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A single amino acid substitution in influenza hemagglutinin abrogates recognition by monoclonal antibody and a spectrum of subtype‐specific L3T4 + T cell clones
Author(s) -
Brian Thomas D.,
Skehel John J.,
Mills Kingston H. G.,
Graham Christine M.
Publication year - 1987
Publication title -
european journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.272
H-Index - 201
eISSN - 1521-4141
pISSN - 0014-2980
DOI - 10.1002/eji.1830170122
Subject(s) - biology , hemagglutinin (influenza) , monoclonal antibody , epitope , virology , mutant , virus , antigen , microbiology and biotechnology , antibody , peptide , influenza a virus , peptide sequence , gene , genetics , biochemistry
Abstract A fine specificity analysis of influenza hemagglutinin‐specific IA k ‐restricted T cell clones using natural virus variants of the H3N2 subtype, monoclonal antibody‐selected variants and a synthetic peptide corresponding to a variable region of the HA 1 polypeptide has provided insight on the structural basis for T cell recognition. A glycine to argine substitution at HA 1 135 abrogates recognition by a panel of T cell clones which, according to their reactivity for natural virus variants, have different antigenic specificities: three clones recognize a synthetic peptide (HA 1 residues 118–138) but fail to recognize the monoclonal antibody‐selected mutant (Gly 135 /Arg). There is no correlation, however, between differences in T cell specificity for the natural virus variants and HA 1 amino acid sequences in this region. Two further clones have a reduced proliferative response to mutant recognize a completely different spectrum of natural variants, and only one of these clones recognizes the synthetic peptide. We speculate that influenza hemagglutinin employs a common strategy during antigenic drift to evade antibody recognition and effective processing/presentation to subtype‐specific T cell clones.