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PMID: 7519220 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The majority of neutralizing Abs in HIV-1-infected patients recognize linear V3 loop sequences. Studies using HIV-1MN multiple antigenic peptides.

Journal of immunology (Baltimore, Md. : 1950) ·Vol. 153 ·No. 4 ·1994-08-15 ·Pages 1895-904

Vogel T, Kurth R, Norley S

Abstract

Multiple antigenic peptides (MAP) comprising eight synthetic peptides corresponding to the V3 loop of HIV-1MN or HIV-1IIIB linked to a lysine core were used to characterize the humoral Ab response of HIV-1-infected patients against this domain. One hundred percent of the tested sera from HIV-1-infected European patients reacted significantly with the HIV-1MN V3 loop MAP. Most, but not all, sera also reacted against the HIV-1IIIB V3 loop MAP, albeit with low titers. The in vitro neutralization capacity of the patients' sera against HIV-1MN or HIV-1IIIB infection were tested. All sera showed significant neutralizing titers against HIV-1MN, in comparison with the low (when detectable) neutralizing titers against HIV-1IIIB. Competition assays revealed that the majority of HIV-1MN-neutralizing Abs in patients' sera react with the V3 loop peptides. Only a small fraction of the total neutralizing capacity, presumably specific for other neutralizing epitopes, could not be adsorbed with HIV-1MN V3 loop peptides. The V3 loop peptides could also compete for the binding of Abs in patients' sera mediating Ab-dependent cellular cytotoxicity (ADCC) of HIV-1MN infected cells, inhibiting 30 to 80% of the ADCC activity. Finally, the HIV-1MN V3 loop MAP, when used as immunogen in the presence of RIBI adjuvant without a carrier protein, elicited Abs able to neutralize HIV-1MN (but not HIV-1IIIB) and to initiate ADCC of HIV-1MN-infected cells. This neutralizing and ADCC activity, mediated by V3MN-specific rabbit Abs, could be totally absorbed by V3MN loop peptides.

MeSH Terms
Amino Acid Sequence Antibody Specificity Antibody-Dependent Cell Cytotoxicity/immunology Epitopes HIV Antibodies/immunology HIV Envelope Protein gp120/immunology HIV Infections/immunology HIV-1/immunology Humans Molecular Sequence Data Neutralization Tests Peptide Fragments/immunology Peptides/chemistry,immunology
Chemicals
Epitopes HIV Antibodies HIV Envelope Protein gp120 HIV envelope protein gp120 (305-321) Peptide Fragments Peptides
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Vogel T
Paul Ehrlich Institute, Langen, Germany.
Kurth R
Norley S
Article Info
Journal
Journal of immunology (Baltimore, Md. : 1950)
Abbr.
J Immunol
ISSN
0022-1767
Published
1994-08-15
Pages
1895-904
Language
English
Region
United States
NLM ID
2985117R
Subset
IM
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