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Volumn 119, Issue 1, 2006, Pages 1-7

Variation and infectivity neutralization in influenza

Author keywords

Antibody; Antigenicity; Haemagglutinin; Receptor binding; Structure

Indexed keywords

AMINO ACID; IMMUNOGLOBULIN F(AB) FRAGMENT; LYMPHOCYTE ANTIGEN RECEPTOR; NEUTRALIZING ANTIBODY; SIALIC ACID; VIRUS HEMAGGLUTININ;

EID: 33746870392     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/j.1365-2567.2006.02421.x     Document Type: Review
Times cited : (131)

References (61)
  • 1
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley DC, Skehel JJ. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu Rev Biochem 1987; 56:365-94.
    • (1987) Annu Rev Biochem , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 2
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel JJ, Wiley DC. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu Rev Biochem 2000; 69:531-69.
    • (2000) Annu Rev Biochem , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 4
    • 0029881573 scopus 로고    scopus 로고
    • Characterization of a novel influenza hemagglutinin, H15: Criteria for determination of influenza A subtypes
    • Rohm C, Zhou N, Suss J, Mackenzie J, Webster RG. Characterization of a novel influenza hemagglutinin, H15: criteria for determination of influenza A subtypes. Virology 1996; 217:508-16.
    • (1996) Virology , vol.217 , pp. 508-516
    • Rohm, C.1    Zhou, N.2    Suss, J.3    Mackenzie, J.4    Webster, R.G.5
  • 5
    • 13944278749 scopus 로고    scopus 로고
    • Characterization of a novel influenza A virus hemagglutinin subtype (H16) obtained from black-headed gulls
    • Fouchier RA, Munster V, Wallensten A et al. Characterization of a novel influenza A virus hemagglutinin subtype (H16) obtained from black-headed gulls. J Virol 2005; 79:2814-22.
    • (2005) J Virol , vol.79 , pp. 2814-2822
    • Fouchier, R.A.1    Munster, V.2    Wallensten, A.3
  • 6
    • 0026175939 scopus 로고
    • Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses
    • Nobusawa E, Aoyama T, Kato H, Suzuki Y, Tateno Y, Nakajima K. Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 1991; 182:475-85.
    • (1991) Virology , vol.182 , pp. 475-485
    • Nobusawa, E.1    Aoyama, T.2    Kato, H.3    Suzuki, Y.4    Tateno, Y.5    Nakajima, K.6
  • 7
    • 0019860749 scopus 로고
    • Sequence relationships among the hemagglutinin genes of 12 subtypes of influenza A virus
    • Air GM. Sequence relationships among the hemagglutinin genes of 12 subtypes of influenza A virus. Proc Natl Acad Sci USA 1981; 78:7639-43.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7639-7643
    • Air, G.M.1
  • 8
    • 0036500549 scopus 로고    scopus 로고
    • H5 avian and H9 swine influenza virus haemagglutinin structures: Possible origin of influenza subtypes
    • Ha Y, Stevens DJ, Skehel JJ, Wiley DC. H5 avian and H9 swine influenza virus haemagglutinin structures: possible origin of influenza subtypes. Embo J 2002; 21:865-75.
    • (2002) Embo J , vol.21 , pp. 865-875
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 9
    • 3142574848 scopus 로고    scopus 로고
    • H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes
    • Russell RJ, Gamblin SJ, Haire LF, Stevens DJ, Xiao B, Ha Y, Skehel JJ. H1 and H7 influenza haemagglutinin structures extend a structural classification of haemagglutinin subtypes. Virology 2004; 325:287-96.
    • (2004) Virology , vol.325 , pp. 287-296
    • Russell, R.J.1    Gamblin, S.J.2    Haire, L.F.3    Stevens, D.J.4    Xiao, B.5    Ha, Y.6    Skehel, J.J.7
  • 11
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough PA, Hughson FM, Skehel JJ, Wiley DC. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 1994; 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 12
    • 0033529752 scopus 로고    scopus 로고
    • N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil
    • Chen J, Skehel JJ, Wiley DC. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. Proc Natl Acad Sci USA 1999; 96:8967-72.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 13
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson IA, Skehel JJ, Wiley DC. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 1981; 289:366-73.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 14
    • 0020595851 scopus 로고
    • Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity
    • Rogers G, Paulson JC, Daniels RS, Skehel JJ, Wilson IA, Wiley DC. Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity. Nature 1983; 304:76-8.
    • (1983) Nature , vol.304 , pp. 76-78
    • Rogers, G.1    Paulson, J.C.2    Daniels, R.S.3    Skehel, J.J.4    Wilson, I.A.5    Wiley, D.C.6
  • 15
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W, Brown JH, Cusack S, Paulson JC, Skehel JJ, Wiley DC. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 1988; 333:426-31.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 16
    • 0024466223 scopus 로고
    • Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study
    • Sauter NK, Bednarski MD, Wurzburg BA, Hanson JE, White-sides GM, Skehel JJ, Wiley DC. Hemagglutinins from two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: a 500-MHz proton nuclear magnetic resonance study. Biochemistry 1989; 28:8388-96.
    • (1989) Biochemistry , vol.28 , pp. 8388-8396
    • Sauter, N.K.1    Bednarski, M.D.2    Wurzburg, B.A.3    Hanson, J.E.4    White-sides, G.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 17
    • 0026799307 scopus 로고
    • Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: Analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography
    • Sauter NK, Hanson JE, Glick GD, Brown JH, Crowther RL, Park SJ, Skehel JJ, Wiley DC. Binding of influenza virus hemagglutinin to analogs of its cell-surface receptor, sialic acid: analysis by proton nuclear magnetic resonance spectroscopy and X-ray crystallography. Biochemistry 1992; 31:9609-21.
    • (1992) Biochemistry , vol.31 , pp. 9609-9621
    • Sauter, N.K.1    Hanson, J.E.2    Glick, G.D.3    Brown, J.H.4    Crowther, R.L.5    Park, S.J.6    Skehel, J.J.7    Wiley, D.C.8
  • 18
    • 0030917883 scopus 로고    scopus 로고
    • Binding of the influenza A virus to cell-surface receptors: Structures of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography
    • Eisen MB, Sabesan S, Skehel JJ, Wiley DC. Binding of the influenza A virus to cell-surface receptors: structures of five hemagglutinin- sialyloligosaccharide complexes determined by X-ray crystallography. Virology 1997; 232:19-31.
    • (1997) Virology , vol.232 , pp. 19-31
    • Eisen, M.B.1    Sabesan, S.2    Skehel, J.J.3    Wiley, D.C.4
  • 19
    • 0035949581 scopus 로고    scopus 로고
    • X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs
    • Ha Y, Stevens DJ, Skehel JJ, Wiley DC. X-ray structures of H5 avian and H9 swine influenza virus hemagglutinins bound to avian and human receptor analogs. Proc Natl Acad Sci USA 2001; 98:11181-6.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 11181-11186
    • Ha, Y.1    Stevens, D.J.2    Skehel, J.J.3    Wiley, D.C.4
  • 20
    • 12144288130 scopus 로고    scopus 로고
    • The structure and receptor binding properties of the 1918 influenza hemagglutinin
    • Gamblin SJ, Haire LF, Russell RJ et al. The structure and receptor binding properties of the 1918 influenza hemagglutinin. Science 2004: 303:1838-42.
    • (2004) Science , vol.303 , pp. 1838-1842
    • Gamblin, S.J.1    Haire, L.F.2    Russell, R.J.3
  • 21
    • 0028774043 scopus 로고
    • Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs
    • Watowich SJ, Skehel JJ, Wiley DC. Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs. Structure 1994; 2:719-31.
    • (1994) Structure , vol.2 , pp. 719-731
    • Watowich, S.J.1    Skehel, J.J.2    Wiley, D.C.3
  • 22
    • 0020520729 scopus 로고
    • Receptor determinants of human and animal influenza virus isolates: Differences in receptor specificity of the H3 hemagglutinin based on species of origin
    • Rogers GN, Paulson JC. Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin based on species of origin. Virology 1983; 127:361-73.
    • (1983) Virology , vol.127 , pp. 361-373
    • Rogers, G.N.1    Paulson, J.C.2
  • 23
    • 0033856695 scopus 로고    scopus 로고
    • Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals
    • Matrosovich M, Tuzikov A, Bovin N, Gambaryan A, Klimov A, Castrucci MR, Donatelli I, Kawaoka Y. Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals. J Virol 2000; 74:8502-12.
    • (2000) J Virol , vol.74 , pp. 8502-8512
    • Matrosovich, M.1    Tuzikov, A.2    Bovin, N.3    Gambaryan, A.4    Klimov, A.5    Castrucci, M.R.6    Donatelli, I.7    Kawaoka, Y.8
  • 24
    • 0024439330 scopus 로고
    • Avian-to-human transmission of the PB1 gene of influenza A viruses in the 1957 and 1968 pandemics
    • Kawaoka Y, Krauss S, Webster RG. Avian-to-human transmission of the PB1 gene of influenza A viruses in the 1957 and 1968 pandemics. J Virol 1989; 63:4603-8.
    • (1989) J Virol , vol.63 , pp. 4603-4608
    • Kawaoka, Y.1    Krauss, S.2    Webster, R.G.3
  • 25
    • 0032927194 scopus 로고    scopus 로고
    • The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties
    • Matrosovich M, Zhou N, Kawaoka Y, Webster R. The surface glycoproteins of H5 influenza viruses isolated from humans, chickens, and wild aquatic birds have distinguishable properties. J Virol 1999; 73:1146-55.
    • (1999) J Virol , vol.73 , pp. 1146-1155
    • Matrosovich, M.1    Zhou, N.2    Kawaoka, Y.3    Webster, R.4
  • 27
    • 25444432780 scopus 로고    scopus 로고
    • Avian influenza A (H5N1) infection in humans
    • Beigel JH, Farrar J, Han AM et al. Avian influenza A (H5N1) infection in humans. N Engl J Med 2005; 353:1374-85.
    • (2005) N Engl J Med , vol.353 , pp. 1374-1385
    • Beigel, J.H.1    Farrar, J.2    Han, A.M.3
  • 30
    • 0019512990 scopus 로고
    • Mechanism of antigenic drift in influenza virus. Amino acid sequence changes in an antigenically active region of Hong Kong (H3N2) influenza virus hemagglutinin
    • Laver WG, Air GM, Webster RG. Mechanism of antigenic drift in influenza virus. Amino acid sequence changes in an antigenically active region of Hong Kong (H3N2) influenza virus hemagglutinin. J Mol Biol 1981; 145:339-61.
    • (1981) J Mol Biol , vol.145 , pp. 339-361
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3
  • 31
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation
    • Wiley DC, Wilson IA, Skehel JJ. Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation. Nature 1981; 289:366-73.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 32
    • 0020629723 scopus 로고
    • Antigenic drift in influenza virus H3 hemagglutinin from 1968 to 1980: Multiple evolutionary pathways and sequential amino acid changes at key antigenic sites
    • Both GW, Sleigh MJ, Cox NJ, Kendal AP. Antigenic drift in influenza virus H3 hemagglutinin from 1968 to 1980: multiple evolutionary pathways and sequential amino acid changes at key antigenic sites. J Virol 1983; 48:52-60.
    • (1983) J Virol , vol.48 , pp. 52-60
    • Both, G.W.1    Sleigh, M.J.2    Cox, N.J.3    Kendal, A.P.4
  • 34
    • 0019500784 scopus 로고
    • Antigenic drift in the hemagglutinin of the Hong Kong influenza subtype: Correlation of amino acid changes with alterations in viral antigenicity
    • Sleigh MJ, Both GW, Underwood PA, Bender VJ. Antigenic drift in the hemagglutinin of the Hong Kong influenza subtype: correlation of amino acid changes with alterations in viral antigenicity. J Virol 1981; 37:845-53.
    • (1981) J Virol , vol.37 , pp. 845-853
    • Sleigh, M.J.1    Both, G.W.2    Underwood, P.A.3    Bender, V.J.4
  • 35
    • 0022437566 scopus 로고
    • The molecular basis of antigenic variation in influenza virus
    • Air GM, Laver WG. The molecular basis of antigenic variation in influenza virus. Adv Virus Res 1986; 31:53-102.
    • (1986) Adv Virus Res , vol.31 , pp. 53-102
    • Air, G.M.1    Laver, W.G.2
  • 36
    • 0020050946 scopus 로고
    • Molecular mechanisms of variation in influenza viruses
    • Webster RG, Laver WG, Air GM, Schild GC. Molecular mechanisms of variation in influenza viruses. Nature 1982; 296:115-21.
    • (1982) Nature , vol.296 , pp. 115-121
    • Webster, R.G.1    Laver, W.G.2    Air, G.M.3    Schild, G.C.4
  • 37
    • 0020416123 scopus 로고
    • The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype)
    • Caton AJ, Brownlee GG, Yewdell JW, Gerhard W. The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 1982; 31:417-27.
    • (1982) Cell , vol.31 , pp. 417-427
    • Caton, A.J.1    Brownlee, G.G.2    Yewdell, J.W.3    Gerhard, W.4
  • 38
    • 0022643215 scopus 로고
    • The antigenicity and evolution of influenza H1 haemagglutinin, from 1950-1957 and 1977-83: Two pathways from one gene
    • Raymond FL, Caton AJ, Cox NJ, Kendal AP, Brownlee GG. The antigenicity and evolution of influenza H1 haemagglutinin, from 1950-1957 and 1977-83: two pathways from one gene. Virology 1986; 148:275-87.
    • (1986) Virology , vol.148 , pp. 275-287
    • Raymond, F.L.1    Caton, A.J.2    Cox, N.J.3    Kendal, A.P.4    Brownlee, G.G.5
  • 40
    • 0021123386 scopus 로고
    • Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutinin
    • Knossow M, Daniels RS, Douglas AR, Skehel JJ, Wiley DC. Three-dimensional structure of an antigenic mutant of the influenza virus haemagglutinin. Nature 1984; 311:678-80.
    • (1984) Nature , vol.311 , pp. 678-680
    • Knossow, M.1    Daniels, R.S.2    Douglas, A.R.3    Skehel, J.J.4    Wiley, D.C.5
  • 42
    • 0029026358 scopus 로고
    • Structure of influenza virus haemagglutinin complexed with a neutralizing antibody
    • Bizebard T, Gigant B, Rigolet P et al. Structure of influenza virus haemagglutinin complexed with a neutralizing antibody. Nature 1995; 376:92-4.
    • (1995) Nature , vol.376 , pp. 92-94
    • Bizebard, T.1    Gigant, B.2    Rigolet, P.3
  • 43
    • 0033053331 scopus 로고    scopus 로고
    • A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site
    • Fleury D, Barrere B, Bizebard T, Daniels RS, Skehel JJ, Knossow M. A complex of influenza hemagglutinin with a neutralizing antibody that binds outside the virus receptor binding site. Nat Struct Biol 1999; 6:530-4.
    • (1999) Nat Struct Biol , vol.6 , pp. 530-534
    • Fleury, D.1    Barrere, B.2    Bizebard, T.3    Daniels, R.S.4    Skehel, J.J.5    Knossow, M.6
  • 45
    • 0025246369 scopus 로고
    • Structural basis of immune recognition of influenza virus hemagglutinin
    • Wilson IA, Cox NJ. Structural basis of immune recognition of influenza virus hemagglutinin. Annu Rev Immunol 1990; 8:737-71.
    • (1990) Annu Rev Immunol , vol.8 , pp. 737-771
    • Wilson, I.A.1    Cox, N.J.2
  • 46
    • 0017137615 scopus 로고
    • The analysis of the monoclonal immune response to influenza virus. II. The antigenicity of the viral hemagglutinin
    • Gerhard W. The analysis of the monoclonal immune response to influenza virus. II. The antigenicity of the viral hemagglutinin. J Exp Med 1976; 144:985-95.
    • (1976) J Exp Med , vol.144 , pp. 985-995
    • Gerhard, W.1
  • 47
    • 0019827545 scopus 로고
    • Antigenic structure of influenza virus haemagglutinin defined by hybridoma antibodies
    • Gerhard W, Yewdell J, Frankel ME, Webster R. Antigenic structure of influenza virus haemagglutinin defined by hybridoma antibodies. Nature 1981; 290:713-7.
    • (1981) Nature , vol.290 , pp. 713-717
    • Gerhard, W.1    Yewdell, J.2    Frankel, M.E.3    Webster, R.4
  • 48
    • 0018668683 scopus 로고
    • Antigenic drift in type a influenza virus. sequence differences in the hemagglutinin of Hong Kong (H3N2) variants selected with monoclonal hybridoma antibodies
    • Laver WG, Air GM, Webster RG, Gerhard W, Ward CW, Dopheide TA. Antigenic drift in type A influenza virus. sequence differences in the hemagglutinin of Hong Kong (H3N2) variants selected with monoclonal hybridoma antibodies. Virology 1979; 98:226-37.
    • (1979) Virology , vol.98 , pp. 226-237
    • Laver, W.G.1    Air, G.M.2    Webster, R.G.3    Gerhard, W.4    Ward, C.W.5    Dopheide, T.A.6
  • 49
    • 0020955303 scopus 로고
    • Analyses of the antigenicity of influenza haemagglutinin at the pH optimum for virus-mediated membrane fusion
    • Daniels RS, Douglas AR, Skehel JJ, Wiley DC. Analyses of the antigenicity of influenza haemagglutinin at the pH optimum for virus-mediated membrane fusion. J Gen Virol 1983; 64:1657-62.
    • (1983) J Gen Virol , vol.64 , pp. 1657-1662
    • Daniels, R.S.1    Douglas, A.R.2    Skehel, J.J.3    Wiley, D.C.4
  • 51
    • 4444376554 scopus 로고    scopus 로고
    • 2004 Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin
    • Abe Y, Takashita E, Sugawara K, Matsuzaki Y, Muraki Y, Hongo S 2004 Effect of the addition of oligosaccharides on the biological activities and antigenicity of influenza A/H3N2 virus hemagglutinin. J Virol 2004; 78:9605-11.
    • (2004) J Virol , vol.78 , pp. 9605-9611
    • Abe, Y.1    Takashita, E.2    Sugawara, K.3    Matsuzaki, Y.4    Muraki, Y.5    Hongo, S.6
  • 52
    • 2442542997 scopus 로고    scopus 로고
    • Recent changes among human influenza viruses
    • Lin YP, Gregory V, Bennett M, Hay A. Recent changes among human influenza viruses. Virus Res 2004; 103:47-52.
    • (2004) Virus Res , vol.103 , pp. 47-52
    • Lin, Y.P.1    Gregory, V.2    Bennett, M.3    Hay, A.4
  • 54
    • 0022519337 scopus 로고
    • Three-dimensional structure of an antigen-antibody complex at 2.8 a resolution
    • Amit AG, Mariuzza RA, Phillips SE, Poljak RJ. Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution. Science 1986; 233:747-53.
    • (1986) Science , vol.233 , pp. 747-753
    • Amit, A.G.1    Mariuzza, R.A.2    Phillips, S.E.3    Poljak, R.J.4
  • 55
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman PM, Varghese JN, Laver WG. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 1983; 303:41-4.
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 56
    • 0028965256 scopus 로고
    • Virus-neutralizing antibodies of immunoglobulin G (IgG) but not of IgM or IgA isotypes can cure influenza virus pneumonia in SCID mice
    • Palladino G, Mozdzanowska K, Washko G, Gerhard W. Virus-neutralizing antibodies of immunoglobulin G (IgG) but not of IgM or IgA isotypes can cure influenza virus pneumonia in SCID mice. J Virol 1995; 69:2075-81.
    • (1995) J Virol , vol.69 , pp. 2075-2081
    • Palladino, G.1    Mozdzanowska, K.2    Washko, G.3    Gerhard, W.4
  • 57
    • 0030722677 scopus 로고    scopus 로고
    • Role of the B-cell response in recovery of mice from primary influenza virus infection
    • Gerhard W, Mozdzanowska K, Furchner M, Washko G, Maiese K. Role of the B-cell response in recovery of mice from primary influenza virus infection. Immunol Rev 1997; 159:95-103.
    • (1997) Immunol Rev , vol.159 , pp. 95-103
    • Gerhard, W.1    Mozdzanowska, K.2    Furchner, M.3    Washko, G.4    Maiese, K.5
  • 59
    • 0030815421 scopus 로고    scopus 로고
    • High and low efficiency neutralization epitopes on the haemagglutinin of type A influenza virus
    • Schofield DJ, Stephenson JR, Dimmock NJ. High and low efficiency neutralization epitopes on the haemagglutinin of type A influenza virus. J Gen Virol 1997; 78:2441-6.
    • (1997) J Gen Virol , vol.78 , pp. 2441-2446
    • Schofield, D.J.1    Stephenson, J.R.2    Dimmock, N.J.3
  • 60
    • 0020619874 scopus 로고
    • Neutralization of poliovirus by a monoclonal antibody: Kinetics and stoichiometry
    • Icenogle J, Shiwen H, Duke G, Gilbert S, Rueckert R, Anderegg J. Neutralization of poliovirus by a monoclonal antibody: kinetics and stoichiometry. Virology 1983; 127:412-25.
    • (1983) Virology , vol.127 , pp. 412-425
    • Icenogle, J.1    Shiwen, H.2    Duke, G.3    Gilbert, S.4    Rueckert, R.5    Anderegg, J.6
  • 61
    • 0029552239 scopus 로고
    • Update on the neutralization of animal viruses
    • Dimmock NJ. Update on the neutralization of animal viruses. Rev Med Virol 1995; 5:165-79.
    • (1995) Rev Med Virol , vol.5 , pp. 165-179
    • Dimmock, N.J.1


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