Premium
Fine Molecular Specificity of Linear and Assembled Antibody Binding Sites in HIV‐1 p24
Author(s) -
HAAHEIM L. R.,
MASKELL J. P,
MASCAGNI P.,
COATES A. R. M.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb01555.x
Subject(s) - antibody , human immunodeficiency virus (hiv) , computational biology , chemistry , virology , biology , immunology
A set of seven murine monoclonal antibodies were generated against a chemically synthesized 11‐kDa 104‐mer peptide covering the C‐terminal residues 270‐373 of the p24g.it; protein (HIV‐I BRU strain). All monoclonal antibodies recognized HIV‐ LMN infected MOLT? cells by fluorescence und gave positive Western blot signals with viral gag peptides [p55 and/or p24), Oligopeptide binding regions were located with competitive enzyme‐linked immunosorbent assays. Detailed epitope scanning analyses (the Geysen technique) were performed by serological testing of the monoclonal antibodies against 99 overlapping hexapeptides which corresponded to the entire 104‐mer region. The antibodies bound to p24 peptide sequences located within the 275 2y3 and 351 36S regions. One antibody (LH 104‐B) which reacted with residues 357‐362 bound lo p55 alone. In contrast another antibody (LH 104–1). which recognized the residues 358–363. i.e. with five out of six residues in common with antibody LIIKM‐B for its epitope region, reacted exclusively with p24. At least two of the antibodies (LH104‐C and ‐A) which bound to p24 alone, apparently recognized conformational epitopes, They gave positive reactions with the regions 288—293/351–356 and 284–289/351–356, respectively. This work shows that chemical synthesis of large peptides is a viable alternative approach to immunochemical studies of viral proteins.