Ligands for Antibody to M-Protein are Exposed at the Surface of Influenza Virions: Effect of Proteolytic Treatment on their Activity

Université de Liège, Laboratoire de Microbiologie générale et médicale, Institut de Pathologie, B-4000, Liège, Belgium Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated conce...

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Bibliographic Details
Published in:Journal of general virology 1979-11, Vol.45 (2), p.283-289
Main Authors: Reginster, Monique, Joassin, Luc, Fontaine-Delcambe, Patricia
Format: Article
Language:English
Subjects:
Animals
Antibodies, Viral - immunology
Binding Sites, Antibody
Blood Proteins - immunology
Complement Fixation Tests
Hemagglutination Inhibition Tests
Immunoglobulins
Influenza A virus - drug effects
Influenza A virus - immunology
Neutralization Tests
Orthomyxoviridae - immunology
Peptide Hydrolases - pharmacology
Rabbits - immunology
Viral Proteins - immunology
Virion - immunology
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Summary:Université de Liège, Laboratoire de Microbiologie générale et médicale, Institut de Pathologie, B-4000, Liège, Belgium Antiserum to pure M-protein extracted from PR8 virions neutralized the infectivity and inhibited the haemagglutinating activity of various influenza A virions. It agglutinated concentrated suspensions of these virions and fixed complement in their presence. Antibodies to M-protein were readily absorbed by intact virions or by spikeless particles obtained after proteolytic treatment, giving clear evidence that M-protein is exposed at the surface of the virus envelope. The data suggest that when antibodies to M-protein occupy specific ligands exposed at the surface of the virion they interfere with sites critical for infectivity and haemagglutinating activity. Received 16 February 1979; accepted 2 May 1979.
ISSN:0022-1317
1465-2099
DOI:10.1099/0022-1317-45-2-283