메뉴 건너뛰기




Volumn 72, Issue 8, 1998, Pages 6373-6380

Molecular mechanisms of serum resistance of human influenza H3N2 virus and their involvement in virus adaptation in a new host

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ;

EID: 0031902989     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.8.6373-6380.1998     Document Type: Article
Times cited : (52)

References (43)
  • 1
    • 0024827395 scopus 로고
    • The neuraminidase of influenza virus
    • Air, G. M., and W. G. Laver. 1989. The neuraminidase of influenza virus. Proteins 6:341-356.
    • (1989) Proteins , vol.6 , pp. 341-356
    • Air, G.M.1    Laver, W.G.2
  • 2
    • 0025298243 scopus 로고
    • Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins
    • Anders, E. M., C. A. Hartley, and D. C. Jackson. 1990. Bovine and mouse serum beta inhibitors of influenza A viruses are mannose-binding lectins. Proc. Natl. Acad. Sci. USA 87:4485-4489.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4485-4489
    • Anders, E.M.1    Hartley, C.A.2    Jackson, D.C.3
  • 3
    • 0028344851 scopus 로고
    • Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin
    • Anders, E. M., C. A. Hartley, P. C. Reading, and R. A. Ezekowitz. 1994. Complement-dependent neutralization of influenza virus by a serum mannose-binding lectin. J. Gen. Virol. 75:615-622.
    • (1994) J. Gen. Virol. , vol.75 , pp. 615-622
    • Anders, E.M.1    Hartley, C.A.2    Reading, P.C.3    Ezekowitz, R.A.4
  • 4
    • 0026054562 scopus 로고
    • The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity
    • Baum, L. G., and J. C. Paulson. 1991. The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity. Virology 180:10-15.
    • (1991) Virology , vol.180 , pp. 10-15
    • Baum, L.G.1    Paulson, J.C.2
  • 6
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor, R. J., Y. Kawaoka, R. G. Webster, and J. C. Paulson. 1994. Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology 205:17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 7
    • 0027302926 scopus 로고
    • Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity
    • Couceiro, J. N., J. C. Paulson, and L. G. Baum. 1993. Influenza virus strains selectively recognize sialyloligosaccharides on human respiratory epithelium; the role of the host cell in selection of hemagglutinin receptor specificity. Virus Res. 29:155-265.
    • (1993) Virus Res. , vol.29 , pp. 155-265
    • Couceiro, J.N.1    Paulson, J.C.2    Baum, L.G.3
  • 9
    • 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, M. B., S. Sabesan, J. J. Skehel, and D. C. Wiley. 1997. Binding of the influenza A virus to cell-surface receptors - structures of five hemagglutinin-sialyloligosaccharide complexes determined by x-ray crystallography. Virology 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
  • 10
    • 0026698245 scopus 로고
    • A solid-phase enzyme-linked assay for influenza virus receptor-binding activity
    • Gambaryan, A. S., and M. N. Matrosovich. 1992. A solid-phase enzyme-linked assay for influenza virus receptor-binding activity. J. Virol. Methods 39:111-123.
    • (1992) J. Virol. Methods , vol.39 , pp. 111-123
    • Gambaryan, A.S.1    Matrosovich, M.N.2
  • 11
    • 0030737610 scopus 로고    scopus 로고
    • Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers. Non-egg-adapted human H1 and H3 influenza A, and influenza B viruses share a common high binding affinity for 6′-sialyl(N-acetyllactosamine)
    • Gambaryan, A. S., A. B. Tuzikov, V. E. Piskarev, S. S. Yamnikova, D. K. Lvov, J. C. Robertson, N. V. Bovin, and M. N. Matrosovich. 1997. Specification of receptor-binding phenotypes of influenza virus isolates from different hosts using synthetic sialylglycopolymers. Non-egg-adapted human H1 and H3 influenza A, and influenza B viruses share a common high binding affinity for 6′-sialyl(N-acetyllactosamine). Virology 233:224-234.
    • (1997) Virology , vol.233 , pp. 224-234
    • Gambaryan, A.S.1    Tuzikov, A.B.2    Piskarev, V.E.3    Yamnikova, S.S.4    Lvov, D.K.5    Robertson, J.C.6    Bovin, N.V.7    Matrosovich, M.N.8
  • 12
    • 0029979088 scopus 로고    scopus 로고
    • Two evolutionary strategies of influenza viruses to escape host non-specific inhibitors: Alteration of hemagglutinin or neuraminidase specificity
    • Gimsa, U., I. Grotzinger, and J. Gimsa. 1996. Two evolutionary strategies of influenza viruses to escape host non-specific inhibitors: alteration of hemagglutinin or neuraminidase specificity. Virus Res. 42:127-135.
    • (1996) Virus Res. , vol.42 , pp. 127-135
    • Gimsa, U.1    Grotzinger, I.2    Gimsa, J.3
  • 13
    • 0002835185 scopus 로고
    • Chemistry of virus receptors
    • F. M. Burnet and W. M. Stanley (ed.), Academic Press, Inc., New York, N.Y.
    • Gottschalk, A. 1959. Chemistry of virus receptors, p. 51-61. In F. M. Burnet and W. M. Stanley (ed.), The viruses: biochemical, biological, and biophysical properties, vol. 3. Academic Press, Inc., New York, N.Y.
    • (1959) The Viruses: Biochemical, Biological, and Biophysical Properties , vol.3 , pp. 51-61
    • Gottschalk, A.1
  • 14
    • 0012464505 scopus 로고
    • Glycoproteins as influenza virus hemagglutinin inhibitors and as cellular virus receptors
    • A. Gottschalk (ed.), Elsevier Publishing Co., Amsterdam, The Netherlands
    • Gottschalk, A., G. Belyavin, and F. Biddle. 1972. Glycoproteins as influenza virus hemagglutinin inhibitors and as cellular virus receptors, p. 1082-1096. In A. Gottschalk (ed.), Glycoproteins. Their composition, structure and function, part A. Elsevier Publishing Co., Amsterdam, The Netherlands.
    • (1972) Glycoproteins. Their Composition, Structure and Function, Part A , pp. 1082-1096
    • Gottschalk, A.1    Belyavin, G.2    Biddle, F.3
  • 15
    • 0026632757 scopus 로고
    • Characterization of a new avian-like influenza A virus from horses in China
    • Guo, Y., M. Wang, Y. Kawaoka, O. Gorman, T. Ito, T. Saito, and R. G. Webster. 1992. Characterization of a new avian-like influenza A virus from horses in China. Virology 188:245-255.
    • (1992) Virology , vol.188 , pp. 245-255
    • Guo, Y.1    Wang, M.2    Kawaoka, Y.3    Gorman, O.4    Ito, T.5    Saito, T.6    Webster, R.G.7
  • 17
    • 0026653795 scopus 로고
    • Two distinct serum mannose-binding lectins function as β-inhibitors of influenza virus: Identification of bovine serum β-inhibitor as conglutinin
    • Hartley, C. A., D. C. Jackson, and E. M. Anders. 1992. Two distinct serum mannose-binding lectins function as β-inhibitors of influenza virus: identification of bovine serum β-inhibitor as conglutinin. J. Virol. 66:4358-4363.
    • (1992) J. Virol. , vol.66 , pp. 4358-4363
    • Hartley, C.A.1    Jackson, D.C.2    Anders, E.M.3
  • 18
    • 0031014661 scopus 로고    scopus 로고
    • Changes in the hemagglutinin molecule of influenza type A (H3N2) virus associated with increased virulence for mice
    • Hartley, C. A., P. C. Reading, A. C. Ward, and E. M. Anders. 1997. Changes in the hemagglutinin molecule of influenza type A (H3N2) virus associated with increased virulence for mice. Arch. Virol. 142:75-88.
    • (1997) Arch. Virol. , vol.142 , pp. 75-88
    • Hartley, C.A.1    Reading, P.C.2    Ward, A.C.3    Anders, E.M.4
  • 19
    • 0002044965 scopus 로고
    • Sialic acid as receptor determinant of ortho- and paramyxoviruses
    • A. Rosenberg (ed.), Plenum Press, New York, N.Y.
    • Herrler, G., J. Hausmann, and H. D. Klenk. 1995. Sialic acid as receptor determinant of ortho- and paramyxoviruses, p. 315-336. In A. Rosenberg (ed.), Biology of the sialic acids. Plenum Press, New York, N.Y.
    • (1995) Biology of the Sialic Acids , pp. 315-336
    • Herrler, G.1    Hausmann, J.2    Klenk, H.D.3
  • 20
    • 0030981954 scopus 로고    scopus 로고
    • Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection
    • Ito, T., Y. Suzuki, A. Takada, A. Kawamoto, K. Otsuki, H. Masuda, M. Yamada, T. Suzuki, H. Kida, and Y. Kawaoka. 1997. Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection. J. Virol. 71:3357-3362.
    • (1997) J. Virol. , vol.71 , pp. 3357-3362
    • Ito, T.1    Suzuki, Y.2    Takada, A.3    Kawamoto, A.4    Otsuki, K.5    Masuda, H.6    Yamada, M.7    Suzuki, T.8    Kida, H.9    Kawaoka, Y.10
  • 22
    • 0030896808 scopus 로고    scopus 로고
    • Preferential selection of receptor-binding variants of influenza virus hemagglutinin by the neutralizing antibody repertoire of transgenic mice expressing a human immunoglobulin mu minigene
    • Laeeq, S., C. A. Smith, S. D. Wagner, and D. B. Thomas. 1997. Preferential selection of receptor-binding variants of influenza virus hemagglutinin by the neutralizing antibody repertoire of transgenic mice expressing a human immunoglobulin mu minigene. J. Virol. 71:2600-2605.
    • (1997) J. Virol. , vol.71 , pp. 2600-2605
    • Laeeq, S.1    Smith, C.A.2    Wagner, S.D.3    Thomas, D.B.4
  • 23
    • 0028028246 scopus 로고
    • Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza A virus: Multivalency and steric stabilization of particulate biological systems
    • Lees, W. J., A. Spaltenstein, J. E. Kingery-Wood, and G. M. Whitesides. 1994. Polyacrylamides bearing pendant α-sialoside groups strongly inhibit agglutination of erythrocytes by influenza A virus: multivalency and steric stabilization of particulate biological systems. J. Med. Chem. 37:3419-3433.
    • (1994) J. Med. Chem. , vol.37 , pp. 3419-3433
    • Lees, W.J.1    Spaltenstein, A.2    Kingery-Wood, J.E.3    Whitesides, G.M.4
  • 24
    • 0014513394 scopus 로고
    • Substituted sialic acid prosthetic groups as determinants of viral hemagglutination
    • Levinson, B., D. Pepper, and G. Belyavin. 1969. Substituted sialic acid prosthetic groups as determinants of viral hemagglutination. J. Virol. 3:477-483.
    • (1969) J. Virol. , vol.3 , pp. 477-483
    • Levinson, B.1    Pepper, D.2    Belyavin, G.3
  • 26
    • 0026681694 scopus 로고
    • Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant
    • Matrosovich, M. N., A. S. Gambaryan, and M. P. Chumakov. 1992. Influenza viruses differ in recognition of 4-O-acetyl substitution of sialic acid receptor determinant. Virology 188:854-858.
    • (1992) Virology , vol.188 , pp. 854-858
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Chumakov, M.P.3
  • 28
    • 0030587463 scopus 로고    scopus 로고
    • Influenza viruses display high-affinity binding to human polyglycosylceramides represented on a solid-phase assay surface
    • Matrosovich, M. N., H. Miller-Podraza, S. Teneberg, J. Robertson, and K.-A. Karlsson. 1996. Influenza viruses display high-affinity binding to human polyglycosylceramides represented on a solid-phase assay surface. Virology 223:413-416.
    • (1996) Virology , vol.223 , pp. 413-416
    • Matrosovich, M.N.1    Miller-Podraza, H.2    Teneberg, S.3    Robertson, J.4    Karlsson, K.-A.5
  • 29
    • 0030748536 scopus 로고    scopus 로고
    • Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site
    • Matrosovich, M. N., A. S. Gambaryan, S. Teneberg, V. E. Piskarev, S. S. Yamnikova, D. K. Lvov, J. S. Robertson, and K.-A. Karlsson. 1997. Avian influenza A viruses differ from human viruses by recognition of sialyloligosaccharides and gangliosides and by a higher conservation of the HA receptor-binding site. Virology 233:224-234.
    • (1997) Virology , vol.233 , pp. 224-234
    • Matrosovich, M.N.1    Gambaryan, A.S.2    Teneberg, S.3    Piskarev, V.E.4    Yamnikova, S.S.5    Lvov, D.K.6    Robertson, J.S.7    Karlsson, K.-A.8
  • 31
    • 0000545033 scopus 로고
    • Interactions of animal viruses with cell surface receptors
    • M. Conn (ed.), Academic Press, Orlando, Fla.
    • Paulson, J. C. 1985. Interactions of animal viruses with cell surface receptors, p. 131-219. In M. Conn (ed.), The receptors, vol. 2. Academic Press, Orlando, Fla.
    • (1985) The Receptors , vol.2 , pp. 131-219
    • Paulson, J.C.1
  • 32
    • 0024360659 scopus 로고
    • Basis for the potent inhibition of influenza virus infection by equine and guinea pig α2-macroglobulin
    • Pritchett, T. J., and J. C. Paulson. 1989. Basis for the potent inhibition of influenza virus infection by equine and guinea pig α2-macroglobulin. J. Biol. Chem. 264:9850-9858.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9850-9858
    • Pritchett, T.J.1    Paulson, J.C.2
  • 33
    • 0020595851 scopus 로고
    • Single amino acid substitutions in influenza hemagglutinin change receptor binding specificity
    • Rogers, G. N., J. C. Paulson, R. S. Daniels, J. J. Skehel, I. A. Wilson, and D. C. Wiley. 1983. Single amino acid substitutions in influenza hemagglutinin change receptor binding specificity. Nature 304:76-78.
    • (1983) Nature , vol.304 , pp. 76-78
    • Rogers, G.N.1    Paulson, J.C.2    Daniels, R.S.3    Skehel, J.J.4    Wilson, I.A.5    Wiley, D.C.6
  • 34
    • 0021040861 scopus 로고
    • Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: Selection of receptor specific variants
    • Rogers, G. N., T. J. Pritchett, J. L. Lane, and J. C. Paulson. 1983. Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants. Virology 131:394-408.
    • (1983) Virology , vol.131 , pp. 394-408
    • Rogers, G.N.1    Pritchett, T.J.2    Lane, J.L.3    Paulson, J.C.4
  • 35
    • 0025958279 scopus 로고
    • Distinct glycoprotein inhibitors of influenza A virus in different animal sera
    • Ryan-Poirier, K. A., and Y. Kawaoka. 1991. Distinct glycoprotein inhibitors of influenza A virus in different animal sera. J. Virol. 65:389-395.
    • (1991) J. Virol. , vol.65 , pp. 389-395
    • Ryan-Poirier, K.A.1    Kawaoka, Y.2
  • 36
    • 0027175267 scopus 로고
    • α2-Macroglobulin is the major neutralizing inhibitor of influenza virus hemagglutination
    • Ryan-Poirier, K. A., and Y. Kawaoka. 1993. α2-Macroglobulin is the major neutralizing inhibitor of influenza virus hemagglutination. Virology 193:974-976.
    • (1993) Virology , vol.193 , pp. 974-976
    • Ryan-Poirier, K.A.1    Kawaoka, Y.2
  • 37
    • 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, N. K., J. E. Hanson, G. D. Glick, J. H. Brown, R. L. Crowther, P. Seong-Joon, J. J. Skehel, and D. C. Wiley. 1992. 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 31:9609-9621.
    • (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    Seong-Joon, P.6    Skehel, J.J.7    Wiley, D.C.8
  • 38
    • 0020348005 scopus 로고
    • Chemistry, metabolism, and biological functions of sialic acids
    • Schauer, R. 1982. Chemistry, metabolism, and biological functions of sialic acids. Adv. Carbohydr. Chem. Biochem. 40:131-234.
    • (1982) Adv. Carbohydr. Chem. Biochem. , vol.40 , pp. 131-234
    • Schauer, R.1
  • 39
    • 0028133152 scopus 로고
    • Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains
    • Suzuki, Y. 1994. Gangliosides as influenza virus receptors. Variation of influenza viruses and their recognition of the receptor sialo-sugar chains. Prog. Lipid Res. 33:429-457.
    • (1994) Prog. Lipid Res. , vol.33 , pp. 429-457
    • Suzuki, Y.1
  • 40
    • 0028230805 scopus 로고
    • Modulation of immunodominant sites in influenza hemagglutinin compromise antigenic variation and select receptor-binding variant viruses
    • Temoltzin-Palacios, F., and D. B. Thomas. 1994. Modulation of immunodominant sites in influenza hemagglutinin compromise antigenic variation and select receptor-binding variant viruses. J. Exp. Med. 179:1719-1724.
    • (1994) J. Exp. Med. , vol.179 , pp. 1719-1724
    • Temoltzin-Palacios, F.1    Thomas, D.B.2
  • 41
    • 0026541128 scopus 로고
    • Diversity in the sialic acids
    • Varki, A. 1992. Diversity in the sialic acids. Glycobiology 2:25-40.
    • (1992) Glycobiology , vol.2 , pp. 25-40
    • Varki, A.1
  • 42
    • 0023915219 scopus 로고
    • Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid
    • Weis, W., J. H. Brown, S. Cusack, J. C. Paulson, J. J. Skehel, and D. C. Wiley. 1988. Structure of the influenza virus hemagglutinin complexed with its receptor, sialic acid. Nature 333:426-431.
    • (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
  • 43
    • 0022620007 scopus 로고
    • Selection of influenza A virus adsorptive mutants by growth in the presence of a mixture of monoclonal antihemagglutinin antibodies
    • Yewdell, J. W., A. J. Caton, and W. Gerhard. 1986. Selection of influenza A virus adsorptive mutants by growth in the presence of a mixture of monoclonal antihemagglutinin antibodies. J. Virol. 57:623-628.
    • (1986) J. Virol. , vol.57 , pp. 623-628
    • Yewdell, J.W.1    Caton, A.J.2    Gerhard, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.