts: Global mortality of the 1918-1920 "spanish" influenza pandemic
    • Johnson, N. P. & Mueller, J. Updating the accounts: global mortality of the 1918-1920 "Spanish" influenza pandemic. Bull. Hist. Med. 76, 105-115 (2002).
    • (2002) Bull. Hist. Med. , vol.76 , pp. 105-115
    • Johnson, N.P.1    Mueller, J.2
  • 5
    • 80455168614 scopus 로고    scopus 로고
    • Why do influenza virus subtypes die out? A hypothesis
    • Palese, P. & Wang, T. T. Why do influenza virus subtypes die out? A hypothesis. MBio 2, e00150-11 (2011).
    • (2011) MBio , vol.2 , pp. e00150-e00211
    • Palese, P.1    Wang, T.T.2
  • 6
    • 84924069867 scopus 로고    scopus 로고
    • Pandemic influenza vaccine was too late in 2009
    • Racaniello, V. Pandemic influenza vaccine was too late in 2009. Virology Blog [online], http://www.virology. ws/2010/12/09/pandemic-influenza-vaccine-was-too-late-in-2009 (2010).
    • (2010) Virology Blog
    • Racaniello, V.1
  • 7
    • 84890965081 scopus 로고    scopus 로고
    • Universal influenza virus vaccines: Need for clinical trials
    • Krammer, F. & Palese, P. Universal influenza virus vaccines: need for clinical trials. Nature Immunol. 15, 3-5 (2014).
    • (2014) Nature Immunol. , vol.15 , pp. 3-5
    • Krammer, F.1    Palese, P.2
  • 8
    • 34748870647 scopus 로고
    • Protective effect of vaccination against induced influenza A
    • Francis, T., Salk, J. E., Pearson, H. E. & Brown, P. N. Protective effect of vaccination against induced influenza A. J. Clin. Invest. 24, 536-546 (1945).
    • (1945) J. Clin. Invest. , vol.24 , pp. 536-546
    • Francis, T.1    Salk, J.E.2    Pearson, H.E.3    Brown, P.N.4
  • 9
    • 34748899356 scopus 로고
    • Protective effect of vaccination against induced influenza B
    • Salk, J. E., Pearson, H. E., Brown, P. N. & Francis, T. Protective effect of vaccination against induced influenza B. J. Clin. Invest. 24, 547-553 (1945).
    • (1945) J. Clin. Invest. , vol.24 , pp. 547-553
    • Salk, J.E.1    Pearson, H.E.2    Brown, P.N.3    Francis, T.4
  • 10
    • 0005626705 scopus 로고
    • Importance of antigenic composition of influenza virus vaccine in protecting against the natural disease; Observations during the winter of 1947-1948
    • Salk, J. E. & Suriano, P. C. Importance of antigenic composition of influenza virus vaccine in protecting against the natural disease; observations during the winter of 1947-1948. Am. J. Public Health Nations Health 39, 345-355 (1949).
    • (1949) Am. J. Public Health Nations Health , vol.39 , pp. 345-355
    • Salk, J.E.1    Suriano, P.C.2
  • 11
    • 0001720378 scopus 로고
    • The influenza programme of WHO
    • Payne, A. M. The influenza programme of WHO. Bull. World Health Organ. 8, 755-774 (1953).
    • (1953) Bull. World Health Organ. , vol.8 , pp. 755-774
    • Payne, A.M.1
  • 12
    • 0017596739 scopus 로고
    • Reactogenicity and immunogenicity of bivalent influenza A and monovalent influenza B virus vaccines in high-risk children
    • Allison, J. E., Glezen, W. P., Taber, L. H., Paredes, A. & Webster, R. G. Reactogenicity and immunogenicity of bivalent influenza A and monovalent influenza B virus vaccines in high-risk children. J. Infect. Dis. 136, S672-S676 (1977).
    • (1977) J. Infect. Dis. , vol.136 , pp. S672-S676
    • Allison, J.E.1    Glezen, W.P.2    Taber, L.H.3    Paredes, A.4    Webster, R.G.5
  • 13
    • 0001925693 scopus 로고
    • Comparisons of serologic and febrile responses in humans to vaccination with influenza A viruses or their hemagglutinins
    • Davenport, F. M. et al. Comparisons of serologic and febrile responses in humans to vaccination with influenza A viruses or their hemagglutinins. J. Lab. Clin. Med. 63, 5-13 (1964).
    • (1964) J. Lab. Clin. Med. , vol.63 , pp. 5-13
    • Davenport, F.M.1
  • 15
    • 0014199799 scopus 로고
    • Adaptation and growth characteristics of influenza virus at 25°C
    • Maassab, H. F. Adaptation and growth characteristics of influenza virus at 25°C. Nature 213, 612-614 (1967).
    • (1967) Nature , vol.213 , pp. 612-614
    • Maassab H. ., F.1
  • 16
    • 0022486360 scopus 로고
    • Study of live recombinant cold-adapted influenza bivalent vaccine of type A for use in children: An epidemiological control trial
    • Alexandrova, G. I. et al. Study of live recombinant cold-adapted influenza bivalent vaccine of type A for use in children: an epidemiological control trial. Vaccine 4, 114-118 (1986).
    • (1986) Vaccine , vol.4 , pp. 114-118
    • Alexandrova, G.I.1
  • 17
    • 84879212793 scopus 로고    scopus 로고
    • Comparing influenza vaccine efficacy against mismatched and matched strains: A systematic review and meta-analysis
    • Tricco, A. C. et al. Comparing influenza vaccine efficacy against mismatched and matched strains: a systematic review and meta-analysis. BMC Med. 11, 153 (2013).
    • (2013) BMC Med. , vol.11 , pp. 153
    • Tricco, A.C.1
  • 18
    • 84859522686 scopus 로고    scopus 로고
    • Neonatal outcomes after influenza immunization during pregnancy: A randomized controlled trial
    • Steinhoff, M. C. et al. Neonatal outcomes after influenza immunization during pregnancy: a randomized controlled trial. CMAJ 184, 645-653 (2012).
    • (2012) CMAJ , vol.184 , pp. 645-653
    • Steinhoff, M.C.1
  • 19
    • 84865663784 scopus 로고    scopus 로고
    • Effect of influenza vaccination in the first trimester of pregnancy
    • Sheffield, J. S. et al. Effect of influenza vaccination in the first trimester of pregnancy. Obstet. Gynecol. 120, 532-537 (2012).
    • (2012) Obstet. Gynecol. , vol.120 , pp. 532-537
    • Sheffield, J.S.1
  • 20
    • 84887607325 scopus 로고    scopus 로고
    • Cochrane re-arranged: Support for policies to vaccinate elderly people against influenza
    • Beyer, W. E. et al. Cochrane re-arranged: support for policies to vaccinate elderly people against influenza. Vaccine 31, 6030-6033 (2013).
    • (2013) Vaccine , vol.31 , pp. 6030-6033
    • Beyer, W.E.1
  • 21
    • 84877257252 scopus 로고    scopus 로고
    • Influenza vaccine effectiveness in the community and the household
    • Ohmit, S. E. et al. Influenza vaccine effectiveness in the community and the household. Clin. Infect. Dis. 56, 1363-1369 (2013).
    • (2013) Clin. Infect. Dis. , vol.56 , pp. 1363-1369
    • Ohmit, S.E.1
  • 22
    • 84873314436 scopus 로고    scopus 로고
    • Low and decreasing vaccine effectiveness against influenza A(H3) in 2011/12 among vaccination target groups in Europe: Results from the I-MOVE multicentre case-control study
    • Kissling, E. et al. Low and decreasing vaccine effectiveness against influenza A(H3) in 2011/12 among vaccination target groups in Europe: results from the I-MOVE multicentre case-control study. Euro Surveill. 18, 20390 (2013).
    • (2013) Euro Surveill. , vol.18 , pp. 20390
    • Kissling, E.1
  • 23
    • 0020956181 scopus 로고
    • A comparison of live and inactivated influenza A (H1N1) virus vaccines. 2. Long-term immunity
    • Clark, A. et al. A comparison of live and inactivated influenza A (H1N1) virus vaccines. 2. Long-term immunity. J. Hyg. (Lond.) 90, 361-370 (1983).
    • (1983) J. Hyg. (Lond.) , vol.90 , pp. 361-370
    • Clark, A.1
  • 24
    • 0034072605 scopus 로고    scopus 로고
    • Mismatch between the 1997/1998 influenza vaccine and the major epidemic A(H3N2) virus strain as the cause of an inadequate vaccine-induced antibody response to this strain in the elderly
    • de Jong, J. C., Beyer, W. E., Palache, A. M., Rimmelzwaan, G. F. & Osterhaus, A. D. Mismatch between the 1997/1998 influenza vaccine and the major epidemic A(H3N2) virus strain as the cause of an inadequate vaccine-induced antibody response to this strain in the elderly. J. Med. Virol. 61, 94-99 (2000).
    • (2000) J. Med. Virol. , vol.61 , pp. 94-99
    • De Jong, J.C.1    Beyer, W.E.2    Palache, A.M.3    Rimmelzwaan, G.F.4    Osterhaus, A.D.5
  • 25
    • 84872598906 scopus 로고    scopus 로고
    • High-dose trivalent influenza vaccine compared to standard dose vaccine in elderly adults: Safety, immunogenicity and relative efficacy during the 2009-2010 season
    • DiazGranados, C. A. et al. High-dose trivalent influenza vaccine compared to standard dose vaccine in elderly adults: safety, immunogenicity and relative efficacy during the 2009-2010 season. Vaccine 31, 861-866 (2013).
    • (2013) Vaccine , vol.31 , pp. 861-866
    • Diazgranados, C.A.1
  • 26
    • 84906232635 scopus 로고    scopus 로고
    • Efficacy of high-dose versus standard-dose influenza vaccine in older adults
    • DiazGranados, C. A. et al. Efficacy of high-dose versus standard-dose influenza vaccine in older adults. N. Engl. J. Med. 371, 635-645 (2014).
    • (2014) N. Engl. J. Med. , vol.371 , pp. 635-645
    • Diazgranados, C.A.1
  • 29
    • 84878432684 scopus 로고    scopus 로고
    • AS03-adjuvanted influenza vaccine in elderly people
    • Ledgerwood, J. E. AS03-adjuvanted influenza vaccine in elderly people. Lancet Infect. Dis. 13, 466-467 (2013).
    • (2013) Lancet Infect. Dis. , vol.13 , pp. 466-467
    • Ledgerwood, J.E.1
  • 30
    • 84896733461 scopus 로고    scopus 로고
    • Immunogenicity, reactogenicity, and safety of inactivated quadrivalent influenza vaccine candidate versus inactivated trivalent influenza vaccine in healthy adults aged ≥18 years: A phase III, randomized trial
    • Tinoco, J. C. et al. Immunogenicity, reactogenicity, and safety of inactivated quadrivalent influenza vaccine candidate versus inactivated trivalent influenza vaccine in healthy adults aged ≥18 years: a phase III, randomized trial. Vaccine 32, 1480-1487 (2014).
    • (2014) Vaccine , vol.32 , pp. 1480-1487
    • Tinoco, J.C.1
  • 31
    • 84890902002 scopus 로고    scopus 로고
    • Vaccine for prevention of mild and moderate-to-severe influenza in children
    • Jain, V. K. et al. Vaccine for prevention of mild and moderate-to-severe influenza in children. N. Engl. J. Med. 369, 2481-2491 (2013).
    • (2013) N. Engl. J. Med. , vol.369 , pp. 2481-2491
    • Jain, V.K.1
  • 32
    • 84896483880 scopus 로고    scopus 로고
    • Vaccine for prevention of influenza in children
    • Esposito, S. & Principi, N. Vaccine for prevention of influenza in children. N. Engl. J. Med. 370, 1167 (2014).
    • (2014) N. Engl. J. Med. , vol.370 , pp. 1167
    • Esposito, S.1    Principi, N.2
  • 33
    • 77956119219 scopus 로고    scopus 로고
    • Induction of broadly neutralizing H1N1 influenza antibodies by vaccination
    • Wei, C. J. et al. Induction of broadly neutralizing H1N1 influenza antibodies by vaccination. Science 329, 1060-1064 (2010).
    • (2010) Science , vol.329 , pp. 1060-1064
    • Wei, C.J.1
  • 34
    • 84865118710 scopus 로고    scopus 로고
    • Elicitation of broadly neutralizing influenza antibodies in animals with previous influenza exposure
    • Wei, C. J. et al. Elicitation of broadly neutralizing influenza antibodies in animals with previous influenza exposure. Sci. Transl. Med. 4, 147ra114 (2012).
    • (2012) Sci. Transl Med. , vol.4 , pp. 147ra114
    • Wei, C.J.1
  • 35
    • 84879882264 scopus 로고    scopus 로고
    • Self-assembling influenza nanoparticle vaccines elicit broadly neutralizing H1N1 antibodies
    • Kanekiyo, M. et al. Self-assembling influenza nanoparticle vaccines elicit broadly neutralizing H1N1 antibodies. Nature 499, 102-106 (2013).
    • (2013) Nature , vol.499 , pp. 102-106
    • Kanekiyo, M.1
  • 36
    • 0003564810 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention. Table. Influenza vaccines - United States 2014-15 influenza season
    • Centers for Disease Control and Prevention. Table. Influenza vaccines - United States, 2014-15 influenza season. Centers for Disease Control and Prevention [online], http://www.cdc.gov/flu/protect/vaccine/vaccines.htm (2014).
    • (2014) Centers for Disease Control and Prevention
  • 37
    • 84924071538 scopus 로고    scopus 로고
    • FDA approves new seasonal influenza vaccine made using novel technology
    • US Food and Drug Administration
    • US Food and Drug Administration. FDA approves new seasonal influenza vaccine made using novel technology. US Food and Drug Administration [online], http://www.fda.gov/NewsEvents/Newsroom/PressAnnouncements/ucm335891.htm (2013).
    • (2013) US Food and Drug Administration
  • 38
    • 0032515638 scopus 로고    scopus 로고
    • Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus
    • Claas, E. C. et al. Human influenza A H5N1 virus related to a highly pathogenic avian influenza virus. Lancet 351, 472-477 (1998).
    • (1998) Lancet , vol.351 , pp. 472-477
    • Claas, E.C.1
  • 39
    • 53049110309 scopus 로고    scopus 로고
    • Evolutionary dynamics and emergence of panzootic H5N1 influenza viruses
    • Vijaykrishna, D. et al. Evolutionary dynamics and emergence of panzootic H5N1 influenza viruses. PLoS Pathog. 4, e1000161 (2008).
    • (2008) PLoS Pathog. , vol.4 , pp. e1000161
    • Vijaykrishna, D.1
  • 40
    • 0035823083 scopus 로고    scopus 로고
    • Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses
    • Hatta, M., Gao, P., Halfmann, P. & Kawaoka, Y. Molecular basis for high virulence of Hong Kong H5N1 influenza A viruses. Science 293, 1840-1842 (2001).
    • (2001) Science , vol.293 , pp. 1840-1842
    • Hatta, M.1    Gao, P.2    Halfmann, P.3    Kawaoka, Y.4
  • 41
    • 0003514452 scopus 로고    scopus 로고
    • World Health Organization. The WHO Influenza Monthly Risk Assessment Summaries.
    • World Health Organization. The WHO Influenza Monthly Risk Assessment Summaries. World Health Organization [online]. http://www.who.int/influenza/human-animal-interface/HAI-Risk-Assessment/en/(2015).
    • (2015) World Health Organization
  • 42
    • 84862777115 scopus 로고    scopus 로고
    • Seroevidence for H5N1 influenza infections in humans: Meta-analysis
    • Wang, T. T., Parides, M. K. & Palese, P. Seroevidence for H5N1 influenza infections in humans: meta-analysis. Science 335, 1463 (2012).
    • (2012) Science , vol.335 , pp. 1463
    • Wang, T.T.1    Parides, M.K.2    Palese, P.3
  • 43
    • 67650407532 scopus 로고    scopus 로고
    • Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans
    • Garten, R. et al. Antigenic and genetic characteristics of swine-origin 2009 A(H1N1) influenza viruses circulating in humans. Science 325, 197-201 (2009).
    • (2009) Science , vol.325 , pp. 197-201
    • Garten, R.1
  • 44
    • 84877785371 scopus 로고    scopus 로고
    • Human infection with a novel avian-origin influenza A (H7N9) virus
    • Gao, R. et al. Human infection with a novel avian-origin influenza A (H7N9) virus. N. Engl. J. Med. 368, 1888-1897 (2013).
    • (2013) N. Engl. J. Med. , vol.368 , pp. 1888-1897
    • Gao, R.1
  • 45
    • 84888865092 scopus 로고    scopus 로고
    • Human infection with avian influenza A H6N1 virus: An epidemiological analysis
    • Wei, S. H. et al. Human infection with avian influenza A H6N1 virus: an epidemiological analysis. Lancet Respir. Med. 1, 771-778 (2013).
    • (2013) Lancet Respir. Med. , vol.1 , pp. 771-778
    • Wei, S.H.1
  • 46
    • 84894094300 scopus 로고    scopus 로고
    • Avian influenza A H10N8 - A virus on the verge?
    • Garc?a-Sastre, A. & Schmolke, M. Avian influenza A H10N8 - a virus on the verge? Lancet 383, 676-677 (2014).
    • (2014) Lancet , vol.383 , pp. 676-677
    • Garca-Sastre, A.1    Schmolke, M.2
  • 47
    • 84894063527 scopus 로고    scopus 로고
    • Clinical and epidemiological characteristics of a fatal case of avian influenza A H10N8 virus infection: A descriptive study
    • Chen, H. et al. Clinical and epidemiological characteristics of a fatal case of avian influenza A H10N8 virus infection: a descriptive study. Lancet 383, 714-721 (2014).
    • (2014) Lancet , vol.383 , pp. 714-721
    • Chen, H.1
  • 48
    • 84924019807 scopus 로고    scopus 로고
    • World's first H5N6 bird flu death reported in China
    • Park, M. World's first H5N6 bird flu death reported in China. CNN [online], http://www.cnn.com/2014/05/07/health/h5n6-flu-china-death (2014).
    • (2014) CNN
    • Park, M.1
  • 49
    • 84865001622 scopus 로고    scopus 로고
    • Notes from the field: Outbreak of influenza A (H3N2) virus among persons and swine at a county fair - Indiana, July 2012
    • Centers for Disease Control and Prevention (CDC)
    • Centers for Disease Control and Prevention (CDC). Notes from the field: outbreak of influenza A (H3N2) virus among persons and swine at a county fair - Indiana, July 2012. MMWR Morb. Mortal. Wkly Rep. 61, 561 (2012).
    • (2012) MMWR Morb. Mortal. Wkly Rep. , vol.61 , pp. 561
  • 50
    • 84882635093 scopus 로고    scopus 로고
    • Highly pathogenic avian influenza A(H7N3) virus in poultry workers, Mexico, 2012
    • Lopez-Martinez, I. et al. Highly pathogenic avian influenza A(H7N3) virus in poultry workers, Mexico, 2012. Emerg. Infect. Dis. 19, 1531-1534 (2013).
    • (2013) Emerg. Infect. Dis. , vol.19 , pp. 1531-1534
    • Lopez-Martinez, I.1
  • 51
    • 84865779963 scopus 로고    scopus 로고
    • Emergence of fatal avian influenza in New England harbor seals
    • Anthony, S. J. et al. Emergence of fatal avian influenza in New England harbor seals. MBio 3, e00166-12 (2012).
    • (2012) MBio , vol.3 , pp. e00166-e00212
    • Anthony, S.J.1
  • 52
    • 84911885545 scopus 로고    scopus 로고
    • Avian influenza A(H10N7) virus involvement in mass mortality of harbour seals (Phoca vitulina) in Sweden, March through October 2014
    • Zohari, S., Neimanis, A., Harkonen, T., Moraeus, C. & Valarcher, J. Avian influenza A(H10N7) virus involvement in mass mortality of harbour seals (Phoca vitulina) in Sweden, March through October 2014. Euro Surveill. 19, 20967 (2014).
    • (2014) Euro Surveill. , vol.19 , pp. 20967
    • Zohari, S.1    Neimanis, A.2    Harkonen, T.3    Moraeus, C.4    Valarcher, J.5
  • 53
    • 84911936087 scopus 로고    scopus 로고
    • Avian influenza outbreak in Yorkshire: Strain identified as H5N8
    • [No authors listed.]
    • [No authors listed.] Avian influenza outbreak in Yorkshire: strain identified as H5N8. Vet. Rec. 175, 495-496 (2014).
    • (2014) Vet. Rec. , vol.175 , pp. 495-496
  • 54
    • 84887694501 scopus 로고    scopus 로고
    • The emergence of H7N9 viruses: A chance to redefine correlates of protection for influenza virus vaccines
    • Krammer, F. & Cox, R. J. The emergence of H7N9 viruses: a chance to redefine correlates of protection for influenza virus vaccines. Expert Rev. Vaccines 12, 1369-1372 (2013).
    • (2013) Expert Rev. Vaccines , vol.12 , pp. 1369-1372
    • Krammer, F.1    Cox, R.J.2
  • 55
    • 61349200100 scopus 로고    scopus 로고
    • A phase i clinical trial of a PER.C6® cell grown influenza H7 virus vaccine
    • Cox, R. J. et al. A phase I clinical trial of a PER.C6® cell grown influenza H7 virus vaccine. Vaccine 27, 1889-1897 (2009).
    • (2009) Vaccine , vol.27 , pp. 1889-1897
    • Cox, R.J.1
  • 56
    • 84871147732 scopus 로고    scopus 로고
    • Evaluations for in vitro correlates of immunogenicity of inactivated influenza a H5, H7 and H9 vaccines in humans
    • Couch, R. B. et al. Evaluations for in vitro correlates of immunogenicity of inactivated influenza a H5, H7 and H9 vaccines in humans. PLoS ONE 7, e50830 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e50830
    • Couch, R.B.1
  • 57
    • 84871135645 scopus 로고    scopus 로고
    • A randomized clinical trial of an inactivated avian influenza A (H7N7) vaccine
    • Couch, R. B., Patel, S. M., Wade-Bowers, C. L. & Niño, D. A randomized clinical trial of an inactivated avian influenza A (H7N7) vaccine. PLoS ONE 7, e49704 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e49704
    • Couch, R.B.1    Patel, S.M.2    Wade-Bowers, C.L.3    Niño, D.4
  • 58
    • 34447544007 scopus 로고    scopus 로고
    • Cell culture (Vero) derived whole virus (H5N1) vaccine based on wild-type virus strain induces cross-protective immune responses
    • Kistner, O. et al. Cell culture (Vero) derived whole virus (H5N1) vaccine based on wild-type virus strain induces cross-protective immune responses. Vaccine 25, 6028-6036 (2007).
    • (2007) Vaccine , vol.25 , pp. 6028-6036
    • Kistner, O.1
  • 60
    • 84907704195 scopus 로고    scopus 로고
    • Immunogenicity of avian influenza A/Anhui/01/2005(H5N1) vaccine with MF59 adjuvant: A randomized clinical trial
    • Belshe, R. B. et al. Immunogenicity of avian influenza A/Anhui/01/2005(H5N1) vaccine with MF59 adjuvant: a randomized clinical trial. JAMA 312, 1420-1428 (2014).
    • (2014) JAMA , vol.312 , pp. 1420-1428
    • Belshe, R.B.1
  • 61
    • 84907698232 scopus 로고    scopus 로고
    • Serological responses to an avian influenza A/H7N9 vaccine mixed at the point-of-use with MF59 adjuvant: A randomized clinical trial
    • Mulligan, M. J. et al. Serological responses to an avian influenza A/H7N9 vaccine mixed at the point-of-use with MF59 adjuvant: a randomized clinical trial. JAMA 312, 1409-1419 (2014).
    • (2014) JAMA , vol.312 , pp. 1409-1419
    • Mulligan, M.J.1
  • 62
    • 84906670725 scopus 로고    scopus 로고
    • An H7N1 influenza virus vaccine induces broadly reactive antibody responses against H7N9 in humans
    • Krammer, F. et al. An H7N1 influenza virus vaccine induces broadly reactive antibody responses against H7N9 in humans. Clin. Vaccine Immunol. 21, 1153-1163 (2014).
    • (2014) Clin. Vaccine Immunol. , vol.21 , pp. 1153-1163
    • Krammer, F.1
  • 63
    • 84906996647 scopus 로고    scopus 로고
    • Induction of broadly cross-reactive antibody responses to the influenza HA stem region following H5N1 vaccination in humans
    • Ellebedy, A. H. et al. Induction of broadly cross-reactive antibody responses to the influenza HA stem region following H5N1 vaccination in humans. Proc. Natl Acad. Sci. USA 111, 13133-13138 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 13133-13138
    • Ellebedy, A.H.1
  • 64
    • 84908389429 scopus 로고    scopus 로고
    • Induction of broadly-reactive anti-hemagglutinin stalk antibodies by an H5N1 vaccine in humans
    • Nachbagauer, R. et al. Induction of broadly-reactive anti-hemagglutinin stalk antibodies by an H5N1 vaccine in humans. J. Virol. 88, 13260-13268 (2014).
    • (2014) J. Virol. , vol.88 , pp. 13260-13268
    • Nachbagauer, R.1
  • 65
    • 67650470885 scopus 로고    scopus 로고
    • Evaluation of two live attenuated cold-adapted H5N1 influenza virus vaccines in healthy adults
    • Karron, R. A. et al. Evaluation of two live attenuated cold-adapted H5N1 influenza virus vaccines in healthy adults. Vaccine 27, 4953-4960 (2009).
    • (2009) Vaccine , vol.27 , pp. 4953-4960
    • Karron, R.A.1
  • 66
    • 67349237000 scopus 로고    scopus 로고
    • A live attenuated H7N3 influenza virus vaccine is well tolerated and immunogenic in a phase i trial in healthy adults
    • Talaat, K. R. et al. A live attenuated H7N3 influenza virus vaccine is well tolerated and immunogenic in a phase I trial in healthy adults. Vaccine 27, 3744-3753 (2009).
    • (2009) Vaccine , vol.27 , pp. 3744-3753
    • Talaat, K.R.1
  • 67
    • 79954611107 scopus 로고    scopus 로고
    • An open label phase i trial of a live attenuated H6N1 influenza virus vaccine in healthy adults
    • Talaat, K. R. et al. An open label phase I trial of a live attenuated H6N1 influenza virus vaccine in healthy adults. Vaccine 29, 3144-3148 (2011).
    • (2011) Vaccine , vol.29 , pp. 3144-3148
    • Talaat, K.R.1
  • 68
    • 84871397055 scopus 로고    scopus 로고
    • An open-label phase i trial of a live attenuated H2N2 influenza virus vaccine in healthy adults
    • Talaat, K. R. et al. An open-label phase I trial of a live attenuated H2N2 influenza virus vaccine in healthy adults. Influenza Other Respir. Viruses 7, 66-73 (2013).
    • (2013) Influenza Other Respir. Viruses , vol.7 , pp. 66-73
    • Talaat, K.R.1
  • 69
    • 84895735598 scopus 로고    scopus 로고
    • Assessment of human immune responses to H7 avian influenza virus of pandemic potential: Results from a placebo-controlled, randomized double-blind phase i study of live attenuated H7N3 influenza vaccine
    • Rudenko, L. et al. Assessment of human immune responses to H7 avian influenza virus of pandemic potential: results from a placebo-controlled, randomized double-blind phase I study of live attenuated H7N3 influenza vaccine. PLoS ONE 9, e87962 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e87962
    • Rudenko, L.1
  • 70
    • 84884184553 scopus 로고    scopus 로고
    • H7N3 live attenuated influenza vaccine has a potential to protect against new H7N9 avian influenza virus
    • Rudenko, L., Isakova-Sivak, I. & Donina, S. H7N3 live attenuated influenza vaccine has a potential to protect against new H7N9 avian influenza virus. Vaccine 31, 4702-4705 (2013).
    • (2013) Vaccine , vol.31 , pp. 4702-4705
    • Rudenko, L.1    Isakova-Sivak, I.2    Donina, S.3
  • 71
    • 58149340056 scopus 로고    scopus 로고
    • Safety and immunogenicity of live attenuated influenza reassortant H5 vaccine (phase I-II clinical trials)
    • Rudenko, L. et al. Safety and immunogenicity of live attenuated influenza reassortant H5 vaccine (phase I-II clinical trials). Influenza Other Respir. Viruses 2, 203-209 (2008).
    • (2008) Influenza Other Respir. Viruses , vol.2 , pp. 203-209
    • Rudenko, L.1
  • 72
    • 84904658491 scopus 로고    scopus 로고
    • African green monkeys recapitulate the clinical experience with replication of live attenuated pandemic influenza virus vaccine candidates
    • Matsuoka, Y. et al. African green monkeys recapitulate the clinical experience with replication of live attenuated pandemic influenza virus vaccine candidates. J. Virol. 88, 8139-8152 (2014).
    • (2014) J. Virol. , vol.88 , pp. 8139-8152
    • Matsuoka, Y.1
  • 73
    • 78049489965 scopus 로고    scopus 로고
    • A live attenuated H7N7 candidate vaccine virus induces neutralizing antibody that confers protection from challenge in mice, ferrets, and monkeys
    • Min, J. Y. et al. A live attenuated H7N7 candidate vaccine virus induces neutralizing antibody that confers protection from challenge in mice, ferrets, and monkeys. J. Virol. 84, 11950-11960 (2010).
    • (2010) J. Virol. , vol.84 , pp. 11950-11960
    • Min, J.Y.1
  • 74
    • 59649084891 scopus 로고    scopus 로고
    • Live attenuated influenza viruses containing NS1 truncations as vaccine candidates against H5N1 highly pathogenic avian influenza
    • Steel, J. et al. Live attenuated influenza viruses containing NS1 truncations as vaccine candidates against H5N1 highly pathogenic avian influenza. J. Virol. 83, 1742-1753 (2009).
    • (2009) J. Virol. , vol.83 , pp. 1742-1753
    • Steel, J.1
  • 75
    • 84898877763 scopus 로고    scopus 로고
    • Role of receptor binding specificity in influenza A virus transmission and pathogenesis
    • de Graaf, M. & Fouchier, R. A. Role of receptor binding specificity in influenza A virus transmission and pathogenesis. EMBO J. 33, 823-841 (2014).
    • (2014) EMBO J. , vol.33 , pp. 823-841
    • De Graaf, M.1    Fouchier, R.A.2
  • 76
    • 84880191764 scopus 로고    scopus 로고
    • Prime-boost interval matters: A randomized phase 1 study to identify the minimum interval necessary to observe the H5 DNA influenza vaccine priming effect
    • Ledgerwood, J. E. et al. Prime-boost interval matters: a randomized phase 1 study to identify the minimum interval necessary to observe the H5 DNA influenza vaccine priming effect. J. Infect. Dis. 208, 418-422 (2013).
    • (2013) J. Infect. Dis. , vol.208 , pp. 418-422
    • Ledgerwood, J.E.1
  • 77
    • 84901753162 scopus 로고    scopus 로고
    • A live attenuated influenza A(H5N1) vaccine induces long-term immunity in the absence of a primary antibody response
    • Talaat, K. R. et al. A live attenuated influenza A(H5N1) vaccine induces long-term immunity in the absence of a primary antibody response. J. Infect. Dis. 209, 1860-1869 (2014).
    • (2014) J. Infect. Dis. , vol.209 , pp. 1860-1869
    • Talaat, K.R.1
  • 78
    • 84902346773 scopus 로고    scopus 로고
    • Improving pandemic H5N1 influenza vaccines by combining different vaccine platforms
    • Luke, C. J. & Subbarao, K. Improving pandemic H5N1 influenza vaccines by combining different vaccine platforms. Expert Rev. Vaccines 13, 873-883 (2014).
    • (2014) Expert Rev. Vaccines , vol.13 , pp. 873-883
    • Luke, C.J.1    Subbarao, K.2
  • 79
    • 0032078697 scopus 로고    scopus 로고
    • Development of a mammalian cell (Vero) derived candidate influenza virus vaccine
    • Kistner, O. et al. Development of a mammalian cell (Vero) derived candidate influenza virus vaccine. Vaccine 16, 960-968 (1998).
    • (1998) Vaccine , vol.16 , pp. 960-968
    • Kistner, O.1
  • 80
    • 84921676353 scopus 로고    scopus 로고
    • Rapid production of synthetic influenza vaccines
    • Dormitzer, P. R. Rapid production of synthetic influenza vaccines. Curr. Top. Microbiol. Immunol. 386, 237-273 (2015).
    • (2015) Curr. Top. Microbiol. Immunol. , vol.386 , pp. 237-273
    • Dormitzer, P.R.1
  • 81
    • 0032844790 scopus 로고    scopus 로고
    • Rescue of influenza A virus from recombinant DNA
    • Fodor, E. et al. Rescue of influenza A virus from recombinant DNA. J. Virol. 73, 9679-9682 (1999).
    • (1999) J. Virol. , vol.73 , pp. 9679-9682
    • Fodor, E.1
  • 82
    • 84857455818 scopus 로고    scopus 로고
    • Recombinant protein vaccines produced in insect cells
    • Cox, M. M. Recombinant protein vaccines produced in insect cells. Vaccine 30, 1759-1766 (2012).
    • (2012) Vaccine , vol.30 , pp. 1759-1766
    • Cox, M.M.1
  • 83
    • 77954385193 scopus 로고    scopus 로고
    • Alternative influenza vaccines made by insect cells
    • Krammer, F. & Grabherr, R. Alternative influenza vaccines made by insect cells. Trends Mol. Med. 16, 313-320 (2010).
    • (2010) Trends Mol. Med. , vol.16 , pp. 313-320
    • Krammer, F.1    Grabherr, R.2
  • 84
    • 84863645839 scopus 로고    scopus 로고
    • The human potential of a recombinant pandemic influenza vaccine produced in tobacco plants
    • Jul-Larsen, A. et al. The human potential of a recombinant pandemic influenza vaccine produced in tobacco plants. Hum. Vaccin. Immunother. 8, 653-661 (2012).
    • (2012) Hum. Vaccin. Immunother. , vol.8 , pp. 653-661
    • Jul-Larsen, A.1
  • 85
    • 77955355550 scopus 로고    scopus 로고
    • An influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli
    • Aguilar-Yáñez, J. M. et al. An influenza A/H1N1/2009 hemagglutinin vaccine produced in Escherichia coli. PLoS ONE 5, e11694 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e11694
    • Aguilar-Yáñez, J.M.1
  • 86
    • 84864945063 scopus 로고    scopus 로고
    • Development of VAX128, a recombinant hemagglutinin (HA) influenza-flagellin fusion vaccine with improved safety and immune response
    • Taylor, D. N. et al. Development of VAX128, a recombinant hemagglutinin (HA) influenza-flagellin fusion vaccine with improved safety and immune response. Vaccine 30, 5761-5769 (2012).
    • (2012) Vaccine , vol.30 , pp. 5761-5769
    • Taylor, D.N.1
  • 87
    • 84922391655 scopus 로고    scopus 로고
    • Immunoprotection against influenza virus H9N2 by the oral administration of recombinant Lactobacillus plantarumNC8 expressing hemagglutinin in BALB/c mice
    • Shi, S. H. et al. Immunoprotection against influenza virus H9N2 by the oral administration of recombinant Lactobacillus plantarumNC8 expressing hemagglutinin in BALB/c mice. Virology 464-465, 166-176 (2014).
    • (2014) Virology , vol.464-465 , pp. 166-176
    • Shi, S.H.1
  • 88
    • 84876573743 scopus 로고    scopus 로고
    • Vaccination against influenza with recombinant hemagglutinin expressed by Schizochytrium sp. Confers protective immunity
    • Bayne, A. C. et al. Vaccination against influenza with recombinant hemagglutinin expressed by Schizochytrium sp. confers protective immunity. PLoS ONE 8, e61790 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e61790
    • Bayne, A.C.1
  • 89
    • 0033557773 scopus 로고    scopus 로고
    • Protection of mice against a lethal influenza virus challenge after immunization with yeast-derived secreted influenza virus hemagglutinin
    • Saelens, X. et al. Protection of mice against a lethal influenza virus challenge after immunization with yeast-derived secreted influenza virus hemagglutinin. Eur. J. Biochem. 260, 166-175 (1999).
    • (1999) Eur. J. Biochem. , vol.260 , pp. 166-175
    • Saelens, X.1
  • 90
    • 84871797768 scopus 로고    scopus 로고
    • Recombinant haemagglutinin protein of highly pathogenic avian influenza A (H5N1) virus expressed in Pichia pastoris elicits a neutralizing antibody response in mice
    • Murugan, S. et al. Recombinant haemagglutinin protein of highly pathogenic avian influenza A (H5N1) virus expressed in Pichia pastoris elicits a neutralizing antibody response in mice. J. Virol. Methods 187, 20-25 (2013).
    • (2013) J. Virol. Methods , vol.187 , pp. 20-25
    • Murugan, S.1
  • 91
    • 84868091682 scopus 로고    scopus 로고
    • Cell-free production of trimeric influenza hemagglutinin head domain proteins as vaccine antigens
    • Welsh, J. P., Lu, Y., He, X. S., Greenberg, H. B. & Swartz, J. R. Cell-free production of trimeric influenza hemagglutinin head domain proteins as vaccine antigens. Biotechnol. Bioeng. 109, 2962-2969 (2012).
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 2962-2969
    • Welsh, J.P.1    Lu, Y.2    He, X.S.3    Greenberg, H.B.4    Swartz, J.R.5
  • 92
    • 78650667397 scopus 로고    scopus 로고
    • The receptor-binding domain of influenza virus hemagglutinin produced in Escherichia coli folds into its native, immunogenic structure
    • DuBois, R. M. et al. The receptor-binding domain of influenza virus hemagglutinin produced in Escherichia coli folds into its native, immunogenic structure. J. Virol. 85, 865-872 (2011).
    • (2011) J. Virol. , vol.85 , pp. 865-872
    • Dubois, R.M.1
  • 93
    • 80055113889 scopus 로고    scopus 로고
    • H5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies in humans that preferentially bind to oligomeric form of influenza hemagglutinin
    • Khurana, S. et al. H5N1 virus-like particle vaccine elicits cross-reactive neutralizing antibodies in humans that preferentially bind to oligomeric form of influenza hemagglutinin. J. Virol. 85, 10945-10954 (2011).
    • (2011) J. Virol. , vol.85 , pp. 10945-10954
    • Khurana, S.1
  • 94
    • 80053606312 scopus 로고    scopus 로고
    • Safety and immunogenicity of a virus-like particle pandemic influenza A (H1N1) 2009 vaccine in a blinded, randomized, placebo-controlled trial of adults in Mexico
    • López-Mac?as, C. et al. Safety and immunogenicity of a virus-like particle pandemic influenza A (H1N1) 2009 vaccine in a blinded, randomized, placebo-controlled trial of adults in Mexico. Vaccine 29, 7826-7834 (2011).
    • (2011) Vaccine , vol.29 , pp. 7826-7834
    • López-Macas, C.1
  • 95
    • 75649139519 scopus 로고    scopus 로고
    • Swine-origin pandemic H1N1 influenza virus-like particles produced in insect cells induce hemagglutination inhibiting antibodies in BALB/c mice
    • Krammer, F. et al. Swine-origin pandemic H1N1 influenza virus-like particles produced in insect cells induce hemagglutination inhibiting antibodies in BALB/c mice. Biotechnol. J. 5, 17-23 (2010).
    • (2010) Biotechnol. J. , vol.5 , pp. 17-23
    • Krammer, F.1
  • 96
    • 84882874443 scopus 로고    scopus 로고
    • Development of influenza H7N9 virus like particle (VLP) vaccine: Homologous A/Anhui/1/2013 (H7N9) protection and heterologous A/chicken/Jalisco/CPA1/2012 (H7N3) cross-protection in vaccinated mice challenged with H7N9 virus
    • Smith, G. E. et al. Development of influenza H7N9 virus like particle (VLP) vaccine: homologous A/Anhui/1/2013 (H7N9) protection and heterologous A/chicken/Jalisco/CPA1/2012 (H7N3) cross-protection in vaccinated mice challenged with H7N9 virus. Vaccine 31, 4305-4313 (2013).
    • (2013) Vaccine , vol.31 , pp. 4305-4313
    • Smith, G.E.1
  • 97
    • 84891014819 scopus 로고    scopus 로고
    • One-shot vaccination with an insect cell-derived low-dose influenza A H7 virus-like particle preparation protects mice against H7N9 challenge
    • Klausberger, M. et al. One-shot vaccination with an insect cell-derived low-dose influenza A H7 virus-like particle preparation protects mice against H7N9 challenge. Vaccine 32, 355-362 (2014).
    • (2014) Vaccine , vol.32 , pp. 355-362
    • Klausberger, M.1
  • 98
    • 84870918223 scopus 로고    scopus 로고
    • Residual baculovirus in insect cell-derived influenza virus-like particle preparations enhances immunogenicity
    • Margine, I., Martinez-Gil, L., Chou, Y. Y. & Krammer, F. Residual baculovirus in insect cell-derived influenza virus-like particle preparations enhances immunogenicity. PLoS ONE 7, e51559 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e51559
    • Margine, I.1    Martinez-Gil, L.2    Chou, Y.Y.3    Krammer, F.4
  • 99
    • 55949124182 scopus 로고    scopus 로고
    • Influenza virus-like particles produced by transient expression in Nicotiana benthamiana induce a protective immune response against a lethal viral challenge in mice
    • D'Aoust, M. et al. Influenza virus-like particles produced by transient expression in Nicotiana benthamiana induce a protective immune response against a lethal viral challenge in mice. Plant Biotechnol. J. 6, 930-940 (2008).
    • (2008) Plant Biotechnol. J. , vol.6 , pp. 930-940
    • D'Aoust, M.1
  • 100
    • 77953964469 scopus 로고    scopus 로고
    • The production of hemagglutinin-based virus-like particles in plants: A rapid, efficient and safe response to pandemic influenza
    • D'Aoust, M. A. et al. The production of hemagglutinin-based virus-like particles in plants: a rapid, efficient and safe response to pandemic influenza. Plant Biotechnol. J. 8, 607-619 (2010).
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 607-619
    • D'Aoust, M.A.1
  • 101
    • 84890932195 scopus 로고    scopus 로고
    • A recombinant viruslike particle influenza A (H7N9) vaccine
    • Fries, L. F., Smith, G. E. & Glenn, G. M. A recombinant viruslike particle influenza A (H7N9) vaccine. N. Engl. J. Med. 369, 2564-2566 (2013).
    • (2013) N. Engl. J. Med. , vol.369 , pp. 2564-2566
    • Fries, L.F.1    Smith, G.E.2    Glenn, G.M.3
  • 102
    • 78650981716 scopus 로고    scopus 로고
    • Preclinical and clinical development of plant-made virus-like particle vaccine against avian H5N1 influenza
    • Landry, N. et al. Preclinical and clinical development of plant-made virus-like particle vaccine against avian H5N1 influenza. PLoS ONE 5, e15559 (2010).
    • (2010) PLoS ONE , vol.5 , pp. e15559
    • Landry, N.1
  • 103
    • 84868217771 scopus 로고    scopus 로고
    • Influenza virus H5 DNA vaccination is immunogenic by intramuscular and intradermal routes in humans
    • Ledgerwood, J. E. et al. Influenza virus H5 DNA vaccination is immunogenic by intramuscular and intradermal routes in humans. Clin. Vaccine Immunol. 19, 1792-1797 (2012).
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 1792-1797
    • Ledgerwood, J.E.1
  • 104
    • 84905915216 scopus 로고    scopus 로고
    • Virus-vectored influenza virus vaccines
    • Tripp, R. A. & Tompkins, S. M. Virus-vectored influenza virus vaccines. Viruses 6, 3055-3079 (2014).
    • (2014) Viruses , vol.6 , pp. 3055-3079
    • Tripp, R.A.1    Tompkins, S.M.2
  • 105
    • 65449126737 scopus 로고    scopus 로고
    • Candidate influenza vaccines based on recombinant modified vaccinia virus Ankara
    • Rimmelzwaan, G. F. & Sutter, G. Candidate influenza vaccines based on recombinant modified vaccinia virus Ankara. Expert Rev. Vaccines 8, 447-454 (2009).
    • (2009) Expert Rev. Vaccines , vol.8 , pp. 447-454
    • Rimmelzwaan, G.F.1    Sutter, G.2
  • 106
    • 78049375271 scopus 로고    scopus 로고
    • Evaluation of a modified vaccinia virus Ankara (MVA)-based candidate pandemic influenza A/H1N1 vaccine in the ferret model
    • Kreijtz, J. H. et al. Evaluation of a modified vaccinia virus Ankara (MVA)-based candidate pandemic influenza A/H1N1 vaccine in the ferret model. J. Gen. Virol. 91, 2745-2752 (2010).
    • (2010) J. Gen. Virol. , vol.91 , pp. 2745-2752
    • Kreijtz, J.H.1
  • 107
    • 84904567659 scopus 로고    scopus 로고
    • Modified vaccinia virus Ankara (MVA) as production platform for vaccines against influenza and other viral respiratory diseases
    • Altenburg, A. F. et al. Modified vaccinia virus Ankara (MVA) as production platform for vaccines against influenza and other viral respiratory diseases. Viruses 6, 2735-2761 (2014).
    • (2014) Viruses , vol.6 , pp. 2735-2761
    • Altenburg, A.F.1
  • 108
    • 58849152275 scopus 로고    scopus 로고
    • Recombinant modified vaccinia virus Ankara expressing the hemagglutinin gene confers protection against homologous and heterologous H5N1 influenza virus infections in macaques
    • Kreijtz, J. H. et al. Recombinant modified vaccinia virus Ankara expressing the hemagglutinin gene confers protection against homologous and heterologous H5N1 influenza virus infections in macaques. J. Infect. Dis. 199, 405-413 (2009).
    • (2009) J. Infect. Dis. , vol.199 , pp. 405-413
    • Kreijtz, J.H.1
  • 109
    • 84925757182 scopus 로고    scopus 로고
    • A single immunization with an MVA-based influenza virus H7 vaccine affords protection in the H7N9 pneumonia ferret model
    • Kreijtz, J. H. et al. A single immunization with an MVA-based influenza virus H7 vaccine affords protection in the H7N9 pneumonia ferret model. J. Infect. Dis. http://dx.doi.org/10.1093/infdis/jiu528 (2014).
    • (2014) J. Infect. Dis.
    • Kreijtz, J.H.1
  • 110
    • 84907211149 scopus 로고    scopus 로고
    • Progress toward a universal H5N1 vaccine: A recombinant modified vaccinia virus Ankara-expressing trivalent hemagglutinin vaccine
    • Prabakaran, M. et al. Progress toward a universal H5N1 vaccine: a recombinant modified vaccinia virus Ankara-expressing trivalent hemagglutinin vaccine. PLoS ONE 9, e107316 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e107316
    • Prabakaran, M.1
  • 111
    • 84921462712 scopus 로고    scopus 로고
    • Safety and immunogenicity of a modified-vaccinia-virus-Ankara-based influenza A H5N1 vaccine: A randomised, double-blind phase 1/2a clinical trial
    • Kreijtz, J. H. et al. Safety and immunogenicity of a modified-vaccinia-virus-Ankara-based influenza A H5N1 vaccine: a randomised, double-blind phase 1/2a clinical trial. Lancet Infect. Dis. 14, 1196-1207 (2014).
    • (2014) Lancet Infect. Dis. , vol.14 , pp. 1196-1207
    • Kreijtz, J.H.1
  • 112
    • 78651488739 scopus 로고    scopus 로고
    • Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection
    • Wrammert, J. et al. Broadly cross-reactive antibodies dominate the human B cell response against 2009 pandemic H1N1 influenza virus infection. J. Exp. Med. 208, 181-193 (2011).
    • (2011) J. Exp. Med. , vol.208 , pp. 181-193
    • Wrammert, J.1
  • 113
    • 44449118948 scopus 로고    scopus 로고
    • Rapid cloning of high-affinity human monoclonal antibodies against influenza virus
    • Wrammert, J. et al. Rapid cloning of high-affinity human monoclonal antibodies against influenza virus. Nature 453, 667-671 (2008).
    • (2008) Nature , vol.453 , pp. 667-671
    • Wrammert, J.1
  • 114
    • 80054780343 scopus 로고    scopus 로고
    • H3N2 influenza infection elicits more cross-reactive and less clonally expanded anti-hemagglutinin antibodies than influenza vaccination
    • Moody, M. A. et al. H3N2 influenza infection elicits more cross-reactive and less clonally expanded anti-hemagglutinin antibodies than influenza vaccination. PLoS ONE 6, e25797 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e25797
    • Moody, M.A.1
  • 115
    • 58049198443 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells
    • Throsby, M. et al. Heterosubtypic neutralizing monoclonal antibodies cross-protective against H5N1 and H1N1 recovered from human IgM+ memory B cells. PLoS ONE 3, e3942 (2008).
    • (2008) PLoS ONE , vol.3 , pp. e3942
    • Throsby, M.1
  • 116
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • Sui, J. et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nature Struct. Mol. Biol. 16, 265-273 (2009).
    • (2009) Nature Struct. Mol. Biol. , vol.16 , pp. 265-273
    • Sui, J.1
  • 117
    • 77951876927 scopus 로고    scopus 로고
    • Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine
    • Corti, D. et al. Heterosubtypic neutralizing antibodies are produced by individuals immunized with a seasonal influenza vaccine. J. Clin. Invest. 120, 1663-1673 (2010).
    • (2010) J. Clin. Invest. , vol.120 , pp. 1663-1673
    • Corti, D.1
  • 118
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno, Y., Isegawa, Y., Sasao, F. & Ueda, S. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67, 2552-2558 (1993).
    • (1993) J. Virol. , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 119
    • 43149109969 scopus 로고    scopus 로고
    • Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies
    • Kashyap, A. K. et al. Combinatorial antibody libraries from survivors of the Turkish H5N1 avian influenza outbreak reveal virus neutralization strategies. Proc. Natl Acad. Sci. USA 105, 5986-5991 (2008).
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 5986-5991
    • Kashyap, A.K.1
  • 120
    • 84881237033 scopus 로고    scopus 로고
    • Molecular basis for broad neuraminidase immunity: Conserved epitopes in seasonal and pandemic H1N1 as well as H5N1 influenza viruses
    • Wan, H. et al. Molecular basis for broad neuraminidase immunity: conserved epitopes in seasonal and pandemic H1N1 as well as H5N1 influenza viruses. J. Virol. 87, 9290-9300 (2013).
    • (2013) J. Virol. , vol.87 , pp. 9290-9300
    • Wan, H.1
  • 121
    • 80053474133 scopus 로고    scopus 로고
    • A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin
    • Krause, J. C. et al. A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin. J. Virol. 85, 10905-10908 (2011).
    • (2011) J. Virol. , vol.85 , pp. 10905-10908
    • Krause, J.C.1
  • 122
    • 84863568230 scopus 로고    scopus 로고
    • Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses
    • Krause, J. C. et al. Human monoclonal antibodies to pandemic 1957 H2N2 and pandemic 1968 H3N2 influenza viruses. J. Virol. 86, 6334-6340 (2012).
    • (2012) J. Virol. , vol.86 , pp. 6334-6340
    • Krause, J.C.1
  • 123
    • 84866953140 scopus 로고    scopus 로고
    • Cross-neutralization of influenza A viruses mediated by a single antibody loop
    • Ekiert, D. C. et al. Cross-neutralization of influenza A viruses mediated by a single antibody loop. Nature 489, 526-532 (2012).
    • (2012) Nature , vol.489 , pp. 526-532
    • Ekiert, D.C.1
  • 124
    • 80052184942 scopus 로고    scopus 로고
    • Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin
    • Whittle, J. R. et al. Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc. Natl Acad. Sci. USA 108, 14216-14221 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 14216-14221
    • Whittle, J.R.1
  • 125
    • 80055111172 scopus 로고    scopus 로고
    • Naturally occurring antibodies in a human can neutralize a broad spectrum of influenza strains including H3, H1, H2 and H5
    • Ohshima, N. et al. Naturally occurring antibodies in a human can neutralize a broad spectrum of influenza strains including H3, H1, H2 and H5. J. Virol. 85, 11048-11057 (2011).
    • (2011) J. Virol. , vol.85 , pp. 11048-11057
    • Ohshima, N.1
  • 126
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • Ekiert, D. C. et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324, 246-251 (2009).
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 127
    • 84891910969 scopus 로고    scopus 로고
    • A common solution to group 2 influenza virus neutralization
    • Friesen, R. H. et al. A common solution to group 2 influenza virus neutralization. Proc. Natl Acad. Sci. USA 111, 445-450 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 445-450
    • Friesen, R.H.1
  • 128
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • Ekiert, D. C. et al. A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333, 843-850 (2011).
    • (2011) Science , vol.333 , pp. 843-850
    • Ekiert, D.C.1
  • 129
    • 84911434712 scopus 로고    scopus 로고
    • Characterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin
    • Tan, G. S. et al. Characterization of a broadly neutralizing monoclonal antibody that targets the fusion domain of group 2 influenza A virus hemagglutinin. J. Virol. 88, 13580-13592 (2014).
    • (2014) J. Virol. , vol.88 , pp. 13580-13592
    • Tan, G.S.1
  • 130
    • 84863597077 scopus 로고    scopus 로고
    • A pan-h1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo
    • Tan, G. S. et al. A pan-h1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo. J. Virol. 86, 6179-6188 (2012).
    • (2012) J. Virol. , vol.86 , pp. 6179-6188
    • Tan, G.S.1
  • 131
    • 77649242815 scopus 로고    scopus 로고
    • Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins
    • Wang, T. T. et al. Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins. PLoS Pathog. 6, e1000796 (2010).
    • (2010) PLoS Pathog. , vol.6 , pp. e1000796
    • Wang, T.T.1
  • 132
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • Dreyfus, C. et al. Highly conserved protective epitopes on influenza B viruses. Science 337, 1343-1348 (2012).
    • (2012) Science , vol.337 , pp. 1343-1348
    • Dreyfus, C.1
  • 133
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti, D. et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856 (2011).
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 134
    • 84880427552 scopus 로고    scopus 로고
    • An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies
    • Nakamura, G. et al. An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies. Cell Host Microbe 14, 93-103 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 93-103
    • Nakamura, G.1
  • 135
    • 84865289490 scopus 로고    scopus 로고
    • A carboxy-terminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates
    • Krammer, F. et al. A carboxy-terminal trimerization domain stabilizes conformational epitopes on the stalk domain of soluble recombinant hemagglutinin substrates. PLoS ONE 7, e43603 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e43603
    • Krammer, F.1
  • 136
    • 84875236527 scopus 로고    scopus 로고
    • Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies
    • Harris, A. K. et al. Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodies. Proc. Natl Acad. Sci. USA 110, 4592-4597 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 4592-4597
    • Harris, A.K.1
  • 137
    • 84892615764 scopus 로고    scopus 로고
    • Mechanisms of hemagglutinin targeted influenza virus neutralization
    • Brandenburg, B. et al. Mechanisms of hemagglutinin targeted influenza virus neutralization. PLoS ONE 8, e80034 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e80034
    • Brandenburg, B.1
  • 138
    • 84862908804 scopus 로고    scopus 로고
    • Complement-dependent lysis of influenza A virus-infected cells by broadly cross-reactive human monoclonal antibodies
    • Terajima, M. et al. Complement-dependent lysis of influenza A virus-infected cells by broadly cross-reactive human monoclonal antibodies. J. Virol. 85, 13463-13467 (2011).
    • (2011) J. Virol. , vol.85 , pp. 13463-13467
    • Terajima, M.1
  • 139
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcγR interactions for protection against influenza virus in vivo
    • Dilillo, D. J., Tan, G. S., Palese, P. & Ravetch, J. V. Broadly neutralizing hemagglutinin stalk-specific antibodies require FcγR interactions for protection against influenza virus in vivo. Nature Med. 20, 143-151 (2014).
    • (2014) Nature Med. , vol.20 , pp. 143-151
    • Dilillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4
  • 140
    • 84877317499 scopus 로고    scopus 로고
    • Antibody-dependent cellular cytotoxicity is associated with control of pandemic H1N1 influenza virus infection of macaques
    • Jegaskanda, S., Weinfurter, J. T., Friedrich, T. C. & Kent, S. J. Antibody-dependent cellular cytotoxicity is associated with control of pandemic H1N1 influenza virus infection of macaques. J. Virol. 87, 5512-5522 (2013).
    • (2013) J. Virol. , vol.87 , pp. 5512-5522
    • Jegaskanda, S.1    Weinfurter, J.T.2    Friedrich, T.C.3    Kent, S.J.4
  • 141
    • 84873547392 scopus 로고    scopus 로고
    • Cross-reactive influenza-specific antibody-dependent cellular cytotoxicity antibodies in the absence of neutralizing antibodies
    • Jegaskanda, S. et al. Cross-reactive influenza-specific antibody-dependent cellular cytotoxicity antibodies in the absence of neutralizing antibodies. J. Immunol. 190, 1837-1848 (2013).
    • (2013) J. Immunol. , vol.190 , pp. 1837-1848
    • Jegaskanda, S.1
  • 142
    • 84904263611 scopus 로고    scopus 로고
    • Influenza-specific antibody-dependent cellular cytotoxicity: Toward a universal influenza vaccine
    • Jegaskanda, S., Reading, P. C. & Kent, S. J. Influenza-specific antibody-dependent cellular cytotoxicity: toward a universal influenza vaccine. J. Immunol. 193, 469-475 (2014).
    • (2014) J. Immunol. , vol.193 , pp. 469-475
    • Jegaskanda, S.1    Reading, P.C.2    Kent, S.J.3
  • 143
    • 84875776863 scopus 로고    scopus 로고
    • H3N2 influenza virus infection induces broadly reactive hemagglutinin stalk antibodies in humans and mice
    • Margine, I. et al. H3N2 influenza virus infection induces broadly reactive hemagglutinin stalk antibodies in humans and mice. J. Virol. 87, 4728-4737 (2013).
    • (2013) J. Virol. , vol.87 , pp. 4728-4737
    • Margine, I.1
  • 144
    • 84869059071 scopus 로고    scopus 로고
    • Hemagglutinin stalk-reactive antibodies are boosted following sequential infection with seasonal and pandemic H1N1 influenza virus in mice
    • Krammer, F., Pica, N., Hai, R., Tan, G. S. & Palese, P. Hemagglutinin stalk-reactive antibodies are boosted following sequential infection with seasonal and pandemic H1N1 influenza virus in mice. J. Virol. 86, 10302-10307 (2012).
    • (2012) J. Virol. , vol.86 , pp. 10302-10307
    • Krammer, F.1    Pica, N.2    Hai, R.3    Tan, G.S.4    Palese, P.5
  • 145
    • 84883856356 scopus 로고    scopus 로고
    • Neutralizing antibodies against previously encountered influenza virus strains increase over time: A longitudinal analysis
    • Miller, M. S. et al. Neutralizing antibodies against previously encountered influenza virus strains increase over time: a longitudinal analysis. Sci. Transl. Med. 5, 198ra107 (2013).
    • (2013) Sci. Transl Med. , vol.5 , pp. 198ra107
    • Miller, M.S.1
  • 146
    • 84863115945 scopus 로고    scopus 로고
    • Hemagglutinin stalk antibodies elicited by the 2009 pandemic influenza virus as a mechanism for the extinction of seasonal H1N1 viruses
    • Pica, N. et al. Hemagglutinin stalk antibodies elicited by the 2009 pandemic influenza virus as a mechanism for the extinction of seasonal H1N1 viruses. Proc. Natl Acad. Sci. USA 109, 2573-2578 (2012).
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 2573-2578
    • Pica, N.1
  • 147
    • 84864824020 scopus 로고    scopus 로고
    • Pandemic H1N1 influenza infection and vaccination in humans induces cross-protective antibodies that target the hemagglutinin stem
    • Thomson, C. A. et al. Pandemic H1N1 influenza infection and vaccination in humans induces cross-protective antibodies that target the hemagglutinin stem. Front. Immunol. 3, 87 (2012).
    • (2012) Front. Immunol. , vol.3 , pp. 87
    • Thomson, C.A.1
  • 148
    • 84872924387 scopus 로고    scopus 로고
    • 1976 and 2009 H1N1 influenza virus vaccines boost anti-hemagglutinin stalk antibodies in humans
    • Miller, M. S. et al. 1976 and 2009 H1N1 influenza virus vaccines boost anti-hemagglutinin stalk antibodies in humans. J. Infect. Dis. 207, 98-105 (2013).
    • (2013) J. Infect. Dis. , vol.207 , pp. 98-105
    • Miller, M.S.1
  • 149
    • 84891384401 scopus 로고    scopus 로고
    • B cell response and hemagglutinin stalk-reactive antibody production in different age cohorts following 2009 H1N1 influenza virus vaccination
    • Sangster, M. Y. et al. B cell response and hemagglutinin stalk-reactive antibody production in different age cohorts following 2009 H1N1 influenza virus vaccination. Clin. Vaccine Immunol. 20, 867-876 (2013).
    • (2013) Clin. Vaccine Immunol. , vol.20 , pp. 867-876
    • Sangster, M.Y.1
  • 150
    • 84896917279 scopus 로고    scopus 로고
    • Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages
    • Whittle, J. R. et al. Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages. J. Virol. 88, 4047-4057 (2014).
    • (2014) J. Virol. , vol.88 , pp. 4047-4057
    • Whittle, J.R.1
  • 151
    • 84907327243 scopus 로고    scopus 로고
    • Challenges of selecting seasonal influenza vaccine strains for humans with diverse pre-exposure histories
    • Hensley, S. E. Challenges of selecting seasonal influenza vaccine strains for humans with diverse pre-exposure histories. Curr. Opin. Virol. 8, 85-89 (2014).
    • (2014) Curr. Opin. Virol. , vol.8 , pp. 85-89
    • Hensley, S.E.1
  • 152
    • 84884238986 scopus 로고    scopus 로고
    • Immune history shapes specificity of pandemic H1N1 influenza antibody responses
    • Li, Y. et al. Immune history shapes specificity of pandemic H1N1 influenza antibody responses. J. Exp. Med. 210, 1493-1500 (2013).
    • (2013) J. Exp. Med. , vol.210 , pp. 1493-1500
    • Li, Y.1
  • 153
    • 84903131264 scopus 로고    scopus 로고
    • In the shadow of hemagglutinin: A growing interest in influenza viral neuraminidase and its role as a vaccine antigen
    • Wohlbold, T. J. & Krammer, F. In the shadow of hemagglutinin: a growing interest in influenza viral neuraminidase and its role as a vaccine antigen. Viruses 6, 2465-2494 (2014).
    • (2014) Viruses , vol.6 , pp. 2465-2494
    • Wohlbold, T.J.1    Krammer, F.2
  • 154
    • 84887477456 scopus 로고    scopus 로고
    • A monoclonal antibody targeting a highly conserved epitope in influenza B neuraminidase provides protection against drug resistant strains
    • Doyle, T. M. et al. A monoclonal antibody targeting a highly conserved epitope in influenza B neuraminidase provides protection against drug resistant strains. Biochem. Biophys. Res. Commun. 441, 226-229 (2013).
    • (2013) Biochem. Biophys. Res. Commun. , vol.441 , pp. 226-229
    • Doyle, T.M.1
  • 155
    • 84886079382 scopus 로고    scopus 로고
    • Universal anti-neuraminidase antibody inhibiting all influenza A subtypes
    • Doyle, T. M. et al. Universal anti-neuraminidase antibody inhibiting all influenza A subtypes. Antiviral Res. 100, 567-574 (2013).
    • (2013) Antiviral Res. , vol.100 , pp. 567-574
    • Doyle, T.M.1
  • 156
    • 84897878395 scopus 로고    scopus 로고
    • Playing hide and seek: How glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection
    • Tate, M. D. et al. Playing hide and seek: how glycosylation of the influenza virus hemagglutinin can modulate the immune response to infection. Viruses 6, 1294-1316 (2014).
    • (2014) Viruses , vol.6 , pp. 1294-1316
    • Tate, M.D.1
  • 157
    • 84880558705 scopus 로고    scopus 로고
    • Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza viruses
    • Medina, R. A. et al. Glycosylations in the globular head of the hemagglutinin protein modulate the virulence and antigenic properties of the H1N1 influenza viruses. Sci. Transl. Med. 5, 187ra70 (2013).
    • (2013) Sci. Transl Med. , vol.5 , pp. 187ra70
    • Medina, R.A.1
  • 158
    • 70849114731 scopus 로고    scopus 로고
    • Glycans on influenza hemagglutinin affect receptor binding and immune response
    • Wang, C. C. et al. Glycans on influenza hemagglutinin affect receptor binding and immune response. Proc. Natl Acad. Sci. USA 106, 18137-18142 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 18137-18142
    • Wang, C.C.1
  • 159
    • 84894305002 scopus 로고    scopus 로고
    • Vaccination of monoglycosylated hemagglutinin induces cross-strain protection against influenza virus infections
    • Chen, J. R. et al. Vaccination of monoglycosylated hemagglutinin induces cross-strain protection against influenza virus infections. Proc. Natl Acad. Sci. USA 111, 2476-2481 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 2476-2481
    • Chen, J.R.1
  • 160
    • 84903455358 scopus 로고    scopus 로고
    • Biogenesis of influenza A virus hemagglutinin cross-protective stem epitopes
    • Magadán, J. G. et al. Biogenesis of influenza A virus hemagglutinin cross-protective stem epitopes. PLoS Pathog. 10, e1004204 (2014).
    • (2014) PLoS Pathog. , vol.10 , pp. e1004204
    • Magadán, J.G.1
  • 161
    • 84881141968 scopus 로고    scopus 로고
    • Comparative glycomics analysis of influenza hemagglutinin (H5N1) produced in vaccine relevant cell platforms
    • An, Y. et al. Comparative glycomics analysis of influenza hemagglutinin (H5N1) produced in vaccine relevant cell platforms. J. Proteome Res. 12, 3707-3720 (2013).
    • (2013) J. Proteome Res. , vol.12 , pp. 3707-3720
    • An, Y.1
  • 162
    • 84906948184 scopus 로고    scopus 로고
    • Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy
    • Palmberger, D., Ashjaei, K., Strell, S., Hoffmann-Sommergruber, K. & Grabherr, R. Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy. Biotechnol. J. 9, 1206-1214 (2014).
    • (2014) Biotechnol. J. , vol.9 , pp. 1206-1214
    • Palmberger, D.1    Ashjaei, K.2    Strell, S.3    Hoffmann-Sommergruber, K.4    Grabherr, R.5
  • 163
    • 84890874733 scopus 로고    scopus 로고
    • Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain
    • Eggink, D., Goff, P. H. & Palese, P. Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain. J. Virol. 88, 699-704 (2014).
    • (2014) J. Virol. , vol.88 , pp. 699-704
    • Eggink, D.1    Goff, P.H.2    Palese, P.3
  • 164
    • 84862220814 scopus 로고    scopus 로고
    • Broader neutralizing antibodies against H5N1 viruses using prime-boost immunization of hyperglycosylated hemagglutinin DNA and virus-like particles
    • Lin, S. C., Lin, Y. F., Chong, P. & Wu, S. C. Broader neutralizing antibodies against H5N1 viruses using prime-boost immunization of hyperglycosylated hemagglutinin DNA and virus-like particles. PLoS ONE 7, e39075 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e39075
    • Lin, S.C.1    Lin, Y.F.2    Chong, P.3    Wu, S.C.4
  • 165
    • 84899892665 scopus 로고    scopus 로고
    • Glycan masking of hemagglutinin for adenovirus vector and recombinant protein immunizations elicits broadly neutralizing antibodies against H5N1 avian influenza viruses
    • Lin, S. C., Liu, W. C., Jan, J. T. & Wu, S. C. Glycan masking of hemagglutinin for adenovirus vector and recombinant protein immunizations elicits broadly neutralizing antibodies against H5N1 avian influenza viruses. PLoS ONE 9, e92822 (2014).
    • (2014) PLoS ONE , vol.9 , pp. e92822
    • Lin, S.C.1    Liu, W.C.2    Jan, J.T.3    Wu, S.C.4
  • 166
    • 0020626189 scopus 로고
    • Preparation of influenza virus subviral particles lacking the HA1 subunit of hemagglutinin: Unmasking of cross-reactive HA2 determinants
    • Graves, P. N., Schulman, J. L., Young, J. F. & Palese, P. Preparation of influenza virus subviral particles lacking the HA1 subunit of hemagglutinin: unmasking of cross-reactive HA2 determinants. Virology 126, 106-116 (1983).
    • (1983) Virology , vol.126 , pp. 106-116
    • Graves, P.N.1    Schulman, J.L.2    Young, J.F.3    Palese, P.4
  • 167
    • 0030013837 scopus 로고    scopus 로고
    • The immunological activity of a deletion mutant of influenza virus haemagglutinin lacking the globular region
    • Sagawa, H., Ohshima, A., Kato, I., Okuno, Y. & Isegawa, Y. The immunological activity of a deletion mutant of influenza virus haemagglutinin lacking the globular region. J. Gen. Virol. 77, 1483-1487 (1996).
    • (1996) J. Gen. Virol. , vol.77 , pp. 1483-1487
    • Sagawa, H.1    Ohshima, A.2    Kato, I.3    Okuno, Y.4    Isegawa, Y.5
  • 168
    • 79952140653 scopus 로고    scopus 로고
    • Influenza virus vaccine based on the conserved hemagglutinin stalk domain
    • Steel, J. et al. Influenza virus vaccine based on the conserved hemagglutinin stalk domain. MBio 1, e00018-10 (2010).
    • (2010) MBio , vol.1 , pp. e00018-10
    • Steel, J.1
  • 169
    • 77956379133 scopus 로고    scopus 로고
    • Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge
    • Bommakanti, G. et al. Design of an HA2-based Escherichia coli expressed influenza immunogen that protects mice from pathogenic challenge. Proc. Natl Acad. Sci. USA 107, 13701-13706 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 13701-13706
    • Bommakanti, G.1
  • 170
    • 84870656355 scopus 로고    scopus 로고
    • Design of Escherichia coli-expressed stalk domain immunogens of H1N1 hemagglutinin that protect mice from lethal challenge
    • Bommakanti, G. et al. Design of Escherichia coli-expressed stalk domain immunogens of H1N1 hemagglutinin that protect mice from lethal challenge. J. Virol. 86, 13434-13444 (2012).
    • (2012) J. Virol. , vol.86 , pp. 13434-13444
    • Bommakanti, G.1
  • 171
    • 84903476533 scopus 로고    scopus 로고
    • Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection
    • Mallajosyula, V. V. et al. Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection. Proc. Natl Acad. Sci. USA 111, E2514-E2523 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. E2514-E2523
    • Mallajosyula, V.V.1
  • 172
    • 84891912497 scopus 로고    scopus 로고
    • Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines
    • Lu, Y., Welsh, J. P. & Swartz, J. R. Production and stabilization of the trimeric influenza hemagglutinin stem domain for potentially broadly protective influenza vaccines. Proc. Natl Acad. Sci. USA 111, 125-130 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 125-130
    • Lu, Y.1    Welsh, J.P.2    Swartz, J.R.3
  • 173
    • 84870382373 scopus 로고    scopus 로고
    • Heterosubtypic protection against influenza A induced by adenylate cyclase toxoids delivering conserved HA2 subunit of hemagglutinin
    • Staneková, Z. et al. Heterosubtypic protection against influenza A induced by adenylate cyclase toxoids delivering conserved HA2 subunit of hemagglutinin. Antiviral Res. 97, 24-35 (2013).
    • (2013) Antiviral Res. , vol.97 , pp. 24-35
    • Staneková, Z.1
  • 174
    • 65549111747 scopus 로고    scopus 로고
    • Broadly cross-reactive monoclonal antibodies against HA2 glycopeptide of influenza A virus hemagglutinin of H3 subtype reduce replication of influenza A viruses of human and avian origin
    • Stropkovská, A. et al. Broadly cross-reactive monoclonal antibodies against HA2 glycopeptide of influenza A virus hemagglutinin of H3 subtype reduce replication of influenza A viruses of human and avian origin. Acta Virol. 53, 15-20 (2009).
    • (2009) Acta Virol. , vol.53 , pp. 15-20
    • Stropkovská, A.1
  • 175
    • 84861325359 scopus 로고    scopus 로고
    • Influenza viruses expressing chimeric hemagglutinins: Globular head and stalk domains derived from different subtypes
    • Hai, R. et al. Influenza viruses expressing chimeric hemagglutinins: globular head and stalk domains derived from different subtypes. J. Virol. 86, 5774-5781 (2012).
    • (2012) J. Virol. , vol.86 , pp. 5774-5781
    • Hai, R.1
  • 176
    • 84885953445 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin stalk-based antibodies and vaccines
    • Krammer, F. & Palese, P. Influenza virus hemagglutinin stalk-based antibodies and vaccines. Curr. Opin. Virol. 3, 521-530 (2013).
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 521-530
    • Krammer, F.1    Palese, P.2
  • 177
    • 84896720073 scopus 로고    scopus 로고
    • Assessment of influenza virus hemagglutinin stalk-based immunity in ferrets
    • Krammer, F. et al. Assessment of influenza virus hemagglutinin stalk-based immunity in ferrets. J. Virol. 88, 3432-3442 (2014).
    • (2014) J. Virol. , vol.88 , pp. 3432-3442
    • Krammer, F.1
  • 178
    • 84878611784 scopus 로고    scopus 로고
    • Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies
    • Krammer, F., Pica, N., Hai, R., Margine, I. & Palese, P. Chimeric hemagglutinin influenza virus vaccine constructs elicit broadly protective stalk-specific antibodies. J. Virol. 87, 6542-6550 (2013).
    • (2013) J. Virol. , vol.87 , pp. 6542-6550
    • Krammer, F.1    Pica, N.2    Hai, R.3    Margine, I.4    Palese, P.5
  • 179
    • 84893496184 scopus 로고    scopus 로고
    • H3 stalk-based chimeric hemagglutinin influenza virus constructs protect mice from H7N9 challenge
    • Krammer, F. et al. H3 stalk-based chimeric hemagglutinin influenza virus constructs protect mice from H7N9 challenge. J. Virol. 88, 2340-2343 (2014).
    • (2014) J. Virol. , vol.88 , pp. 2340-2343
    • Krammer, F.1
  • 180
    • 84885950726 scopus 로고    scopus 로고
    • Hemagglutinin stalk-based universal vaccine constructs protect against group 2 influenza A viruses
    • Margine, I. et al. Hemagglutinin stalk-based universal vaccine constructs protect against group 2 influenza A viruses. J. Virol. 87, 10435-10446 (2013).
    • (2013) J. Virol. , vol.87 , pp. 10435-10446
    • Margine, I.1
  • 181
    • 84890554900 scopus 로고    scopus 로고
    • Adjuvants and immunization strategies to induce influenza virus hemagglutinin stalk antibodies
    • Goff, P. H. et al. Adjuvants and immunization strategies to induce influenza virus hemagglutinin stalk antibodies. PLoS ONE 8, e79194 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e79194
    • Goff, P.H.1
  • 182
    • 79953139384 scopus 로고    scopus 로고
    • Protection against divergent influenza H1N1 virus by a centralized influenza hemagglutinin
    • Weaver, E. A., Rubrum, A. M., Webby, R. J. & Barry, M. A. Protection against divergent influenza H1N1 virus by a centralized influenza hemagglutinin. PLoS ONE 6, e18314 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e18314
    • Weaver, E.A.1    Rubrum, A.M.2    Webby, R.J.3    Barry, M.A.4
  • 183
    • 84896019901 scopus 로고    scopus 로고
    • Eliciting broadly protective antibody responses against influenza
    • Kirchenbaum, G. A. & Ross, T. M. Eliciting broadly protective antibody responses against influenza. Curr. Opin. Immunol. 28, 71-76 (2014).
    • (2014) Curr. Opin. Immunol. , vol.28 , pp. 71-76
    • Kirchenbaum, G.A.1    Ross, T.M.2
  • 184
    • 78651097861 scopus 로고    scopus 로고
    • Feasibility of reconstructed ancestral H5N1 influenza viruses for cross-clade protective vaccine development
    • Ducatez, M. F. et al. Feasibility of reconstructed ancestral H5N1 influenza viruses for cross-clade protective vaccine development. Proc. Natl Acad. Sci. USA 108, 349-354 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 349-354
    • Ducatez, M.F.1
  • 185
    • 84859090933 scopus 로고    scopus 로고
    • Computationally optimized antigens to overcome influenza viral diversity
    • Giles, B. M. & Ross, T. M. Computationally optimized antigens to overcome influenza viral diversity. Expert Rev. Vaccines 11, 267-269 (2012).
    • (2012) Expert Rev. Vaccines , vol.11 , pp. 267-269
    • Giles, B.M.1    Ross, T.M.2
  • 186
    • 84856411125 scopus 로고    scopus 로고
    • Antibody breadth and protective efficacy are increased by vaccination with computationally optimized hemagglutinin but not with polyvalent hemagglutinin-based H5N1 virus-like particle vaccines
    • Giles, B. M., Bissel, S. J., Dealmeida, D. R., Wiley, C. A. & Ross, T. M. Antibody breadth and protective efficacy are increased by vaccination with computationally optimized hemagglutinin but not with polyvalent hemagglutinin-based H5N1 virus-like particle vaccines. Clin. Vaccine Immunol. 19, 128-139 (2012).
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 128-139
    • Giles, B.M.1    Bissel, S.J.2    Dealmeida, D.R.3    Wiley, C.A.4    Ross, T.M.5
  • 187
    • 79953244722 scopus 로고    scopus 로고
    • A computationally optimized broadly reactive antigen (COBRA) based H5N1 VLP vaccine elicits broadly reactive antibodies in mice and ferrets
    • Giles, B. M. & Ross, T. M. A computationally optimized broadly reactive antigen (COBRA) based H5N1 VLP vaccine elicits broadly reactive antibodies in mice and ferrets. Vaccine 29, 3043-3054 (2011).
    • (2011) Vaccine , vol.29 , pp. 3043-3054
    • Giles, B.M.1    Ross, T.M.2
  • 188
    • 84860380354 scopus 로고    scopus 로고
    • A computationally optimized hemagglutinin virus-like particle vaccine elicits broadly reactive antibodies that protect nonhuman primates from H5N1 infection
    • Giles, B. M. et al. A computationally optimized hemagglutinin virus-like particle vaccine elicits broadly reactive antibodies that protect nonhuman primates from H5N1 infection. J. Infect. Dis. 205, 1562-1570 (2012).
    • (2012) J. Infect. Dis. , vol.205 , pp. 1562-1570
    • Giles, B.M.1
  • 189
    • 0025124414 scopus 로고
    • Independent and disparate evolution in nature of influenza A virus hemagglutinin and neuraminidase glycoproteins
    • Kilbourne, E. D., Johansson, B. E. & Grajower, B. Independent and disparate evolution in nature of influenza A virus hemagglutinin and neuraminidase glycoproteins. Proc. Natl Acad. Sci. USA 87, 786-790 (1990).
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 786-790
    • Kilbourne, E.D.1    Johansson, B.E.2    Grajower, B.3
  • 190
    • 0036304688 scopus 로고    scopus 로고
    • Divergent evolution of hemagglutinin and neuraminidase genes in recent influenza A:H3N2 viruses isolated in Canada
    • Abed, Y., Hardy, I., Li, Y. & Boivin, G. Divergent evolution of hemagglutinin and neuraminidase genes in recent influenza A:H3N2 viruses isolated in Canada. J. Med. Virol. 67, 589-595 (2002).
    • (2002) J. Med. Virol. , vol.67 , pp. 589-595
    • Abed, Y.1    Hardy, I.2    Li, Y.3    Boivin, G.4
  • 191
    • 84865140575 scopus 로고    scopus 로고
    • Genetic evolution of the neuraminidase of influenza A (H3N2) viruses from 1968 to 2009 and its correspondence to haemagglutinin evolution
    • Westgeest, K. B. et al. Genetic evolution of the neuraminidase of influenza A (H3N2) viruses from 1968 to 2009 and its correspondence to haemagglutinin evolution. J. Gen. Virol. 93, 1996-2007 (2012).
    • (2012) J. Gen. Virol. , vol.93 , pp. 1996-2007
    • Westgeest, K.B.1
  • 192
    • 84897107877 scopus 로고    scopus 로고
    • Stability of neuraminidase in inactivated influenza vaccines
    • Sultana, I. et al. Stability of neuraminidase in inactivated influenza vaccines. Vaccine 32, 2225-2230 (2014).
    • (2014) Vaccine , vol.32 , pp. 2225-2230
    • Sultana, I.1
  • 193
    • 0016366813 scopus 로고
    • Induction of partial immunity to influenza by a neuraminidase-specific vaccine
    • Couch, R. B., Kasel, J. A., Gerin, J. L., Schulman, J. L. & Kilbourne, E. D. Induction of partial immunity to influenza by a neuraminidase-specific vaccine. J. Infect. Dis. 129, 411-420 (1974).
    • (1974) J. Infect. Dis. , vol.129 , pp. 411-420
    • Couch, R.B.1    Kasel, J.A.2    Gerin, J.L.3    Schulman, J.L.4    Kilbourne, E.D.5
  • 194
    • 0023546371 scopus 로고
    • Antigen-presenting B cells and helper T cells cooperatively mediate intravirionic antigenic competition between influenza A virus surface glycoproteins
    • Johansson, B. E., Moran, T. M. & Kilbourne, E. D. Antigen-presenting B cells and helper T cells cooperatively mediate intravirionic antigenic competition between influenza A virus surface glycoproteins. Proc. Natl Acad. Sci. USA 84, 6869-6873 (1987).
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 6869-6873
    • Johansson, B.E.1    Moran, T.M.2    Kilbourne, E.D.3
  • 195
    • 0027321481 scopus 로고
    • Dissociation of influenza virus hemagglutinin and neuraminidase eliminates their intravirionic antigenic competition
    • Johansson, B. E. & Kilbourne, E. D. Dissociation of influenza virus hemagglutinin and neuraminidase eliminates their intravirionic antigenic competition. J. Virol. 67, 5721-5723 (1993).
    • (1993) J. Virol. , vol.67 , pp. 5721-5723
    • Johansson, B.E.1    Kilbourne, E.D.2
  • 196
    • 0028205159 scopus 로고
    • Immunization with purified N1 and N2 influenza virus neuraminidases demonstrates cross-reactivity without antigenic competition
    • Johansson, B. E. & Kilbourne, E. D. Immunization with purified N1 and N2 influenza virus neuraminidases demonstrates cross-reactivity without antigenic competition. Proc. Natl Acad. Sci. USA 91, 2358-2361 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 2358-2361
    • Johansson, B.E.1    Kilbourne, E.D.2
  • 197
    • 0029591660 scopus 로고
    • Purified influenza A virus N2 neuraminidase vaccine is immunogenic and non-toxic in humans
    • Kilbourne, E. D. et al. Purified influenza A virus N2 neuraminidase vaccine is immunogenic and non-toxic in humans. Vaccine 13, 1799-1803 (1995).
    • (1995) Vaccine , vol.13 , pp. 1799-1803
    • Kilbourne, E.D.1
  • 198
    • 84864013012 scopus 로고    scopus 로고
    • Protection against a lethal H5N1 influenza challenge by intranasal immunization with virus-like particles containing 2009 pandemic H1N1 neuraminidase in mice
    • Easterbrook, J. D. et al. Protection against a lethal H5N1 influenza challenge by intranasal immunization with virus-like particles containing 2009 pandemic H1N1 neuraminidase in mice. Virology 432, 39-44 (2012).
    • (2012) Virology , vol.432 , pp. 39-44
    • Easterbrook, J.D.1
  • 199
    • 0023244108 scopus 로고
    • Immunologic response to the influenza virus neuraminidase is influenced by prior experience with the associated viral hemagglutinin. I. Studies in human vaccinees
    • Kilbourne, E. D., Cerini, C. P., Khan, M. W., Mitchell, J. W. & Ogra, P. L. Immunologic response to the influenza virus neuraminidase is influenced by prior experience with the associated viral hemagglutinin. I. Studies in human vaccinees. J. Immunol. 138, 3010-3013 (1987).
    • (1987) J. Immunol. , vol.138 , pp. 3010-3013
    • Kilbourne, E.D.1    Cerini, C.P.2    Khan, M.W.3    Mitchell, J.W.4    Ogra, P.L.5
  • 200
    • 65449185906 scopus 로고    scopus 로고
    • Universal M2 ectodomain-based influenza A vaccines: Preclinical and clinical developments
    • Schotsaert, M., De Filette, M., Fiers, W. & Saelens, X. Universal M2 ectodomain-based influenza A vaccines: preclinical and clinical developments. Expert Rev. Vaccines 8, 499-508 (2009).
    • (2009) Expert Rev. Vaccines , vol.8 , pp. 499-508
    • Schotsaert, M.1    De Filette, M.2    Fiers, W.3    Saelens, X.4
  • 201
    • 0032874490 scopus 로고    scopus 로고
    • A universal influenza A vaccine based on the extracellular domain of the M2 protein
    • Neirynck, S. et al. A universal influenza A vaccine based on the extracellular domain of the M2 protein. Nature Med. 5, 1157-1163 (1999).
    • (1999) Nature Med. , vol.5 , pp. 1157-1163
    • Neirynck, S.1
  • 202
    • 45549108140 scopus 로고    scopus 로고
    • An influenza A vaccine based on tetrameric ectodomain of matrix protein 2
    • De Filette, M. et al. An influenza A vaccine based on tetrameric ectodomain of matrix protein 2. J. Biol. Chem. 283, 11382-11387 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 11382-11387
    • De Filette, M.1
  • 203
    • 84895071915 scopus 로고    scopus 로고
    • Nanoclusters self-assembled from conformation-stabilized influenza M2e as broadly cross-protective influenza vaccines
    • Wang, L. et al. Nanoclusters self-assembled from conformation-stabilized influenza M2e as broadly cross-protective influenza vaccines. Nanomedicine 10, 473-482 (2014).
    • (2014) Nanomedicine , vol.10 , pp. 473-482
    • Wang, L.1
  • 204
    • 37449031125 scopus 로고    scopus 로고
    • Potent immunogenicity and efficacy of a universal influenza vaccine candidate comprising a recombinant fusion protein linking influenza M2e to the TLR5 ligand flagellin
    • Huleatt, J. et al. Potent immunogenicity and efficacy of a universal influenza vaccine candidate comprising a recombinant fusion protein linking influenza M2e to the TLR5 ligand flagellin. Vaccine 26, 201-214 (2008).
    • (2008) Vaccine , vol.26 , pp. 201-214
    • Huleatt, J.1
  • 205
    • 19444368726 scopus 로고    scopus 로고
    • Universal influenza A vaccine: Optimization of M2-based constructs
    • De Filette, M. et al. Universal influenza A vaccine: optimization of M2-based constructs. Virology 337, 149-161 (2005).
    • (2005) Virology , vol.337 , pp. 149-161
    • De Filette, M.1
  • 206
    • 84861823634 scopus 로고    scopus 로고
    • In contrast to conventional inactivated influenza vaccines, 4xM2e. HSP70c fusion protein fully protected mice against lethal dose of H1, H3 and H9 influenza A isolates circulating in Iran
    • Ebrahimi, S. M., Dabaghian, M., Tebianian, M. & Jazi, M. H. In contrast to conventional inactivated influenza vaccines, 4xM2e. HSP70c fusion protein fully protected mice against lethal dose of H1, H3 and H9 influenza A isolates circulating in Iran. Virology 430, 63-72 (2012).
    • (2012) Virology , vol.430 , pp. 63-72
    • Ebrahimi, S.M.1    Dabaghian, M.2    Tebianian, M.3    Jazi, M.H.4
  • 207
    • 79251585956 scopus 로고    scopus 로고
    • Universal vaccine based on ectodomain of matrix protein 2 of influenza A: Fc receptors and alveolar macrophages mediate protection
    • El Bakkouri, K. et al. Universal vaccine based on ectodomain of matrix protein 2 of influenza A: Fc receptors and alveolar macrophages mediate protection. J. Immunol. 186, 1022-1031 (2011).
    • (2011) J. Immunol. , vol.186 , pp. 1022-1031
    • El Bakkouri, K.1
  • 208
    • 84927732590 scopus 로고    scopus 로고
    • Efficacy and safety of treatment with an anti-M2e monoclonal antibody in experimental human influenza
    • Ramos, E. L. et al. Efficacy and safety of treatment with an anti-M2e monoclonal antibody in experimental human influenza. J. Infect. Dis. http://dx.doi.org/10.1093/infdis/jiu539 (2014).
    • (2014) J. Infect. Dis.
    • Ramos, E.L.1
  • 209
    • 79951645476 scopus 로고    scopus 로고
    • Potent CD8+ T-cell immunogenicity in humans of a novel heterosubtypic influenza A vaccine, MVA-NP+M1
    • Berthoud, T. K. et al. Potent CD8+ T-cell immunogenicity in humans of a novel heterosubtypic influenza A vaccine, MVA-NP+M1. Clin. Infect. Dis. 52, 1-7 (2011).
    • (2011) Clin. Infect. Dis. , vol.52 , pp. 1-7
    • Berthoud, T.K.1
  • 210
    • 84868283459 scopus 로고    scopus 로고
    • A T cell-inducing influenza vaccine for the elderly: Safety and immunogenicity of MVA-NP+M1 in adults aged over 50 years
    • Antrobus, R. D. et al. A T cell-inducing influenza vaccine for the elderly: safety and immunogenicity of MVA-NP+M1 in adults aged over 50 years. PLoS ONE 7, e48322 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e48322
    • Antrobus, R.D.1
  • 211
    • 84862219175 scopus 로고    scopus 로고
    • Preliminary assessment of the efficacy of a T-cell-based influenza vaccine, MVA-NP+M1, in humans
    • Lillie, P. J. et al. Preliminary assessment of the efficacy of a T-cell-based influenza vaccine, MVA-NP+M1, in humans. Clin. Infect. Dis. 55, 19-25 (2012).
    • (2012) Clin. Infect. Dis. , vol.55 , pp. 19-25
    • Lillie, P.J.1
  • 212
    • 84880022591 scopus 로고    scopus 로고
    • Improved adjuvanting of seasonal influenza vaccines: Preclinical studies of MVA-NP+M1 coadministration with inactivated influenza vaccine
    • Mullarkey, C. E. et al. Improved adjuvanting of seasonal influenza vaccines: preclinical studies of MVA-NP+M1 coadministration with inactivated influenza vaccine. Eur. J. Immunol. 43, 1940-1952 (2013).
    • (2013) Eur. J. Immunol. , vol.43 , pp. 1940-1952
    • Mullarkey, C.E.1
  • 213
    • 84891835368 scopus 로고    scopus 로고
    • Coadministration of seasonal influenza vaccine and MVA-NP+M1 simultaneously achieves potent humoral and cell-mediated responses
    • Antrobus, R. D. et al. Coadministration of seasonal influenza vaccine and MVA-NP+M1 simultaneously achieves potent humoral and cell-mediated responses. Mol. Ther. 22, 233-238 (2014).
    • (2014) Mol. Ther. , vol.22 , pp. 233-238
    • Antrobus, R.D.1
  • 214
    • 84875150077 scopus 로고    scopus 로고
    • Immunity against heterosubtypic influenza virus induced by adenovirus and MVA expressing nucleoprotein and matrix protein-1
    • Lambe, T. et al. Immunity against heterosubtypic influenza virus induced by adenovirus and MVA expressing nucleoprotein and matrix protein-1. Sci. Rep. 3, 1443 (2013).
    • (2013) Sci. Rep. , vol.3 , pp. 1443
    • Lambe, T.1
  • 215
    • 84898769488 scopus 로고    scopus 로고
    • IL-15 adjuvanted multivalent vaccinia-based universal influenza vaccine requires CD4+ T cells for heterosubtypic protection
    • Valkenburg, S. A. et al. IL-15 adjuvanted multivalent vaccinia-based universal influenza vaccine requires CD4+ T cells for heterosubtypic protection. Proc. Natl Acad. Sci. USA 111, 5676-5681 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 5676-5681
    • Valkenburg, S.A.1
  • 216
    • 84880615843 scopus 로고    scopus 로고
    • Protection against lethal influenza with a viral mimic
    • Baker, S. F. et al. Protection against lethal influenza with a viral mimic. J. Virol. 87, 8591-8605 (2013).
    • (2013) J. Virol. , vol.87 , pp. 8591-8605
    • Baker, S.F.1
  • 217
    • 84878743809 scopus 로고    scopus 로고
    • Deliberate reduction of hemagglutinin and neuraminidase expression of influenza virus leads to an ultraprotective live vaccine in mice
    • Yang, C., Skiena, S., Futcher, B., Mueller, S. & Wimmer, E. Deliberate reduction of hemagglutinin and neuraminidase expression of influenza virus leads to an ultraprotective live vaccine in mice. Proc. Natl Acad. Sci. USA 110, 9481-9486 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9481-9486
    • Yang, C.1    Skiena, S.2    Futcher, B.3    Mueller, S.4    Wimmer, E.5
  • 218
    • 84870676890 scopus 로고    scopus 로고
    • Pseudotyped influenza A virus as a vaccine for the induction of heterotypic immunity
    • Powell, T. J., Silk, J. D., Sharps, J., Fodor, E. & Townsend, A. R. Pseudotyped influenza A virus as a vaccine for the induction of heterotypic immunity. J. Virol. 86, 13397-13406 (2012).
    • (2012) J. Virol. , vol.86 , pp. 13397-13406
    • Powell, T.J.1    Silk, J.D.2    Sharps, J.3    Fodor, E.4    Townsend, A.R.5
  • 219
    • 78649953803 scopus 로고    scopus 로고
    • Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes
    • Wang, T. T. et al. Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes. Proc. Natl Acad. Sci. USA 107, 18979-18984 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , pp. 18979-18984
    • Wang, T.T.1
  • 220
    • 79957449934 scopus 로고    scopus 로고
    • Heterosubtypic protective immunity against influenza A virus induced by fusion peptide of the hemagglutinin in comparison to ectodomain of M2 protein
    • Staneková, Z. et al. Heterosubtypic protective immunity against influenza A virus induced by fusion peptide of the hemagglutinin in comparison to ectodomain of M2 protein. Acta Virol. 55, 61-67 (2011).
    • (2011) Acta Virol. , vol.55 , pp. 61-67
    • Staneková, Z.1
  • 221
    • 84871725198 scopus 로고    scopus 로고
    • Two distinct regions of HA2 glycopolypeptide of influenza virus hemagglutinin elicit cross-protective immunity against influenza
    • Janul?ková, J., Staneková, Z., Mucha, V., Kostolansk?, F. & Varecková, E. Two distinct regions of HA2 glycopolypeptide of influenza virus hemagglutinin elicit cross-protective immunity against influenza. Acta Virol. 56, 169-176 (2012).
    • (2012) Acta Virol. , vol.56 , pp. 169-176
    • Janulková, J.1    Staneková, Z.2    Mucha, V.3    Kostolansk, F.4    Varecková, E.5
  • 222
    • 84861480715 scopus 로고    scopus 로고
    • Safety and immunogenicity of multimeric-001 - A novel universal influenza vaccine
    • Atsmon, J. et al. Safety and immunogenicity of multimeric-001-a novel universal influenza vaccine. J. Clin. Immunol. 32, 595-603 (2012).
    • (2012) J. Clin. Immunol. , vol.32 , pp. 595-603
    • Atsmon, J.1
  • 223
    • 84908080093 scopus 로고    scopus 로고
    • Priming by a novel universal influenza vaccine (multimeric-001) - A gateway for improving immune response in the elderly population
    • Atsmon, J. et al. Priming by a novel universal influenza vaccine (multimeric-001)-a gateway for improving immune response in the elderly population. Vaccine 32, 5816-5823 (2014).
    • (2014) Vaccine , vol.32 , pp. 5816-5823
    • Atsmon, J.1
  • 224
    • 84887473368 scopus 로고    scopus 로고
    • Cellular immune correlates of protection against symptomatic pandemic influenza
    • Sridhar, S. et al. Cellular immune correlates of protection against symptomatic pandemic influenza. Nature Med. 19, 1305-1312 (2013).
    • (2013) Nature Med. , vol.19 , pp. 1305-1312
    • Sridhar, S.1
  • 225
    • 80052929143 scopus 로고    scopus 로고
    • Cross-protective immunity against influenza pH1N1 2009 viruses induced by seasonal influenza A (H3N2) virus is mediated by virus-specific T-cells
    • Hillaire, M. L. et al. Cross-protective immunity against influenza pH1N1 2009 viruses induced by seasonal influenza A (H3N2) virus is mediated by virus-specific T-cells. J. Gen. Virol. 92, 2339-2349 (2011).
    • (2011) J. Gen. Virol. , vol.92 , pp. 2339-2349
    • Hillaire, M.L.1
  • 226
    • 84892465971 scopus 로고    scopus 로고
    • Human cytotoxic T lymphocytes directed to seasonal influenza A viruses cross-react with the newly emerging H7N9 virus
    • van de Sandt, C. E. et al. Human cytotoxic T lymphocytes directed to seasonal influenza A viruses cross-react with the newly emerging H7N9 virus. J. Virol. 88, 1684-1693 (2013).
    • (2013) J. Virol. , vol.88 , pp. 1684-1693
    • Van De Sandt, C.E.1
  • 227
    • 84924075140 scopus 로고    scopus 로고
    • Pandemic influenza vaccine manufacturing process and timeline
    • World Health Organization
    • World Health Organization. Pandemic influenza vaccine manufacturing process and timeline. World Health Organization [online], http://www.who.int/csr/disease/swineflu/notes/h1n1-vaccine-20090806/en (2009).
    • (2009) World Health Organization
  • 228
    • 84911404794 scopus 로고    scopus 로고
    • Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus
    • Lee, P. S. et al. Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus. Nature Commun. 5, 3614 (2014).
    • (2014) Nature Commun. , vol.5 , pp. 3614
    • Lee, P.S.1
  • 229
    • 77957767268 scopus 로고    scopus 로고
    • The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site
    • Li, Q. et al. The 2009 pandemic H1N1 neuraminidase N1 lacks the 150-cavity in its active site. Nature Struct. Mol. Biol. 17, 1266-1268 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 1266-1268
    • Li, Q.1
  • 230
    • 23144441143 scopus 로고    scopus 로고
    • GlyProt: In silico glycosylation of proteins
    • Bohne-Lang, A. & von der Lieth, C. W. GlyProt: in silico glycosylation of proteins. Nucleic Acids Res. 33, W214-W219 (2005).
    • (2005) Nucleic Acids Res. , vol.33 , pp. W214-W219
    • Bohne-Lang, A.1    Von Der Lieth, C.W.2
  • 231
    • 12144288130 scopus 로고    scopus 로고
    • The structure and receptor binding properties of the 1918 influenza hemagglutinin
    • Gamblin, S. et al. The structure and receptor binding properties of the 1918 influenza hemagglutinin. Science 303, 1838-1842 (2004).
    • (2004) Science , vol.303 , pp. 1838-1842
    • Gamblin, S.1
  • 232
    • 55249083577 scopus 로고    scopus 로고
    • Structural characterization of the 1918 influenza virus H1N1 neuraminidase
    • Xu, X., Zhu, X., Dwek, R. A., Stevens, J. & Wilson, I. A. Structural characterization of the 1918 influenza virus H1N1 neuraminidase. J. Virol. 82, 10493-10501 (2008).
    • (2008) J. Virol. , vol.82 , pp. 10493-10501
    • Xu, X.1    Zhu, X.2    Dwek, R.A.3    Stevens, J.4    Wilson, I.A.5


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