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The Journal of Immunology, 1979, 123: 825-832.
Copyright © 1979 by The American Association of Immunologists, Inc.
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Antigenic Determinants of Influenza Virus Hemagglutinin

III. Competitive Binding of Antibodies Directed Against "Common" and "Strain-Specific" Antigenic Determinants of A/Memphis/72 Hemagglutinin1

Robyn J. Russell, William H. Burns2, David O. White3, E. Margot Anders, Colin W. Ward4 and David C. Jackson

From the Department of Microbiology, University of Melbourne, Parkville, Victoria, 3052, Australia

Abstract

Immunoglobulin G directed against the hemagglutinin (HA) of influenza virus A/Memphis/102/72 (H3N2) was adsorbed with either of two related viruses, A/Port Chalmers/73 (H3N2) or A/Papua New Guinea/75 (H3N2) to fractionate the antibody into "strain-specific" ("specific") and "cross-reactive" ("common") populations. These IgG preparations were tested with use of a solidphase radioimmunoassay for their ability to compete with one another in binding to the antigenic determinants of Memphis HA. Their binding avidities were also determined.

It was found that anti-"specific" and anti-"common" IgG preparations competed with each other for the antigenic regions on Memphis HA. In addition, the assignment of anti-HA antibodies to either the anti-"specific" or the anti-"common" category was shown to be completely dependent on the particular virus used for adsorption; the more distantly related the strains being compared, the higher the proportion of antibodies that registered as anti-"specific", and the higher the average binding avidity of the anti-"specific" antibody population.

It is concluded that so-called anti-"specific" anti-"common" antibodies are directed against the same regions on the HA molecule. This does not necessarily imply that there is only a single antigenic determinant; there may be more than one, each inducing the production of a heterogeneous population of antibody molecules binding with different avidities to that determinant.

Footnotes

1 This work was supported by a grant to Professor David O. White from the National Health and Medical Research Council of Australia.

2 Present address: Johns Hopkins Hospital, Oncology Center, Baltimore, Maryland 21205.

3 To whom reprint requests should be addressed.

4 Division of Protein Chemistry, Commonwealth Scientific and Industrial Research Organization, Parkville, Victoria, 3052, Australia.






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