Open AccessMonoclonal antibodies to the hemagglutinin Sa antigenic site of a/pr/8/34 influenza virus distinguish biologic mutants of swine influenza virus.
Author(s) -
Edwin D. Kilbourne,
Walter Gerhard,
Charles W. Whitaker
Publication year - 1983
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.80.20.6399
Subject(s) - virology , hemagglutinin (influenza) , monoclonal antibody , biology , antigenic drift , influenza a virus , virus , epitope , antigenicity , antigen , orthomyxoviridae , mutant , antiserum , antibody , microbiology and biotechnology , immunology , gene , biochemistry
The dimorphic L and H hemagglutinin mutants of A/NJ/11/76(H1N1) (swine) influenza virus differ pleiotropically in their replication and virulence characteristics and in their antigenicity. L mutants replicate less well in chicken embryos and Madin-Darby canine kidney cells and are more infective for swine than are H mutants. L and H mutants are not antigenically distinguishable in cross-neutralization tests with homotypic antisera, but they can be identified with certain heterotypic heterogeneous antisera. The present studies demonstrate that two monoclonal antibodies (Sa-5 and Sa-13) to the Sa antigenic site of the hemagglutinin of A/PR/8/34H1N1 influenza virus react with mutants and viral reassortants containing the H hemagglutinin in radioimmunoassay, neutralization, and hemagglutination-inhibition tests but to a lesser degree or not at all with L mutants and reassortants. Conversely, monoclonal antibody (9C8) to the L mutant does not react with H mutants. L to H and H to L revertants, whether or not selected with monoclonal antibody, demonstrate concomitant change in biological and antigenic phenotype. Reactivity of H mutants with Sa monoclonal antibodies localizes the mutational site to a position on the hemagglutinin near the receptor binding site--a position in which single amino acid changes could readily influence both antigenic and biologic activity.