메뉴 건너뛰기




Volumn 241, Issue 1, 1998, Pages 101-111

Studies of the binding properties of influenza hemagglutinin receptor- site mutants

Author keywords

[No Author keywords available]

Indexed keywords

VIRUS HEMAGGLUTININ; VIRUS RECEPTOR;

EID: 0032005708     PISSN: 00426822     EISSN: None     Source Type: Journal    
DOI: 10.1006/viro.1997.8958     Document Type: Article
Times cited : (128)

References (31)
  • 1
    • 0029021814 scopus 로고
    • Selection of recombinant vaccinia viruses on the basis of plaque formation
    • Blasco R., Moss B. Selection of recombinant vaccinia viruses on the basis of plaque formation. Gene. 158:1995;157-162.
    • (1995) Gene , vol.158 , pp. 157-162
    • Blasco, R.1    Moss, B.2
  • 2
    • 0023739416 scopus 로고
    • A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex
    • Brändli A. W., Hansson G. C., Rodriguez-Boulan E., Simons K. A polarized epithelial cell mutant deficient in translocation of UDP-galactose into the Golgi complex. J. Biol. Chem. 263:1988;16283-16290.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16283-16290
    • Brändli, A.W.1    Hansson, G.C.2    Rodriguez-Boulan, E.3    Simons, K.4
  • 3
    • 0027281690 scopus 로고
    • Direct colorimetric detection of a receptor-ligand interaction by a polymerized assembly
    • Charych D. H., Nagy J. O., Spevac W., Bednarski M. D. Direct colorimetric detection of a receptor-ligand interaction by a polymerized assembly. Science. 261:1993;585-588.
    • (1993) Science , vol.261 , pp. 585-588
    • Charych, D.H.1    Nagy, J.O.2    Spevac, W.3    Bednarski, M.D.4
  • 4
    • 0027988832 scopus 로고
    • Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates
    • Connor R. J., Kawaoka Y., Webster R. G., Paulson J. C. Receptor specificity in human, avian, and equine H2 and H3 influenza virus isolates. Virology. 205:1994;17-23.
    • (1994) Virology , vol.205 , pp. 17-23
    • Connor, R.J.1    Kawaoka, Y.2    Webster, R.G.3    Paulson, J.C.4
  • 5
    • 0020955303 scopus 로고
    • Analyses of the antigenicity of influenza hemagglutinin at the pH optimum for virus-mediated membrane fusion
    • Daniels R. S., Douglas A. R., Skehel J. J., Wiley D. C. Analyses of the antigenicity of influenza hemagglutinin at the pH optimum for virus-mediated membrane fusion. J. Gen. Virol. 64:1983;1657-1662.
    • (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
  • 8
    • 0030917883 scopus 로고    scopus 로고
    • Binding of the influenza A virus to cell-surface receptors: Structure of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography
    • Eisen M. B., Sabesan S., Skehel J. J., Wiley D. C. Binding of the influenza A virus to cell-surface receptors: Structure of five hemagglutinin-sialyloligosaccharide complexes determined by X-ray crystallography. Virology. 232:1997;19-31.
    • (1997) Virology , vol.232 , pp. 19-31
    • Eisen, M.B.1    Sabesan, S.2    Skehel, J.J.3    Wiley, D.C.4
  • 9
    • 0025850680 scopus 로고
    • High-efficiency formation of influenza virus transfectants
    • Enami M., Palese P. High-efficiency formation of influenza virus transfectants. J. Virol. 65:1991;2711-2713.
    • (1991) J. Virol. , vol.65 , pp. 2711-2713
    • Enami, M.1    Palese, P.2
  • 10
    • 0002835185 scopus 로고
    • The chemistry of virus receptors
    • New York: Academic Press. p. 51-61
    • Gottschalk A. The chemistry of virus receptors. The Viruses. 1959;Academic Press, New York. p. 51-61.
    • (1959) The Viruses
    • Gottschalk, A.1
  • 11
    • 0019795259 scopus 로고
    • Glycosylation does not determine segregation of viral envelope proteins in the plasma membranes of epithelial cells
    • Green R. F., Meiss H. K., Rodriguez-Boulan E. Glycosylation does not determine segregation of viral envelope proteins in the plasma membranes of epithelial cells. J. Cell. Biol. 89:1981;230-239.
    • (1981) J. Cell. Biol. , vol.89 , pp. 230-239
    • Green, R.F.1    Meiss, H.K.2    Rodriguez-Boulan, E.3
  • 12
    • 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., Suzuki Y., Takada A., Kawamoto A., Otsuki K., Masuda H., Yamada M., Suzuki T., Kida H., Kawaoka Y. Differences in sialic acid-galactose linkages in the chicken egg amnion and allantois influence human influenza virus receptor specificity and variant selection. J. Virol. 71:1997;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
  • 14
    • 0344603795 scopus 로고
    • Sequential mutations in hemagglutinins of influenza B virus isolates: Definition of antigenic domains
    • Krystal M., Young J. F., Palese P., Wilson I. A., Skehel J. J., Wiley D. C. Sequential mutations in hemagglutinins of influenza B virus isolates: Definition of antigenic domains. Proc. Natl. Acad. Sci. USA. 80:1983;4527-4531.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4527-4531
    • Krystal, M.1    Young, J.F.2    Palese, P.3    Wilson, I.A.4    Skehel, J.J.5    Wiley, D.C.6
  • 15
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 159:1987;367-382.
    • (1987) Methods Enzymol. , vol.159 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 16
    • 0028828081 scopus 로고
    • Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutination activity
    • Ohuchi M., Feldmann A., Ohuchi R., Klenk H.-D. Neuraminidase is essential for fowl plague virus hemagglutinin to show hemagglutination activity. Virology. 212:1995;77-83.
    • (1995) Virology , vol.212 , pp. 77-83
    • Ohuchi, M.1    Feldmann, A.2    Ohuchi, R.3    Klenk, H.-D.4
  • 17
    • 0024360659 scopus 로고
    • Basis for potent inhibition of influenza virus infection by equine and Guinea pig alpha-2-macroglobulin
    • Pritchett T. J., Paulson J. C. Basis for potent inhibition of influenza virus infection by equine and Guinea pig alpha-2-macroglobulin. J. Biol. Chem. 264:1989;9850-9858.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9850-9858
    • Pritchett, T.J.1    Paulson, J.C.2
  • 19
    • 0020595851 scopus 로고
    • Single amino acid substitutions in influenza hemagglutinin change receptor binding specificity
    • Rogers G. N., Paulson J. C., Daniels R. S., Skehel J. J., Wilson I. A., Wiley D. C. Single amino acid substitutions in influenza hemagglutinin change receptor binding specificity. Nature. 304:1983;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
  • 20
    • 0024466223 scopus 로고
    • Hemagglutinins of two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study
    • Sauter N. K., Bednarski M. D., Wurzberg B. A., Hanson J. E., Whitesides G. M., Skehel J. J., Wiley D. C. Hemagglutinins of two influenza virus variants bind to sialic acid derivatives with millimolar dissociation constants: A 500-MHz proton nuclear magnetic resonance study. Biochemistry. 28:1989;8388-8396.
    • (1989) Biochemistry , vol.28 , pp. 8388-8396
    • Sauter, N.K.1    Bednarski, M.D.2    Wurzberg, B.A.3    Hanson, J.E.4    Whitesides, G.M.5    Skehel, J.J.6    Wiley, D.C.7
  • 21
    • 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., Hanson J. E., Glick G. D., Brown J. H., Crowther R. L., Park S.-J., Skehel J. J., Wiley D. C. 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. 31:1992;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    Park, S.-J.6    Skehel, J.J.7    Wiley, D.C.8
  • 22
    • 0026343370 scopus 로고
    • Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: Evidence for virus-specific regulation of pH of an intracellular compartment involved in glycoprotein transport
    • Steinhauer D. A., Wharton S. A., Skehel J. J., Wiley D. C., Hay A. J. Amantadine selection of a mutant influenza virus containing an acid-stable hemagglutinin glycoprotein: Evidence for virus-specific regulation of pH of an intracellular compartment involved in glycoprotein transport. Proc. Natl. Acad. Sci. USA. 88:1991a;11525-11529.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11525-11529
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4    Hay, A.J.5
  • 23
    • 0025882934 scopus 로고
    • Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties
    • Steinhauer D. A., Wharton S. A., Wiley D. C., Skehel J. J. Deacylation of the hemagglutinin of influenza A/Aichi/2/68 has no effect on membrane fusion properties. Virology. 184:1991b;445-448.
    • (1991) Virology , vol.184 , pp. 445-448
    • Steinhauer, D.A.1    Wharton, S.A.2    Wiley, D.C.3    Skehel, J.J.4
  • 24
    • 0028824850 scopus 로고
    • Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin
    • Steinhauer D. A., Wharton S. A., Skehel J. J., Wiley D. C. Studies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin. J. Virol. 69:1995;6643-6651.
    • (1995) J. Virol. , vol.69 , pp. 6643-6651
    • Steinhauer, D.A.1    Wharton, S.A.2    Skehel, J.J.3    Wiley, D.C.4
  • 26
    • 0029880005 scopus 로고    scopus 로고
    • A surface plasmon resonance assay for the binding of influenza virus hemagglutinin to its sialic acid receptor
    • Takemoto D. K., Skehel J. J., Wiley D. C. A surface plasmon resonance assay for the binding of influenza virus hemagglutinin to its sialic acid receptor. Virology. 217:1996;452-458.
    • (1996) Virology , vol.217 , pp. 452-458
    • Takemoto, D.K.1    Skehel, J.J.2    Wiley, D.C.3
  • 27
    • 0028774043 scopus 로고
    • Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs
    • Watowich S. J., Skehel J. J., Wiley D. C. Crystal structures of influenza virus hemagglutinin in complex with high-affinity receptor analogs. Structure. 2:1994;719-731.
    • (1994) Structure , vol.2 , pp. 719-731
    • Watowich, S.J.1    Skehel, J.J.2    Wiley, D.C.3
  • 28
    • 0000016640 scopus 로고
    • Design and evaluation of a tightly binding fluorescent ligand for influenza A hemagglutinin
    • Weinhold E., Knowles J. R. Design and evaluation of a tightly binding fluorescent ligand for influenza A hemagglutinin. J. Am. Chem. Soc. 114:1992;9270-9275.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9270-9275
    • Weinhold, E.1    Knowles, J.R.2
  • 29
    • 0023915219 scopus 로고
    • Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid
    • Weis W. I., Brown J. H., Cusack S., Paulson J. C., Skehel J. J., Wiley D. C. Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature. 333:1988;426-431.
    • (1988) Nature , vol.333 , pp. 426-431
    • Weis, W.I.1    Brown, J.H.2    Cusack, S.3    Paulson, J.C.4    Skehel, J.J.5    Wiley, D.C.6
  • 30
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley D. C., Skehel J. J. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:1987;365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 31
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 angstroms resolution
    • Wilson I. A., Skehel J. J., Wiley D. C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 angstroms resolution. Nature. 289:1981;366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.