REACTIVITIES OF HIV-1 GAG-DERIVED PEPTIDES WITH ANTIBODIES OF HIV-1-INFECTED AND UNINFECTED HUMANS

HAIST, S and MARZ, J and WOLF, H and MODROW, S (1992) REACTIVITIES OF HIV-1 GAG-DERIVED PEPTIDES WITH ANTIBODIES OF HIV-1-INFECTED AND UNINFECTED HUMANS. AIDS RESEARCH AND HUMAN RETROVIRUSES, 8 (11). pp. 1909-1917. ISSN 0889-2229,

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Abstract

A group of 41 peptides, each 24 amino acids long and overlapping with each other by 12 residues spanning the total gag open reading frame (orf) of HIV-1 (HTLV-III(BH) 10 isolate) were synthesized using Fmoc chemistry. The purified compounds were used in ELISA assays and tested for antibody reactivities in sera of human HIV-1-infected and noninfected individuals. Sera of HIV humans showed reactivity against four defined regions, two in p 1 7, one in p24, and one in p 1 5. The values of these reactivities were elevated especially in serum samples of HIV- individuals showing cross-reaction with gag proteins on Western blot. Amino acid sequence comparison of HIV-1 gag proteins with those of human endogenous retroviruses (ERV K10, ERV 3) revealed significant similarities predominantly in the domains showing elevated antibody cross-reactions. The majority of sera from HIV-1+ individuals showed strong reactivities to the cross-reactive regions and to various other peptide sequences, a sequential epitope recognized by all HIV-1+ sera could, however, not be identified. The results suggest that human individuals may have immune reactions to endogenous retroviral protein sequences, which are enhanced by infections with HIV-1. Specific antibodies to HIV-1 gag proteins are probably mainly directed to tertiary structure defined epitopes formed by particle formation of the p24 monomers to the nucleocapsid.

Item Type: Article
Uncontrolled Keywords: HUMAN-IMMUNODEFICIENCY-VIRUS; CORE ANTIGENS; MONOCLONAL-ANTIBODIES; NUCLEOTIDE-SEQUENCE; LYMPHOTROPIC VIRUS; RNA TRANSCRIPTS; HUMAN-CELLS; PROTEIN; INFECTION; EPITOPES;
Depositing User: Dr. Gernot Deinzer
Last Modified: 19 Oct 2022 08:44
URI: https://pred.uni-regensburg.de/id/eprint/54292

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