Changes in H3 influenza A virus receptor specificity during replication in humans

Virus Research

Volumn 56, Issue 2, 1998, Pages 169-176

  Ryan Poirier, Kathleen ^a,b,c   Suzuki, Yasuo ^d   Bean, William J ^a   Kobasa, Darwyn ^a   Takada, Ayato ^a,e   Ito, Toshihiro ^f   Kawaoka, Yoshihiro ^a,b  

^a ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^b UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

^c LE BONHEUR CHILDREN S HOSPITAL   (United States)

^d UNIVERSITY OF SHIZUOKA   (Japan)

^e Graduate School of Science   (Japan)

^f TOTTORI UNIVERSITY   (Japan)

Author keywords

Hemagglutinin; Influenza virus; Receptor specificity; Serum inhibitor

Indexed keywords

GANGLIOSIDE; HEMAGGLUTININ; VIRUS RECEPTOR;

HORSE; HUMAN; INFLUENZA VIRUS A; NONHUMAN; PRIORITY JOURNAL; RABBIT; RECEPTOR SENSITIVITY; REVIEW; SWINE; VIRUS NEUTRALIZATION; VIRUS REPLICATION;

AVES; EQUIDAE; EQUUS CABALLUS; INFLUENZA A VIRUS; INFLUENZA VIRUS; ORYCTOLAGUS CUNICULUS; SUS SCROFA;

EID: 0032144192     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-1702(98)00067-7     Document Type: Article

References (29)

1. Al-Nakib W., Tyrrell D.A. Drugs against rhinoviruses. J. Antimicrob. Chemother. 30:1992;115-117.
2. Ananthanarayan R., Paniker C.K.J. Non-specific inhibitors of influenza viruses in normal sera. Bull. WHO. 22:1960;409-419.
3. Baum L.G., Paulson J.C. Sialyloligosaccharides of the respiratory epithelium in the selection of human influenza virus receptor specificity. Acta Histochem. (Jena). 89(Suppl. 40):1990;35-38.
4. Bean W.J., Schell M., Katz J., Kawaoka Y., Naeve C., Gorman O., Webster R.G. Evolution of the H3 influenza virus hemagglutinin from human and nonhuman hosts. J. Virol. 66:1992;1129-1138.
5. Deom C.M., Caton A.J., Schulze I.T. Host cell-mediated selection of a mutant influenza A virus that has lost a complex oligosaccharide from the tip of the hemagglutinin. Proc. Natl. Acad. Sci. USA. 83:1986;3771-3775.
6. Gottschalk, A., 1959. In: Burnet, F.M., Stanley, W.M. (Eds.), The Viruses. Academic Press, New York, pp. 51-61.
7. Higa H.H., Rogers G.N., Paulson J.C. Influenza virus hemagglutinins differentiate between receptor determinants bearing N-acetyl-N-glycolyl-, and N,O-diacetylneuraminic acids. Virology. 144:1985;279-282.
8. 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 amnion and allantois of chicken eggs influence human influenza virus receptor specificity and variant selection. J. Virol. 71:1997;3357-3362.
9. Katz J.M., Naeve C.W., Webster R.G. Host cell-mediated variation in H3N2 influenza viruses. Virology. 156:1987;386-395.
10. Katz J.M., Wang M., Webster R.G. Direct sequencing of the HA gene of influenza (H3N2) virus in original clinical samples reveals sequence identity with mammalian cell-grown virus. J. Virol. 64:1990;1808-1811.
11. Krizanova O., Rathova V. Serum inhibitors of myxoviruses. Curr. Top. Microbiol. Immunol. 47:1969;125-151.
12. Palmer D.F., Coleman M.T., Dowdle W.R., Schild G.C. Advanced laboratory techniques for influenza diagnosis. Immunol. Ser. 6:1975;51-52.
13. Pritchett T.J., Paulson J.C. Basis for the potent inhibition of influenza virus infection by equine and guinea pig α2-macroglobulin. J. Biol. Chem. 264:1989;9850-9858.
14. Reed L.J., Muench H.A. Simple method of estimating fifty per cent endpoints. Am. J. Hyg. 27:1938;493-497.
15. Robertson J.S., Nicolson C., Bootman J.S., Major D., Robertson E.W., Wood J.M. Sequence analysis of the haemagglutinin (HA) of influenza A (HlNl) viruses present in clinical material and comparison with the HA of laboratory-derived virus. J. Gen. Virol. 72:1991;2671-2677.
16. Rogers G.N., Paulson J.C. Receptor determinants of human and animal influenza virus isolates: differences in receptor specificity of the H3 hemagglutinin teased on species of origin. Virology. 127:1983;361-373.
17. Rogers G.N., Paulson J.C., Daniels R.S., Skehel J.J., Wilson I.A., Wiley D.C. Single amino acid substitutions in influenza haemagglutinin change receptor binding specificity. Nature. 304:1983;76-78.
18. Rogers G.N., Pritchett T.J., Lane J.L., Paulson J.C. Differential sensitivity of human, avian, and equine influenza A viruses to a glycoprotein inhibitor of infection: selection of receptor specific variants. Virology. 131:1983;394-408.
19. Ryan-Poirier K.A., Kawaoka Y. Distinct glycoprotein inhibitors of influenza A virus in different animal sera. J. Virol. 65:1991;389-395.
20. Ryan-Poirier K.A., Kawaoka Y. α2-Macroglobulin is the major neutralizing inhibitor of influenza A virus in pig serum. Virology. 193:1993;974-976.
21. Scholtissek C., Rohde W., Von Hoyningen V., Rott R. On the origin of the human influenza virus subtype H2N2 and H3N2. Virology. 87:1978;13-20.
22. Smith D.H., Byrn R.A., Marsters S.A., Gregory T., Groopman J.E., Capon D.J. Blocking of HIV-1 infectivity by a soluble, secreted form of the CD4 antigen. Science. 238:1987;1704-1707.
23. Suzuki Y., Nagao Y., Kato H., Matsumoto M., Nerome K., Nakajima K., Nobusawa E. Human influenza A virus hemagglutinin distinguishes sialyloligosaccharides in membrane associated gangliosides as its receptor which mediates the adsorption and fusion processes of virus infection. J. Biol. Chem. 261:1986;17057-17061.
24. Suzuki Y., Nakao T., Ito T., Watanabe N., Toda Y., Guiyun X., Suzuki T., Kobayashi T., Kimura Y., Yamada A., Sugawara K., Nishimura H., Kitame F., Nakamura K., Deya E., Kiso M., Hasegawa A. Structural determination of gangliosides that bind to influenza A, B, and C viruses by an improved binding assay: strain-specific receptor epitopes in sialo sugar chains. Virology. 189:1992;121-131.
25. Underwood P.A., Skehel J.J., Wiley D.C. Receptor-binding characteristics of monoclonal antibody-selected antigenic variants of influenza virus. J. Virol. 61:1987;206-208.
26. Verhoeyen M., Fang R., Min Jou W., Devos R., Huylebroeck D., Saman E., Fiers W. Antigenic drift between the haemagglutinin of the Hong Kong influenza strains A/Aichi/2/68 and A/Victoria/3/75. Nature (Lond.). 286:1980;771-776.
27. Weis W., 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.
28. Wilson I.A., Skehel J.J., Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3A resolution. Nature (Lond.). 289:1981;366-373.
29. Yewdell J.W., Caton A.J., Gerhard W. Selection of influenza A virus adsorptive mutants by growth in the presence of a mixture of monoclonal antihemagglutinin antibodies. J. Virol. 57:1986;623-628.