1887

Abstract

To locate sites important for the structure and function of the haemagglutinin—neuraminidase glycoprotein (HN) of Sendai virus, the biological characteristics of antibody-selected escape mutants were correlated with mutations in the primary HN amino acid sequence. An escape mutant virus deficient only in neuraminidase function but with an HN content equal to that of the wild-type virus had an amino acid change at residue 184, implying that this position may be important for maintaining a functionally active enzymic site. In contrast, other escape mutant viruses with reductions in haemagglutination (eightfold) and neuraminidase activities (70 to 80%) had a sharply diminished HN content and substitutions either at residue 375, or double mutations at residues 279 and 461. The loss of biological activity with the concomitant loss of HN content suggests that these sites may be important for the processing and transport of HN, or in maintaining a structure resistant to proteolytic degradation; residue 451 was shown to have an undefined role in fusion activity. The monoclonal antibodies (MAbs) used to isolate the mutant viruses included those of the IgA and IgG classes and were divided into four operational groups based on their haemagglutination-inhibition pattern against the selected mutants. MAbs of the IgA class recognized epitopes overlapping with (group A) as well as epitopes distinct from (groups C and D) those recognized by the IgG class; group B included only IgG antibodies. The epitopes recognized by IgA antibodies may identify residues important for the secretory immune response to the HN molecule.

Loading

Article metrics loading...

/content/journal/jgv/10.1099/0022-1317-72-4-817
1991-04-01
2022-08-14
Loading full text...

Full text loading...

/deliver/fulltext/jgv/72/4/JV0720040817.html?itemId=/content/journal/jgv/10.1099/0022-1317-72-4-817&mimeType=html&fmt=ahah

References

  1. Aymard-Henry M. T., Coleman M. T., Dowdle W. R., Laver W. G., Schild G. C., Webster R. G. 1973; Influenza virus neuraminidase and neuraminidase-inhibition test procedures. Bulletin of the World Health Organization 48:199–202
    [Google Scholar]
  2. Bean W. J., Sriram G., Webster R. G. 1980; Electrophoretic analysis of iodine-labeled influenza virus RNA segments. Analytical Biochemistry 102:228–232
    [Google Scholar]
  3. Chanock R. M., Parrott R. H. 1965; Acute respiratory disease in infancy and childhood: present understanding and prospects for prevention. Pediatrics 36:21–39
    [Google Scholar]
  4. Colman P. M., Varghese J. N., Laver W. G. 1983; Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature, London 303:41–44
    [Google Scholar]
  5. Glezen W. P., Loda F. A., Clyde W. A. Jr, Senior R. J., Sheafer C. I., Conley W. G., Denny F. W. 1971; Epidemiologic patterns of acute lower respiratory disease of children in a pediatric group practice. Journal of Pediatrics 78:398–406
    [Google Scholar]
  6. Gorman W. L, Gill D. S, Scroggs R. A, Portner A. 1990; The hemagglutinin-neuraminidase glycoproteins of human parainfluenza virus type 1 and Sendai virus have high structure-function similarity with limited antigenic cross-reactivity. Virology 175:211–221
    [Google Scholar]
  7. Gorman W. L., Takahash T., Scroggs R. A., Portner A. 1991; Identification of amino acid positions associated with neuraminidase activity of the hemagglutinin-neuraminidase glycoproteins of Sendai virus. Virology 180:803–806
    [Google Scholar]
  8. Heath T. D., Martin F. J., Macher B. A. 1983; Association of ganglioside-protein conjugates into cell and Sendai virus: requirement for the HN subunit in viral fusion. Experimental Cell Research 149:163–175
    [Google Scholar]
  9. Homma M., Ohuchi M. 1973; Trypsin action on the growth of Sendai virus in tissue-culture cells. Structural difference of Sendai virus grown in eggs and tissue culture cells. Journal of Virology 12:1457–1465
    [Google Scholar]
  10. Iorio R. M., Syddall R. J., Glickman R. I., Riel A. M., Sheehan J. P., Bratt M. A. 1989; Identification of amino acid residues important to the neuraminidase activity of the HN glycoprotein of Newcastle disease virus. Virology 173:196–204
    [Google Scholar]
  11. Jorgensen E. D., Collins P. L., Lomedico P. T. 1987; Cloning and nucleotide sequence of Newcastle disease virus hemagglutinin-neuraminidase mRNA: identification of a putative sialic acid binding site. Virology 156:12–24
    [Google Scholar]
  12. Laemmli U. K. 1970; Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, London 227:680–685
    [Google Scholar]
  13. Mazanec M. B., Nedrud J. G., Lamm M. E. 1987; Immunoglobulin A monoclonal antibodies protect against Sendai virus. Journal of Virology 61:2624–2626
    [Google Scholar]
  14. Merz D. C., Wolinsky J. S. 1983; Conversion of non-fusing mumps virus infections to fusing infections by selective proteolysis of the HN glycoprotein. Virology 131:328–340
    [Google Scholar]
  15. Mills J., Vankirk J. E., Wright P. F., Chanock R. M. 1971; Experimental respiratory syncytial virus infection of adults: possible mechanisms of resistance to infection and illness. Journal of Immunology 107:123–130
    [Google Scholar]
  16. Miura N., Uchida T., Okada Y. 1982; HVJ (Sendai virus)-induced envelope fusion and cell fusion are blocked by monoclonal anti-HN protein antibody that does not inhibit hemagglutination activity of HVJ. Experimental Cell Research 141:409–420
    [Google Scholar]
  17. Nagai Y., Klenk H.-D. 1977; Activation of precursors to both glycoproteins of NDV by proteolytic cleavage. Virology 77:125–134
    [Google Scholar]
  18. Nagai Y., Klenk H.-D., Rott R. 1976; Proteolytic cleavage of the viral glycoproteins and its significance for the virulence of Newcastle disease virus. Virology 72:494–508
    [Google Scholar]
  19. Örvell C., Grandien M. 1982; The effects of monoclonal antibodies on biological activities of structural proteins of Sendai virus. Journal of Immunology 129:2779–2787
    [Google Scholar]
  20. Ozawa M., Asano A., Okada Y. 1979; Biological activities of glycoproteins of HVJ (Sendai virus) studied by reconstitution of hybrid envelope and by concanavalin A-mediated binding: a new function of HANA protein and structural requirement for F protein in hemolysis. Virology 99:197–202
    [Google Scholar]
  21. Portner A. 1981; The HN glycoprotein of Sendai virus: analysis of site(s) involved in hemagglutinating and neuraminidase activities. Virology 115:375–384
    [Google Scholar]
  22. Portner A. 1984; Monoclonal antibodies as probes of the antigenic structure and functions of Sendai virus glycoproteins. In Non-segmented Negative Strand Viruses pp 345–350 Edited by Bishop D. H. L., Compans R. W. Orlando: Academic Press;
    [Google Scholar]
  23. Portner A., Scroggs R. A., Metzger D. W. 1987; Distinct functions of antigenic sites of the HN glycoprotein of Sendai virus. Virology 158:61–68
    [Google Scholar]
  24. Sanger F., Nicklen S., Coulson A. R. 1977; DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences, U.S.A. 74:5463–5467
    [Google Scholar]
  25. Scheid A., Choppin P. W. 1974; Identification of biological activities of paramyxovirus glycoproteins: activation of cell fusion, hemolysis, and infectivity by proteolytic cleavage of an inactive precursor protein of Sendai virus. Virology 57:475–490
    [Google Scholar]
  26. Scheid A., Caliguiri L. A., Compans R. W., Choppin P. W. 1972; Isolation of paramyxovirus glycoproteins: association of both hemagglutination and neuraminidase activities with the larger SV5 glycoprotein. Virology 50:640–652
    [Google Scholar]
  27. Smith C. B., Purcell R. H., Bellanti M. D., Chanock R. M. 1966; Protective effect of antibody to parainfluenza type 1 virus. New England Journal of Medicine 275:1145–1152
    [Google Scholar]
  28. Thompson S. D., Portner A. 1987; Localization of functional sites on the hemagglutinin-neuraminidase glycoprotein of Sendai virus by sequence analysis of antigenic and temperature-sensitive mutants. Virology 160:1–8
    [Google Scholar]
  29. Tomasi T. B. Jr 1983; Mechanism of immune regulation at mucosal surfaces. Reviews of Infectious Diseases 5:S784–S792
    [Google Scholar]
  30. Tuffereau C., Portner A., Roux L. 1985; The role of haemagglutinin–neuraminidase glycoprotein cell surface expression in the survival of Sendai virus-infected BHK-21 cells. Journal of General Virology 66:2313–2318
    [Google Scholar]
  31. Uchida T., Ueda S., Nakanishi M., Miura N., Okada Y. 1984; HN glycoprotein of HVJ (Sendai virus) enhances the selective cytotoxicity of diphtheria toxin fragment A-containing liposomes on subacute sclerosing panencephalitis virus-infected cells. Experimental Cell Research 152:313–321
    [Google Scholar]
  32. Van Wyke K. L., Bean W. J. Jr, Webster R. G. 1981; Monoclonal antibodies to the influenza A virus nucleoprotein affecting RNA transcription. Journal of Virology 39:313–317
    [Google Scholar]
  33. Van Wyke Coelingh K. L., Winter C. C., Jorgensen E. D., Murphy B. R. 1987; Antigenic and structural properties of the hemagglutinin-neuraminidase glycoprotein of human parainfluenza type 3: sequence analysis of variants selected with monoclonal antibodies which inhibit infectivity, hemagglutination, and neura-minidase activities. Journal of Virology 61:1473–1477
    [Google Scholar]
  34. Waxham M. N., Aronowski J. 1988; Identification of amino acids involved in the sialidase activity of the mumps virus hemagglutinin-neuraminidase protein. Virology 167:226–232
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jgv/10.1099/0022-1317-72-4-817
Loading
/content/journal/jgv/10.1099/0022-1317-72-4-817
Loading

Data & Media loading...

Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error