Antigenic drift in the evolution of H1N1 influenza A viruses resulting from deletion of a single amino acid in the haemagglutinin gene

References

1. Aytay S., Schulze I. T. 1991; Single amino acid substitutions in the hemagglutinin can alter the host range and receptor binding properties of H1 strains of influenza A virus. J Virol 65:3022–3028
   [Google Scholar]
2. Baigent S. J., McCauley J. W. 2001; Glycosylation of haemagglutinin and stalk-length of neuraminidase combine to regulate the growth of avian influenza viruses in tissue culture. Virus Res 79:177–185 [CrossRef]
   [Google Scholar]
3. Baum L. G., Paulson J. C. 1991; The N2 neuraminidase of human influenza virus has acquired a substrate specificity complementary to the hemagglutinin receptor specificity. Virology 180:10–15 [CrossRef]
   [Google Scholar]
4. Bause E. 1983; Structural requirements of N-glycosylation of proteins. Studies with proline peptides as conformational probes. Biochem J 209:331–336
   [Google Scholar]
5. Bause E., Hettkamp H., Legler G. 1982; Conformational aspects of N-glycosylation of proteins. Studies with linear and cyclic peptides as probes. Biochem J 203:761–768
   [Google Scholar]
6. Caton A. J., Brownlee G. G., Yewdell J. W., Gerhard W. 1982; The antigenic structure of the influenza virus A/PR/8/34 hemagglutinin (H1 subtype). Cell 31:417–427 [CrossRef]
   [Google Scholar]
7. Cox R. J., Brokstad K. A. 1999; The postvaccination antibody response to influenza virus proteins. APMIS 107:289–296 [CrossRef]
   [Google Scholar]
8. Daniels R. S., Douglas A. R., Skehel J. J., Wiley D. C., Naeve C. W., Webster R. G., Rogers G. N., Paulson J. C. 1984; Antigenic analyses of influenza virus haemagglutinins with different receptor-binding specificities. Virology 138:174–177 [CrossRef]
   [Google Scholar]
9. Gamblin S. J., Haire L. F., Russell R. J., Stevens D. J., Xiao B., Ha Y., Vasisht N., Steinhauer D. A., Daniels R. S. other authors 2004; The structure and receptor binding properties of the 1918 influenza hemagglutinin. Science 303:1838–1842 [CrossRef]
   [Google Scholar]
10. Hoffmann E., Neumann G., Kawaoka Y., Hobom G., Webster R. G. 2000; A DNA transfection system for generation of influenza A virus from eight plasmids. Proc Natl Acad Sci U S A 97:6108–6113 [CrossRef]
    [Google Scholar]
11. Huang C. C., Couch G. S., Pettersen E. F., Ferrin T. E. 1996; Chimera: an extensible molecular modeling application constructed using standard components. In Pacific Symposium on Biocomputing ‘96 p– 724 Edited by Hunter L., Klein T. E. Singapore: World Scientific Publishing;
    [Google Scholar]
12. Kaverin N. V., Matrosovich M. N., Gambaryan A. S., Rudneva I. A., Shilov A. A., Varich N. L., Makarova N. V., Kropotkina E. A., Sinitsin B. V. 2000; Intergenic HA-NA interactions in influenza A virus: postreassortment substitutions of charged amino acid in the hemagglutinin of different subtypes. Virus Res 66:123–129 [CrossRef]
    [Google Scholar]
13. Kendal A. P., Pereira M. S., Skehel J. J. 1982; Hemagglutination inhibition. In Concepts and Procedures for Laboratory-Based Influenza Surveillance pp B17–B35 Edited by Kendal A. P., Pereira J., Skehel J. Atlanta, GA: Centers for Disease Control and Prevention;
    [Google Scholar]
14. Kumar S., Tamura K., Nei M. 2004; mega3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5:150–163 [CrossRef]
    [Google Scholar]
15. Lu B., Zhou H., Ye D., Kemble G., Jin H. 2005; Improvement of influenza A/Fujian/411/02 (H3N2) virus growth in embryonated chicken eggs by balancing the hemagglutinin and neuraminidase activities, using reverse genetics. J Virol 79:6763–6771 [CrossRef]
    [Google Scholar]
16. Maines T. R., Chen L. M., Matsuoka Y., Chen H., Rowe T., Ortin J., Falcon A., Nguyen T. H., Mai L. Q. other authors 2006; Lack of transmission of H5N1 avian-human reassortant influenza viruses in a ferret model. Proc Natl Acad Sci U S A 103:12121–12126 [CrossRef]
    [Google Scholar]
17. Matrosovich M. N., Gambaryan A. S., Teneberg S., Piskarev V. E., Yamnikova S. S., Lvov D. K., Robertson J. S., Karlsson K. A. 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 [CrossRef]
    [Google Scholar]
18. Matrosovich M., Tuzikov A., Bovin N., Gambaryan A., Klimov A., Castrucci M. R., Donatelli I., Kawaoka Y. 2000; Early alterations of the receptor-binding properties of H1, H2, and H3 avian influenza virus hemagglutinins after their introduction into mammals. J Virol 74:8502–8512 [CrossRef]
    [Google Scholar]
19. Nakajima S., Nishikawa F., Nakajima K. 2000; Comparison of the evolution of recent and late phase of old influenza A (H1N1) viruses. Microbiol Immunol 44:841–847 [CrossRef]
    [Google Scholar]
20. National Research Council. 2002 Guide for the Care and Use of Laboratory Animals Washington, DC: National Academy Press;
    [Google Scholar]
21. Nobusawa E., Aoyama T., Kato H., Suzuki Y., Tateno Y., Nakajima K. 1991; Comparison of complete amino acid sequences and receptor-binding properties among 13 serotypes of hemagglutinins of influenza A viruses. Virology 182:475–485 [CrossRef]
    [Google Scholar]
22. Raymond F. L., Caton A. J., Cox N. J., Kendal A. P., Brownlee G. G. 1986; The antigenicity and evolution of influenza H1 haemagglutinin, from 1950–1957 and 1977–1983: two pathways from one gene. Virology 148:275–287 [CrossRef]
    [Google Scholar]
23. Rocha E., Cox N. J., Black R. A., Harmon M. W., Harrison C. J., Kendal A. P. 1991; Antigenic and genetic variation in influenza A (H1N1) virus isolates recovered from a persistently infected immunodeficient child. J Virol 65:2340–2350
    [Google Scholar]
24. Sanner M. F., Olson A. J., Spehner J. C. 1996; Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38:305–320 [CrossRef]
    [Google Scholar]
25. Sato K., Morishita T., Nobusawa E., Tonegawa K., Sakae K., Nakajima S., Nakajima K. 2004; Amino-acid change on the antigenic region B1 of H3 haemagglutinin may be a trigger for the emergence of drift strain of influenza A virus. Epidemiol Infect 132:399–406 [CrossRef]
    [Google Scholar]
26. Shaw M. W., Xu X., Li Y., Normand S., Ueki R. T., Kunimoto G. Y., Hall H., Klimov A., Cox N. J., Subbarao K. 2002; Reappearance and global spread of variants of influenza B/Victoria/2/87 lineage viruses in the 2000–2001 and 2001–2002 seasons. Virology 303:1–8 [CrossRef]
    [Google Scholar]
27. Stohr K. 2002; Influenza–WHO cares. Lancet Infect Dis 2:517 [CrossRef]
    [Google Scholar]
28. Subbarao K., Chen H., Swayne D., Mingay L., Fodor E., Brownlee G., Xu X., Lu X., Katz J. other authors 2003; Evaluation of a genetically modified reassortant H5N1 influenza A virus vaccine candidate generated by plasmid-based reverse genetics. Virology 305:192–200 [CrossRef]
    [Google Scholar]
29. Wagner R., Wolff T., Herwig A., Pleschka S., Klenk H. D. 2000; Interdependence of hemagglutinin glycosylation and neuraminidase as regulators of influenza virus growth: a study by reverse genetics. J Virol 74:6316–6323 [CrossRef]
    [Google Scholar]
30. Weis W., Brown J. H., Cusack S., Paulson J. C., Skehel J. J., Wiley D. C. 1988; Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid. Nature 333:426–431 [CrossRef]
    [Google Scholar]
31. Wilson I. A., Cox N. J. 1990; Structural basis of immune recognition of influenza virus hemagglutinin. Annu Rev Immunol 8:737–771 [CrossRef]
    [Google Scholar]
32. Wilson I. A., Skehel J. J., Wiley D. C. 1981; Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 289:366–373 [CrossRef]
    [Google Scholar]
33. Xu X., Lindstrom S. E., Shaw M. W., Smith C. B., Hall H. E., Mungall B. A., Subbarao K., Cox N. J., Klimov A. 2004; Reassortment and evolution of current human influenza A and B viruses. Virus Res 103:55–60 [CrossRef]
    [Google Scholar]