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Comparison of antibody responses to different forms of HIV‐1 core antigens by epitope mapping
Author(s) -
Truong Catherine,
Brand Denys,
Mallet François,
Roingeard Philippe,
Barin Francis
Publication year - 1997
Publication title -
journal of medical virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 121
eISSN - 1096-9071
pISSN - 0146-6615
DOI - 10.1002/(sici)1096-9071(199703)51:3<145::aid-jmv2>3.0.co;2-6
Subject(s) - epitope , capsid , antibody , virology , virus , monoclonal antibody , epitope mapping , antigen , linear epitope , biology , microbiology and biotechnology , group specific antigen , chemistry , immunology
The specificity of antibodies to HIV‐1 capsid (p24CA) and matrix (p17MA) proteins, produced in mice against unprocessed immature assembled polyprotein (wild‐type p55 virus‐like particles or chimeric p55 virus‐like particles) or against the monomeric mature form (rp24CA/rp17MA), was analyzed by a microplate epitope mapping assay using a panel of synthetic peptides covering the entire p24CA plus p17MA sequences of HIV‐1 LAI . All immunized mice developed anti‐p24CA and anti‐p17MA antibodies, although the spectrum of specificity of these antibodies was different. Four p24 CA epitopes (residues 176–192, 201–218, 233–253, 285–304) were recognized by anti‐rp24CA/rp17MA antibodies, whereas one p17MA epitope (residues 11–25) and one p24CA epitope (residues 176–192) were constantly recognized by anti‐p55 virus‐like particle antibodies. These results suggest a different specificity pattern of anti‐p24CA and anti‐p17MA antibodies depending on whether they are produced against the soluble mature form or the immature assembled form of the gag proteins. J. Med. Virol. 51:145–151, 1997. © 1997 Wiley‐Liss, Inc.