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|dc.creator||Boudet, F. (Florence)||-|
|dc.creator||Lasarte, J.J. (Juan José)||-|
|dc.creator||Sarobe, P. (Pablo)||-|
|dc.creator||Borras-Cuesta, F. (Francisco)||-|
|dc.creator||Theze, J. (Jacques)||-|
|dc.identifier.citation||Boudet F, Lasarte JJ, Sarobe P, Borras-Cuesta F, Theze J. Fine analysis of immunoreactivity of V3 peptides: antibodies specific for V3 domain of laboratory HIV type 1 strains recognize multiple V3 sequences synthesized from field HIV type 1 isolates. AIDS Res Hum Retroviruses 1996 Dec 10;12(18):1671-1679.||es_ES|
|dc.description.abstract||Production of cross-reactive antibodies recognizing the V3 loop--that is, the principal neutralizing determinant (PND)--of various HIV-1 isolates is an important challenge in the development of passive immunotherapy or vaccinations against AIDS. We have produced two types of antibodies to the V3 domain of HIV-1: (1) antibodies against the HIV-1 MN laboratory strain generated in rabbits and (2) antibodies targeted to the HIV-1 LAI laboratory strain induced in chimpanzees. These antibodies were shown to be specific for HIV-1 subtype B. The cross-reactivity of these antibodies has been evaluated against a large panel of peptides representing different parts of the V3 loop. Seventy-five peptides, referred to as clinical peptides, were synthesized according to HIV-1 sequences recovered from PMBCs of 27 patients followed in three Parisian hospitals. Thirteen V3 peptides derived from 4 HIV-1 laboratory strains (MN, LAI, SF2, and RF) were also included in the study. The results show that both the amino-terminal and central parts of the V3 loop are immunogenic. The rabbit antibodies against the amino-terminal end of the PND proved to be highly cross-reactive against the clinical peptides. The anti-gp160 antibodies induced in one chimpanzee recognized a significant proportion of the panel of V3 clinical sequences. These antibodies cross-reacted mainly with the apex of the V3 loop. These data give some additional indications on the immunogenicity of the V3 loop and further demonstrate that extensive cross-reactivity of anti-V3 antibodies can be obtained on field HIV-1 isolates despite the high variability of the V3 loop amino acid sequence.||es_ES|
|dc.publisher||Mary Ann Liebert||es_ES|
|dc.subject||HIV Envelope Protein gp120/immunology||es_ES|
|dc.subject||HIV Envelope Protein gp160/immunology||es_ES|
|dc.title||Fine analysis of immunoreactivity of V3 peptides: antibodies specific for V3 domain of laboratory HIV type 1 strains recognize multiple V3 sequences synthesized from field HIV type 1 isolates||es_ES|
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