메뉴 건너뛰기




Volumn 2, Issue 1, 2017, Pages

Protective efficacy of influenza group 2 hemagglutinin stem-fragment immunogen vaccines

Author keywords

[No Author keywords available]

Indexed keywords


EID: 85042233316     PISSN: None     EISSN: 20590105     Source Type: Journal    
DOI: 10.1038/s41541-017-0036-2     Document Type: Article
Times cited : (41)

References (44)
  • 1
    • 85042215790 scopus 로고    scopus 로고
    • WHO. 2016 Influenza (Seasonal) fact sheet
    • WHO. 2016 Influenza (Seasonal) fact sheet http://www.who.int/mediacentre/factsheets/fs211/en/ (2016).
    • (2016)
  • 2
    • 31344482504 scopus 로고    scopus 로고
    • 1918 Influenza: The mother of all pandemics
    • Taubenberger, J. K. & Morens, D. M. 1918 Influenza: the mother of all pandemics. Emerg. Infect. Dis. 12, 15-22 (2006).
    • (2006) Emerg. Infect. Dis , vol.12 , pp. 15-22
    • Taubenberger, J.K.1    Morens, D.M.2
  • 3
    • 85042211303 scopus 로고    scopus 로고
    • (eds S. A. Plotkin, W. A. Orenstein, & P. A. Offit) Ch. 18, 294-311 (Elsevier, Philadelphia, 2013)
    • Luke, C. J., Lakdawala, S. S. & Subbarao, E. K. in Vaccines, Vol. 6 (eds S. A. Plotkin, W. A. Orenstein, & P. A. Offit) Ch. 18, 294-311 (Elsevier, Philadelphia, 2013).
    • Vaccines , vol.6
    • Luke, C.J.1    Lakdawala, S.S.2    Subbarao, E.K.3
  • 4
    • 84897377795 scopus 로고    scopus 로고
    • Bat-derived influenza-like viruses H17N10 and H18N11
    • Wu, Y., Wu, Y., Tefsen, B., Shi, Y. & Gao, G. F. Bat-derived influenza-like viruses H17N10 and H18N11. Trends Microbiol. 22, 183-191 (2014).
    • (2014) Trends Microbiol , vol.22 , pp. 183-191
    • Wu, Y.1    Wu, Y.2    Tefsen, B.3    Shi, Y.4    Gao, G.F.5
  • 5
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J. & Wiley, D. C. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69, 531-569 (2000).
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 6
    • 84875551472 scopus 로고    scopus 로고
    • Broadly neutralizing antiviral antibodies
    • Corti, D. & Lanzavecchia, A. Broadly neutralizing antiviral antibodies. Annu. Rev. Immunol. 31, 705-742 (2013).
    • (2013) Annu. Rev. Immunol , vol.31 , pp. 705-742
    • Corti, D.1    Lanzavecchia, A.2
  • 7
    • 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
  • 8
    • 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
  • 9
    • 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
  • 10
    • 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
  • 11
    • 84978224846 scopus 로고    scopus 로고
    • A Perspective on rational designs of a hemagglutinin based universal influenza vaccine
    • Van, T. D., Tran, N., Le, L. & Eisenhaber, F. A Perspective on rational designs of a hemagglutinin based universal influenza vaccine. Curr. Pharm. Des. 3547-3554 (2016).
    • (2016) Curr. Pharm. des , pp. 3547-3554
    • Van, T.D.1    Tran, N.2    Le, L.3    Eisenhaber, F.4
  • 12
    • 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
  • 13
    • 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. https://doi.org/10.1128/mBio.00018-10 (2010).
    • (2010) MBio
    • Steel, J.1
  • 14
    • 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
  • 15
    • 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
  • 16
    • 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
  • 17
    • 84941873935 scopus 로고    scopus 로고
    • A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen
    • Impagliazzo, A. et al. A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen. Science 349, 1301-1306 (2015).
    • (2015) Science , vol.349 , pp. 1301-1306
    • Impagliazzo, A.1
  • 18
    • 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
  • 19
    • 84935040954 scopus 로고    scopus 로고
    • Hemagglutinin sequence conservation guided stem immunogen design from influenza A H3 subtype
    • Mallajosyula, V. V. et al. Hemagglutinin sequence conservation guided stem immunogen design from influenza A H3 subtype. Front. Immunol. 6, 329 (2015).
    • (2015) Front. Immunol , vol.6 , pp. 329
    • Mallajosyula, V.V.1
  • 20
    • 84960448072 scopus 로고    scopus 로고
    • Stalking influenza by vaccination with pre-fusion headless HA mini-stem
    • Valkenburg, S. A. et al. Stalking influenza by vaccination with pre-fusion headless HA mini-stem. Sci. Rep. 6, 22666 (2016).
    • (2016) Sci. Rep , vol.6 , pp. 22666
    • Valkenburg, S.A.1
  • 21
    • 84941023600 scopus 로고    scopus 로고
    • Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
    • Yassine, H. M. et al. Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection. Nat. Med. 21, 1065-1070 (2015).
    • (2015) Nat. Med , vol.21 , pp. 1065-1070
    • Yassine, H.M.1
  • 22
    • 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
  • 23
    • 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
  • 24
    • 84867427047 scopus 로고    scopus 로고
    • Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA
    • Julien, J. P., Lee, P. S. & Wilson, I. A. Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA. Immunol. Rev. 250, 180-198 (2012).
    • (2012) Immunol. Rev , vol.250 , pp. 180-198
    • Julien, J.P.1    Lee, P.S.2    Wilson, I.A.3
  • 25
    • 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
  • 26
    • 84924060844 scopus 로고    scopus 로고
    • Advances in the development of influenza virus vaccines
    • Krammer, F. & Palese, P. Advances in the development of influenza virus vaccines. Nat. Rev. Drug Discov. 14, 167-182 (2015).
    • (2015) Nat. Rev. Drug Discov , vol.14 , pp. 167-182
    • Krammer, F.1    Palese, P.2
  • 27
    • 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
  • 28
    • 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
  • 29
    • 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
  • 30
    • 84990933990 scopus 로고    scopus 로고
    • High-throughput recombinant protein expression in Escherichia coli: Current status and future perspectives
    • Jia, B. & Jeon, C. O. High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives. Open Biol https://doi.org/10.1098/rsob.160196 (2016).
    • (2016) Open Biol
    • Jia, B.1    Jeon, C.O.2
  • 31
    • 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
  • 32
    • 84956934982 scopus 로고    scopus 로고
    • Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
    • DiLillo, D. J., Palese, P., Wilson, P. C. & Ravetch, J. V. Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J. Clin. Invest. 126, 605-610 (2016).
    • (2016) J. Clin. Invest , vol.126 , pp. 605-610
    • DiLillo, D.J.1    Palese, P.2    Wilson, P.C.3    Ravetch, J.V.4
  • 33
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR 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 FcgammaR interactions for protection against influenza virus in vivo. Nat. Med. 20, 143-151 (2014).
    • (2014) Nat. Med , vol.20 , pp. 143-151
    • DiLillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4
  • 34
    • 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
  • 35
    • 84961114525 scopus 로고    scopus 로고
    • Hemagglutinin stalk immunity reduces influenza virus replication and transmission in ferrets
    • Nachbagauer, R. et al. Hemagglutinin stalk immunity reduces influenza virus replication and transmission in ferrets. J. Virol. 90, 3268-3273 (2015).
    • (2015) J. Virol , vol.90 , pp. 3268-3273
    • Nachbagauer, R.1
  • 36
    • 84896714729 scopus 로고    scopus 로고
    • Evaluation of three live attenuated H2 pandemic influenza vaccine candidates in mice and ferrets
    • Chen, G. L. et al. Evaluation of three live attenuated H2 pandemic influenza vaccine candidates in mice and ferrets. J. Virol. 88, 2867-2876 (2014).
    • (2014) J. Virol , vol.88 , pp. 2867-2876
    • Chen, G.L.1
  • 37
    • 84888066215 scopus 로고    scopus 로고
    • Impact of prior seasonal H3N2 influenza vaccination or infection on protection and transmission of emerging variants of influenza A(H3N2)v virus in ferrets
    • Houser, K. V., Pearce, M. B., Katz, J. M. & Tumpey, T. M. Impact of prior seasonal H3N2 influenza vaccination or infection on protection and transmission of emerging variants of influenza A(H3N2)v virus in ferrets. J. Virol. 87, 13480-13489 (2013).
    • (2013) J. Virol , vol.87 , pp. 13480-13489
    • Houser, K.V.1    Pearce, M.B.2    Katz, J.M.3    Tumpey, T.M.4
  • 38
    • 84940723365 scopus 로고    scopus 로고
    • Recombinant H7 hemagglutinin forms subviral particles that protect mice and ferrets from challenge with H7N9 influenza virus
    • Pushko, P. et al. Recombinant H7 hemagglutinin forms subviral particles that protect mice and ferrets from challenge with H7N9 influenza virus. Vaccine 33, 4975-4982 (2015).
    • (2015) Vaccine , vol.33 , pp. 4975-4982
    • Pushko, P.1
  • 39
    • 84904393681 scopus 로고    scopus 로고
    • A single dose of whole inactivated H7N9 influenza vaccine confers protection from severe disease but not infection in ferrets
    • Wong, S. S. et al. A single dose of whole inactivated H7N9 influenza vaccine confers protection from severe disease but not infection in ferrets. Vaccine 32, 4571-4577 (2014).
    • (2014) Vaccine , vol.32 , pp. 4571-4577
    • Wong, S.S.1
  • 40
    • 85012257296 scopus 로고    scopus 로고
    • Defining the antibody cross-reactome directed against the influenza virus surface glycoproteins
    • Nachbagauer, R. et al. Defining the antibody cross-reactome directed against the influenza virus surface glycoproteins. Nat. Immunol. 18, 464-473 (2017).
    • (2017) Nat. Immunol , vol.18 , pp. 464-473
    • Nachbagauer, R.1
  • 41
    • 28944448292 scopus 로고    scopus 로고
    • Protein minimization of the gp120 binding region of human CD4
    • Sharma, D. et al. Protein minimization of the gp120 binding region of human CD4. Biochemistry 44, 16192-16202 (2005).
    • (2005) Biochemistry , vol.44 , pp. 16192-16202
    • Sharma, D.1
  • 42
    • 1642363339 scopus 로고    scopus 로고
    • Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin
    • Guthe, S. et al. Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin. J. Mol. Biol. 337, 905-915 (2004).
    • (2004) J. Mol. Biol , vol.337 , pp. 905-915
    • Guthe, S.1
  • 43
    • 0023760366 scopus 로고
    • Induction, persistence and strain specificity of haemagglutinin-specific secretory antibodies in lungs of mice after intragastric administration of inactivated influenza virus vaccines
    • Chen, K. S. & Quinnan, G. V. Jr. Induction, persistence and strain specificity of haemagglutinin-specific secretory antibodies in lungs of mice after intragastric administration of inactivated influenza virus vaccines. J. Gen. Virol. 69, 2779-2784 (1988).
    • (1988) J. Gen. Virol , vol.69 , pp. 2779-2784
    • Chen, K.S.1    Quinnan, G.V.2
  • 44
    • 84930885285 scopus 로고    scopus 로고
    • A single dose of an avian H3N8 influenza virus vaccine is highly immunogenic and efficacious against a recently emerged seal influenza virus in mice and ferrets
    • Baz, M. et al. A single dose of an avian H3N8 influenza virus vaccine is highly immunogenic and efficacious against a recently emerged seal influenza virus in mice and ferrets. J. Virol. 89, 6907-6917 (2015).
    • (2015) J. Virol , vol.89 , pp. 6907-6917
    • Baz, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.