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Specificity of anti-P25 antibodies produced against whole HIV-1 particles or soluble forms of the protein.
Mabrouk K; Benjouad A; Gluckman JC; Rochat H; Van Rietschoten J;
January 30, 1993
Mol Immunol. 1992 Nov;29(11):1309-18. Unique Identifier : AIDSLINE

Specificity of anti-p25 antibodies produced against either whole Human Immunodeficiency Virus type 1 (HIV-1) particles in humans and chimpanzees, or against soluble forms of the protein in chimpanzees and rabbits was analyzed by ELISA using a panel of 37 long (> or = 30 residues) or shorter (9-21 residues) overlapping peptides covering the entire p25 sequence. Antibodies elicited by intact virions presented similar reactivity patterns in HIV-1-infected humans and in HIV-1-infected or immunized chimpanzees and recognized only a limited region mostly the C-terminus of the molecule. Moreover, 8 of the human sera (36%), which nonetheless reacted with high titers and avidity with native p25, did not bind to any long or short peptide. These results suggest that the majority of antibodies elicited by viral particles are presumably directed to conformational epitopes. In contrast, antibodies raised against soluble forms of p25 could react against all long peptides but one (residues 211-245) and against some short peptides, indicating that most of p25 sequence may be immunogenic under these conditions. These results suggest that the reactivity spectrum of anti p25 antibodies is rather different if they are produced against intact HIV-1 particles or the soluble protein. They also indicate that it may be possible to manipulate the specificity of the humoral immune response by using either intact virions or purified proteins.

Acquired Immunodeficiency Syndrome/*IMMUNOLOGY Amino Acid Sequence Animal Antibodies, Viral/*IMMUNOLOGY Antibody Formation Antibody Specificity Chimpansee troglodytes Comparative Study Enzyme-Linked Immunosorbent Assay Gene Products, gag/*IMMUNOLOGY Human HIV-1/*IMMUNOLOGY Molecular Sequence Data Peptide Fragments Peptide Mapping Rabbits Radioimmunoassay Support, Non-U.S. Gov't JOURNAL ARTICLE