메뉴 건너뛰기




Volumn 24, Issue 12, 2016, Pages 933-943

A Structural and Mathematical Modeling Analysis of the Likelihood of Antibody-Dependent Enhancement in Influenza

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; FC RECEPTOR; INFLUENZA VIRUS HEMAGGLUTININ; INFLUENZA VIRUS HEMAGGLUTININ 2; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; NEUTRALIZING ANTIBODY; VIRUS ANTIBODY;

EID: 84991282630     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2016.09.003     Document Type: Review
Times cited : (11)

References (70)
  • 1
    • 84966397893 scopus 로고    scopus 로고
    • Enhanced clearance of HIV-1-infected cells by broadly neutralizing antibodies against HIV-1 in vivo
    • 1 Lu, C.L., et al. Enhanced clearance of HIV-1-infected cells by broadly neutralizing antibodies against HIV-1 in vivo. Science 352 (2016), 1001–1004.
    • (2016) Science , vol.352 , pp. 1001-1004
    • Lu, C.L.1
  • 2
    • 84966341056 scopus 로고    scopus 로고
    • HIV-1 therapy with monoclonal antibody 3BNC117 elicits host immune responses against HIV-1
    • 2 Schoofs, T., et al. HIV-1 therapy with monoclonal antibody 3BNC117 elicits host immune responses against HIV-1. Science 352 (2016), 997–1001.
    • (2016) Science , vol.352 , pp. 997-1001
    • Schoofs, T.1
  • 3
    • 84897549848 scopus 로고    scopus 로고
    • High-resolution antibody dynamics of vaccine-induced immune responses
    • 3 Laserson, U., et al. High-resolution antibody dynamics of vaccine-induced immune responses. Proc. Natl. Acad. Sci. U.S.A. 111 (2014), 4928–4933.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. 4928-4933
    • Laserson, U.1
  • 4
    • 84866949036 scopus 로고    scopus 로고
    • Structural and genetic basis for development of broadly neutralizing influenza antibodies
    • 4 Lingwood, D., et al. Structural and genetic basis for development of broadly neutralizing influenza antibodies. Nature 489 (2012), 566–570.
    • (2012) Nature , vol.489 , pp. 566-570
    • Lingwood, D.1
  • 5
    • 84922225958 scopus 로고    scopus 로고
    • Rapid development of broadly influenza neutralizing antibodies through redundant mutations
    • 5 Pappas, L., et al. Rapid development of broadly influenza neutralizing antibodies through redundant mutations. Nature 516 (2014), 418–422.
    • (2014) Nature , vol.516 , pp. 418-422
    • Pappas, L.1
  • 6
    • 84955127051 scopus 로고    scopus 로고
    • Adjuvanted influenza-H1N1 vaccination reveals lymphoid signatures of age-dependent early responses and of clinical adverse events
    • 6 Sobolev, O., et al. Adjuvanted influenza-H1N1 vaccination reveals lymphoid signatures of age-dependent early responses and of clinical adverse events. Nat. Immunol. 17 (2016), 204–213.
    • (2016) Nat. Immunol. , vol.17 , pp. 204-213
    • Sobolev, O.1
  • 7
    • 81555228707 scopus 로고    scopus 로고
    • Immune responses to influenza virus infection
    • 7 Kreijtz, J.H., et al. Immune responses to influenza virus infection. Virus Res. 162 (2011), 19–30.
    • (2011) Virus Res. , vol.162 , pp. 19-30
    • Kreijtz, J.H.1
  • 8
    • 84954245342 scopus 로고    scopus 로고
    • Immune history profoundly affects broadly protective B cell responses to influenza
    • 8 Andrews, S.F., et al. Immune history profoundly affects broadly protective B cell responses to influenza. Science Transl. Med., 7, 2015, 316ra192.
    • (2015) Science Transl. Med. , vol.7 , pp. 316ra192
    • Andrews, S.F.1
  • 9
    • 84975744755 scopus 로고    scopus 로고
    • Immunogenic stimulus for germline precursors of antibodies that engage the influenza hemagglutinin receptor-binding site
    • 9 Schmidt, A.G., et al. Immunogenic stimulus for germline precursors of antibodies that engage the influenza hemagglutinin receptor-binding site. Cell Rep. 13 (2015), 2842–2850.
    • (2015) Cell Rep. , vol.13 , pp. 2842-2850
    • Schmidt, A.G.1
  • 10
    • 78649953803 scopus 로고    scopus 로고
    • Vaccination with a synthetic peptide from the influenza virus hemagglutinin provides protection against distinct viral subtypes
    • 10 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. U.S.A. 107 (2010), 18979–18984.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 18979-18984
    • Wang, T.T.1
  • 11
    • 84892615764 scopus 로고    scopus 로고
    • Mechanisms of hemagglutinin targeted influenza virus neutralization
    • 11 Brandenburg, B., et al. Mechanisms of hemagglutinin targeted influenza virus neutralization. PLoS ONE, 8, 2013, e80034.
    • (2013) PLoS ONE , vol.8 , pp. e80034
    • Brandenburg, B.1
  • 12
    • 84914165942 scopus 로고    scopus 로고
    • Relating influenza virus membrane fusion kinetics to stoichiometry of neutralizing antibodies at the single-particle level
    • 12 Otterstrom, J.J., et al. Relating influenza virus membrane fusion kinetics to stoichiometry of neutralizing antibodies at the single-particle level. Proc. Natl. Acad. Sci. U.S.A. 111 (2014), E5143–E5148.
    • (2014) Proc. Natl. Acad. Sci. U.S.A. , vol.111 , pp. E5143-E5148
    • Otterstrom, J.J.1
  • 13
    • 84956934982 scopus 로고    scopus 로고
    • Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
    • 13 DiLillo, D.J., et al. Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J. Clin. Invest. 126 (2016), 605–610.
    • (2016) J. Clin. Invest. , vol.126 , pp. 605-610
    • DiLillo, D.J.1
  • 14
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo
    • 14 DiLillo, D.J., et al. Broadly neutralizing hemagglutinin stalk-specific antibodies require FcgammaR interactions for protection against influenza virus in vivo. Nat. Med. 20 (2014), 143–151.
    • (2014) Nat. Med. , vol.20 , pp. 143-151
    • DiLillo, D.J.1
  • 15
    • 84941873935 scopus 로고    scopus 로고
    • A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen
    • 15 Impagliazzo, A., et al. A stable trimeric influenza hemagglutinin stem as a broadly protective immunogen. Science 349 (2015), 1301–1306.
    • (2015) Science , vol.349 , pp. 1301-1306
    • Impagliazzo, A.1
  • 16
    • 84941023600 scopus 로고    scopus 로고
    • Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
    • 16 Yassine, H.M., et al. Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection. Nat. Med. 21 (2015), 1065–1070.
    • (2015) Nat. Med. , vol.21 , pp. 1065-1070
    • Yassine, H.M.1
  • 17
    • 84973488141 scopus 로고    scopus 로고
    • Both neutralizing and non-neutralizing human H7N9 influenza vaccine-induced monoclonal antibodies confer protection
    • 17 Henry Dunand, C.J., et al. Both neutralizing and non-neutralizing human H7N9 influenza vaccine-induced monoclonal antibodies confer protection. Cell Host Microbe 19 (2016), 800–813.
    • (2016) Cell Host Microbe , vol.19 , pp. 800-813
    • Henry Dunand, C.J.1
  • 18
    • 64849114224 scopus 로고    scopus 로고
    • Antibody recognition of a highly conserved influenza virus epitope
    • 18 Ekiert, D.C., et al. Antibody recognition of a highly conserved influenza virus epitope. Science 324 (2009), 246–251.
    • (2009) Science , vol.324 , pp. 246-251
    • Ekiert, D.C.1
  • 19
    • 80051635697 scopus 로고    scopus 로고
    • A highly conserved neutralizing epitope on group 2 influenza A viruses
    • 19 Ekiert, D.C., et al. A highly conserved neutralizing epitope on group 2 influenza A viruses. Science 333 (2011), 843–850.
    • (2011) Science , vol.333 , pp. 843-850
    • Ekiert, D.C.1
  • 20
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • 20 Corti, D., et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333 (2011), 850–856.
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 21
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • 21 Dreyfus, C., et al. Highly conserved protective epitopes on influenza B viruses. Science 337 (2012), 1343–1348.
    • (2012) Science , vol.337 , pp. 1343-1348
    • Dreyfus, C.1
  • 22
    • 84940981698 scopus 로고    scopus 로고
    • A broadly neutralizing human monoclonal antibody is effective against H7N9
    • 22 Tharakaraman, K., et al. A broadly neutralizing human monoclonal antibody is effective against H7N9. Proc. Natl. Acad. Sci. U.S.A. 112 (2015), 10890–10895.
    • (2015) Proc. Natl. Acad. Sci. U.S.A. , vol.112 , pp. 10890-10895
    • Tharakaraman, K.1
  • 23
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • 23 Okuno, Y., et al. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67 (1993), 2552–2558.
    • (1993) J. Virol. , vol.67 , pp. 2552-2558
    • Okuno, Y.1
  • 24
    • 62049083943 scopus 로고    scopus 로고
    • Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses
    • 24 Sui, J., et al. Structural and functional bases for broad-spectrum neutralization of avian and human influenza A viruses. Nat. Struct. Mol. Biol. 16 (2009), 265–273.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 265-273
    • Sui, J.1
  • 25
    • 84880427552 scopus 로고    scopus 로고
    • An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies
    • 25 Nakamura, G., et al. An in vivo human-plasmablast enrichment technique allows rapid identification of therapeutic influenza A antibodies. Cell Host Microbe 14 (2013), 93–103.
    • (2013) Cell Host Microbe , vol.14 , pp. 93-103
    • Nakamura, G.1
  • 26
    • 77649242815 scopus 로고    scopus 로고
    • Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins
    • 26 Wang, T.T., et al. Broadly protective monoclonal antibodies against H3 influenza viruses following sequential immunization with different hemagglutinins. PLoS pathog., 6, 2010, e1000796.
    • (2010) PLoS pathog. , vol.6 , pp. e1000796
    • Wang, T.T.1
  • 27
    • 84863597077 scopus 로고    scopus 로고
    • A pan-H1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo
    • 27 Tan, G.S., et al. A pan-H1 anti-hemagglutinin monoclonal antibody with potent broad-spectrum efficacy in vivo. J. Virol. 86 (2012), 6179–6188.
    • (2012) J. Virol. , vol.86 , pp. 6179-6188
    • Tan, G.S.1
  • 28
    • 84901024170 scopus 로고    scopus 로고
    • Broadly neutralizing influenza hemagglutinin stem-specific antibody CR8020 targets residues that are prone to escape due to host selection pressure
    • 28 Tharakaraman, K., et al. Broadly neutralizing influenza hemagglutinin stem-specific antibody CR8020 targets residues that are prone to escape due to host selection pressure. Cell Host Microbe 15 (2014), 644–651.
    • (2014) Cell Host Microbe , vol.15 , pp. 644-651
    • Tharakaraman, K.1
  • 29
    • 84925883384 scopus 로고    scopus 로고
    • Options and obstacles for designing a universal influenza vaccine
    • 29 Jang, Y.H., Seong, B.L., Options and obstacles for designing a universal influenza vaccine. Viruses 6 (2014), 3159–3180.
    • (2014) Viruses , vol.6 , pp. 3159-3180
    • Jang, Y.H.1    Seong, B.L.2
  • 30
    • 34250365710 scopus 로고    scopus 로고
    • Prospects for a dengue virus vaccine
    • 30 Whitehead, S.S., et al. Prospects for a dengue virus vaccine. Nat. Rev. Microbiol. 5 (2007), 518–528.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 518-528
    • Whitehead, S.S.1
  • 31
    • 0018580825 scopus 로고
    • In vivo enhancement of dengue virus infection in rhesus monkeys by passively transferred antibody
    • 31 Halstead, S.B., In vivo enhancement of dengue virus infection in rhesus monkeys by passively transferred antibody. J. Infect. Dis. 140 (1979), 527–533.
    • (1979) J. Infect. Dis. , vol.140 , pp. 527-533
    • Halstead, S.B.1
  • 32
    • 0037446912 scopus 로고    scopus 로고
    • Antibody-dependent enhancement, a possible mechanism in augmented pulmonary disease of respiratory syncytial virus in the Bonnet monkey model
    • 32 Ponnuraj, E.M., et al. Antibody-dependent enhancement, a possible mechanism in augmented pulmonary disease of respiratory syncytial virus in the Bonnet monkey model. J. Infect. Dis. 187 (2003), 1257–1263.
    • (2003) J. Infect. Dis. , vol.187 , pp. 1257-1263
    • Ponnuraj, E.M.1
  • 33
    • 0028533290 scopus 로고
    • Antibody-dependent enhancement of respiratory syncytial virus infection by sera from young infants
    • 33 Osiowy, C., et al. Antibody-dependent enhancement of respiratory syncytial virus infection by sera from young infants. Clin. Diagnost. Lab. Immunol. 1 (1994), 670–677.
    • (1994) Clin. Diagnost. Lab. Immunol. , vol.1 , pp. 670-677
    • Osiowy, C.1
  • 34
    • 79952244491 scopus 로고    scopus 로고
    • Enhanced pneumonia and disease in pigs vaccinated with an inactivated human-like (delta-cluster) H1N2 vaccine and challenged with pandemic 2009 H1N1 influenza virus
    • 34 Gauger, P.C., et al. Enhanced pneumonia and disease in pigs vaccinated with an inactivated human-like (delta-cluster) H1N2 vaccine and challenged with pandemic 2009 H1N1 influenza virus. Vaccine 29 (2011), 2712–2719.
    • (2011) Vaccine , vol.29 , pp. 2712-2719
    • Gauger, P.C.1
  • 35
    • 84883859603 scopus 로고    scopus 로고
    • Vaccine-induced anti-HA2 antibodies promote virus fusion and enhance influenza virus respiratory disease
    • 35 Khurana, S., et al. Vaccine-induced anti-HA2 antibodies promote virus fusion and enhance influenza virus respiratory disease. Science Transl. Med., 5, 2013, 200ra114.
    • (2013) Science Transl. Med. , vol.5 , pp. 200ra114
    • Khurana, S.1
  • 36
    • 0024391384 scopus 로고
    • Antibody-dependent enhancement of yellow fever and Japanese encephalitis virus neurovirulence
    • 36 Gould, E.A., Buckley, A., Antibody-dependent enhancement of yellow fever and Japanese encephalitis virus neurovirulence. J. Gen Virol. 70 (1989), 1605–1608.
    • (1989) J. Gen Virol. , vol.70 , pp. 1605-1608
    • Gould, E.A.1    Buckley, A.2
  • 37
    • 0023631947 scopus 로고
    • Immune enhancement of yellow fever virus neurovirulence for mice: studies of mechanisms involved
    • 37 Gould, E.A., et al. Immune enhancement of yellow fever virus neurovirulence for mice: studies of mechanisms involved. J. Gen. Virol. 68 (1987), 3105–3112.
    • (1987) J. Gen. Virol. , vol.68 , pp. 3105-3112
    • Gould, E.A.1
  • 38
    • 0021848969 scopus 로고
    • Antibody-dependent enhancement of tick-borne encephalitis virus infectivity
    • 38 Phillpotts, R.J., et al. Antibody-dependent enhancement of tick-borne encephalitis virus infectivity. J. Gen. Virol. 66 (1985), 1831–1837.
    • (1985) J. Gen. Virol. , vol.66 , pp. 1831-1837
    • Phillpotts, R.J.1
  • 39
    • 78649820026 scopus 로고    scopus 로고
    • How innate immune mechanisms contribute to antibody-enhanced viral infections
    • 39 Ubol, S., Halstead, S.B., How innate immune mechanisms contribute to antibody-enhanced viral infections. Clin. Vaccine Immunol. 17 (2010), 1829–1835.
    • (2010) Clin. Vaccine Immunol. , vol.17 , pp. 1829-1835
    • Ubol, S.1    Halstead, S.B.2
  • 40
    • 0020349520 scopus 로고
    • Immune enhancement of viral infection
    • 40 Halstead, S.B., Immune enhancement of viral infection. Prog. Allergy 31 (1982), 301–364.
    • (1982) Prog. Allergy , vol.31 , pp. 301-364
    • Halstead, S.B.1
  • 41
    • 84908338122 scopus 로고    scopus 로고
    • Dengue viruses are enhanced by distinct populations of serotype cross-reactive antibodies in human immune sera
    • 41 de Alwis, R., et al. Dengue viruses are enhanced by distinct populations of serotype cross-reactive antibodies in human immune sera. PLoS pathog., 10, 2014, e1004386.
    • (2014) PLoS pathog. , vol.10 , pp. e1004386
    • de Alwis, R.1
  • 42
    • 84900843924 scopus 로고    scopus 로고
    • Mouse models to study dengue virus immunology and pathogenesis
    • 42 Zellweger, R.M., Shresta, S., Mouse models to study dengue virus immunology and pathogenesis. Front. Immunol., 5, 2014, 151.
    • (2014) Front. Immunol. , vol.5 , pp. 151
    • Zellweger, R.M.1    Shresta, S.2
  • 43
    • 84926427192 scopus 로고    scopus 로고
    • TLR4 genotype and environmental LPS mediate RSV bronchiolitis through Th2 polarization
    • 43 Caballero, M.T., et al. TLR4 genotype and environmental LPS mediate RSV bronchiolitis through Th2 polarization. J. Clin. Invest. 125 (2015), 571–582.
    • (2015) J. Clin. Invest. , vol.125 , pp. 571-582
    • Caballero, M.T.1
  • 44
    • 0023928581 scopus 로고
    • Antibody-mediated growth of influenza A NWS virus in macrophagelike cell line P388D1
    • 44 Ochiai, H., et al. Antibody-mediated growth of influenza A NWS virus in macrophagelike cell line P388D1. J. Virol. 62 (1988), 20–26.
    • (1988) J. Virol. , vol.62 , pp. 20-26
    • Ochiai, H.1
  • 45
    • 0026566352 scopus 로고
    • Infection enhancement of influenza A NWS virus in primary murine macrophages by anti-hemagglutinin monoclonal antibody
    • 45 Ochiai, H., et al. Infection enhancement of influenza A NWS virus in primary murine macrophages by anti-hemagglutinin monoclonal antibody. J. Med. Virol. 36 (1992), 217–221.
    • (1992) J. Med. Virol. , vol.36 , pp. 217-221
    • Ochiai, H.1
  • 46
    • 77951745708 scopus 로고    scopus 로고
    • Association between the 2008-09 seasonal influenza vaccine and pandemic H1N1 illness during Spring-Summer 2009: four observational studies from Canada
    • 46 Skowronski, D.M., et al. Association between the 2008-09 seasonal influenza vaccine and pandemic H1N1 illness during Spring-Summer 2009: four observational studies from Canada. PLoS Med., 7, 2010, e1000258.
    • (2010) PLoS Med. , vol.7 , pp. e1000258
    • Skowronski, D.M.1
  • 47
    • 2442629758 scopus 로고    scopus 로고
    • Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation
    • 47 Swalley, S.E., et al. Full-length influenza hemagglutinin HA2 refolds into the trimeric low-pH-induced conformation. Biochemistry 43 (2004), 5902–5911.
    • (2004) Biochemistry , vol.43 , pp. 5902-5911
    • Swalley, S.E.1
  • 48
    • 84857981961 scopus 로고    scopus 로고
    • Structural changes in Influenza virus at low pH characterized by cryo-electron tomography
    • 48 Fontana, J., et al. Structural changes in Influenza virus at low pH characterized by cryo-electron tomography. J. Virol. 86 (2012), 2919–2929.
    • (2012) J. Virol. , vol.86 , pp. 2919-2929
    • Fontana, J.1
  • 49
    • 84901304592 scopus 로고    scopus 로고
    • Alternative recognition of the conserved stem epitope in influenza A virus hemagglutinin by a VH3-30-encoded heterosubtypic antibody
    • 49 Wyrzucki, A., et al. Alternative recognition of the conserved stem epitope in influenza A virus hemagglutinin by a VH3-30-encoded heterosubtypic antibody. J. Virol. 88 (2014), 7083–7092.
    • (2014) J. Virol. , vol.88 , pp. 7083-7092
    • Wyrzucki, A.1
  • 50
    • 84867538000 scopus 로고    scopus 로고
    • The fate of influenza A virus after infection of human macrophages and dendritic cells
    • 50 Short, K.R., et al. The fate of influenza A virus after infection of human macrophages and dendritic cells. J. Gen. Virol. 93 (2012), 2315–2325.
    • (2012) J. Gen. Virol. , vol.93 , pp. 2315-2325
    • Short, K.R.1
  • 51
    • 6344270264 scopus 로고    scopus 로고
    • Structured model of influenza virus replication in MDCK cells
    • 51 Sidorenko, Y., Reichl, U., Structured model of influenza virus replication in MDCK cells. Biotechnol. Bioeng. 88 (2004), 1–14.
    • (2004) Biotechnol. Bioeng. , vol.88 , pp. 1-14
    • Sidorenko, Y.1    Reichl, U.2
  • 52
    • 0033579938 scopus 로고    scopus 로고
    • Interactions of influenza virus with cultured cells: detailed kinetic modeling of binding and endocytosis
    • 52 Nunes-Correia, I., et al. Interactions of influenza virus with cultured cells: detailed kinetic modeling of binding and endocytosis. Biochemistry 38 (1999), 1095–1101.
    • (1999) Biochemistry , vol.38 , pp. 1095-1101
    • Nunes-Correia, I.1
  • 53
    • 85012085322 scopus 로고    scopus 로고
    • Characterization of receptor binding profiles of influenza a viruses using an ellipsometry-based label-free glycan microarray assay platform
    • 53 Fei, Y., et al. Characterization of receptor binding profiles of influenza a viruses using an ellipsometry-based label-free glycan microarray assay platform. Biomolecules 5 (2015), 1480–1498.
    • (2015) Biomolecules , vol.5 , pp. 1480-1498
    • Fei, Y.1
  • 54
    • 84862495640 scopus 로고    scopus 로고
    • Properties of mouse and human IgG receptors and their contribution to disease models
    • 54 Bruhns, P., Properties of mouse and human IgG receptors and their contribution to disease models. Blood 119 (2012), 5640–5649.
    • (2012) Blood , vol.119 , pp. 5640-5649
    • Bruhns, P.1
  • 55
    • 0019977498 scopus 로고
    • Cell number and cell characteristics of the normal human lung
    • 55 Crapo, J.D., et al. Cell number and cell characteristics of the normal human lung. Am. Rev. Resp. Dis. 126 (1982), 332–337.
    • (1982) Am. Rev. Resp. Dis. , vol.126 , pp. 332-337
    • Crapo, J.D.1
  • 56
    • 0030945662 scopus 로고    scopus 로고
    • Quantitation of surface CD14 on human monocytes and neutrophils
    • 56 Antal-Szalmas, P., et al. Quantitation of surface CD14 on human monocytes and neutrophils. J. Lleukocyte Biol. 61 (1997), 721–728.
    • (1997) J. Lleukocyte Biol. , vol.61 , pp. 721-728
    • Antal-Szalmas, P.1
  • 57
    • 84964632488 scopus 로고    scopus 로고
    • H7N9 influenza virus neutralizing antibodies that possess few somatic mutations
    • 57 Thornburg, N.J., et al. H7N9 influenza virus neutralizing antibodies that possess few somatic mutations. J. Clin. Invest. 126 (2016), 1482–1494.
    • (2016) J. Clin. Invest. , vol.126 , pp. 1482-1494
    • Thornburg, N.J.1
  • 58
    • 33746190701 scopus 로고    scopus 로고
    • Kinetics of influenza A virus infection in humans
    • 58 Baccam, P., et al. Kinetics of influenza A virus infection in humans. J. Virol. 80 (2006), 7590–7599.
    • (2006) J. Virol. , vol.80 , pp. 7590-7599
    • Baccam, P.1
  • 59
    • 84944055938 scopus 로고    scopus 로고
    • Modeling Influenza Virus Infection: A Roadmap for Influenza Research
    • 59 Boianelli, A., et al. Modeling Influenza Virus Infection: A Roadmap for Influenza Research. Viruses 7 (2015), 5274–5304.
    • (2015) Viruses , vol.7 , pp. 5274-5304
    • Boianelli, A.1
  • 60
    • 84874514993 scopus 로고    scopus 로고
    • Assessing mathematical models of influenza infections using features of the immune response
    • 60 Dobrovolny, H.M., et al. Assessing mathematical models of influenza infections using features of the immune response. PLoS ONE, 8, 2013, e57088.
    • (2013) PLoS ONE , vol.8 , pp. e57088
    • Dobrovolny, H.M.1
  • 61
    • 84940774944 scopus 로고    scopus 로고
    • Innate immunity and the inter-exposure interval determine the dynamics of secondary influenza virus infection and explain observed viral hierarchies
    • 61 Cao, P., et al. Innate immunity and the inter-exposure interval determine the dynamics of secondary influenza virus infection and explain observed viral hierarchies. PLoS Comput. Biol., 11, 2015, e1004334.
    • (2015) PLoS Comput. Biol. , vol.11 , pp. e1004334
    • Cao, P.1
  • 62
    • 84896731326 scopus 로고    scopus 로고
    • Modeling inoculum dose dependent patterns of acute virus infections
    • 62 Li, Y., Handel, A., Modeling inoculum dose dependent patterns of acute virus infections. J. Theor. Biol. 347 (2014), 63–73.
    • (2014) J. Theor. Biol. , vol.347 , pp. 63-73
    • Li, Y.1    Handel, A.2
  • 63
    • 39749139538 scopus 로고    scopus 로고
    • Viral and host factors in human respiratory syncytial virus pathogenesis
    • 63 Collins, P.L., Graham, B.S., Viral and host factors in human respiratory syncytial virus pathogenesis. J. Virol. 82 (2008), 2040–2055.
    • (2008) J. Virol. , vol.82 , pp. 2040-2055
    • Collins, P.L.1    Graham, B.S.2
  • 64
    • 0028263755 scopus 로고
    • Enhanced pulmonary histopathology induced by respiratory syncytial virus (RSV) challenge of formalin-inactivated RSV-immunized BALB/c mice is abrogated by depletion of interleukin-4 (IL-4) and IL-10
    • 64 Connors, M., et al. Enhanced pulmonary histopathology induced by respiratory syncytial virus (RSV) challenge of formalin-inactivated RSV-immunized BALB/c mice is abrogated by depletion of interleukin-4 (IL-4) and IL-10. J. Virol. 68 (1994), 5321–5325.
    • (1994) J. Virol. , vol.68 , pp. 5321-5325
    • Connors, M.1
  • 65
    • 0031441754 scopus 로고    scopus 로고
    • CD8 + T cells control Th2-driven pathology during pulmonary respiratory syncytial virus infection
    • 65 Hussell, T., et al. CD8 + T cells control Th2-driven pathology during pulmonary respiratory syncytial virus infection. Eur. J. Immunol. 27 (1997), 3341–3349.
    • (1997) Eur. J. Immunol. , vol.27 , pp. 3341-3349
    • Hussell, T.1
  • 66
    • 2442706505 scopus 로고    scopus 로고
    • Respiratory syncytial virus (RSV) G glycoprotein is not necessary for vaccine-enhanced disease induced by immunization with formalin-inactivated RSV
    • 66 Johnson, T.R., et al. Respiratory syncytial virus (RSV) G glycoprotein is not necessary for vaccine-enhanced disease induced by immunization with formalin-inactivated RSV. J. Virol. 78 (2004), 6024–6032.
    • (2004) J. Virol. , vol.78 , pp. 6024-6032
    • Johnson, T.R.1
  • 67
    • 84906329950 scopus 로고    scopus 로고
    • Prophylaxis with a respiratory syncytial virus (RSV) anti-G protein monoclonal antibody shifts the adaptive immune response to RSV rA2-line19F infection from Th2 to Th1 in BALB/c mice
    • 67 Boyoglu-Barnum, S., et al. Prophylaxis with a respiratory syncytial virus (RSV) anti-G protein monoclonal antibody shifts the adaptive immune response to RSV rA2-line19F infection from Th2 to Th1 in BALB/c mice. J. Virol. 88 (2014), 10569–10583.
    • (2014) J. Virol. , vol.88 , pp. 10569-10583
    • Boyoglu-Barnum, S.1
  • 68
    • 84900418315 scopus 로고    scopus 로고
    • Cytokine diversity in the Th1-dominated human anti-influenza response caused by variable cytokine expression by Th1 cells, and a minor population of uncommitted IL-2 + IFNgamma- Thpp cells
    • 68 Deng, N., et al. Cytokine diversity in the Th1-dominated human anti-influenza response caused by variable cytokine expression by Th1 cells, and a minor population of uncommitted IL-2 + IFNgamma- Thpp cells. PLoS ONE, 9, 2014, e95986.
    • (2014) PLoS ONE , vol.9 , pp. e95986
    • Deng, N.1
  • 69
    • 0242668753 scopus 로고    scopus 로고
    • Influenza A virus infection inhibits the efficient recruitment of Th2 cells into the airways and the development of airway eosinophilia
    • 69 Wohlleben, G., et al. Influenza A virus infection inhibits the efficient recruitment of Th2 cells into the airways and the development of airway eosinophilia. J. Immunol. 170 (2003), 4601–4611.
    • (2003) J. Immunol. , vol.170 , pp. 4601-4611
    • Wohlleben, G.1
  • 70
    • 84963773526 scopus 로고    scopus 로고
    • The hemagglutinin stem-binding monoclonal antibody VIS410 controls influenza virus-induced acute respiratory distress syndrome
    • 70 Baranovich, T., et al. The hemagglutinin stem-binding monoclonal antibody VIS410 controls influenza virus-induced acute respiratory distress syndrome. Antimicrob. Agents Chemother. 60 (2016), 2118–2131.
    • (2016) Antimicrob. Agents Chemother. , vol.60 , pp. 2118-2131
    • Baranovich, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.