Induction of cytolytic T lymphocytes directed towards the V3 loop of the human immunodeficiency virus type 1 external glycoprotein gp120 by p55gag/V3 chimeric vaccinia viruses

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urn:nbn:de:bvb:355-epub-217612 Copy

Wagner, Ralf ; Böltz, T. ; Deml, Ludwig ; Modrow, Susanne ; Wolf, Hans J.

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Date of publication of this fulltext: 12 Aug 2011 08:57

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Details

Item type:	Article
Date:	1993
Institutions:	Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene
Identification Number:	Value Type 7687647 PubMed ID 10.1099/0022-1317-74-7-1261 DOI
Classification:	Notation Type AIDS Vaccines/isolation & purification MESH Amino Acid Sequence MESH Animals MESH Antibodies, Monoclonal MESH Base Sequence MESH Cell Line MESH Cytotoxicity, Immunologic MESH Epitopes/immunology MESH Gene Products, gag/isolation & purification MESH Genes, gag MESH HIV Envelope Protein gp120/isolation & purification MESH HIV-1/immunology MESH Mice MESH Mice, Inbred BALB C MESH Molecular Sequence Data MESH Oligodeoxyribonucleotides MESH Recombinant Fusion Proteins/isolation & purification MESH T-Lymphocytes, Cytotoxic/immunology MESH Vaccinia virus/isolation & purification MESH
Dewey Decimal Classification:	600 Technology > 610 Medical sciences Medicine
Status:	Published
Refereed:	Unknown
Created at the University of Regensburg:	Unknown
Item ID:	21761

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Abstract

T cell-mediated cytotoxicity may play an important role in controlling infection by human immunodeficiency virus (HIV). In order to study the ability of rationally designed antigens to induce cytolytic T lymphocytes (CTLs) we replaced stretches of 30 to 50 amino acids at the p17-MA/p24-CA cleavage site, within the p24-CA moiety and within the p6-LI portion of the HIV type 1 p55gag precursor by ...

Abstract

T cell-mediated cytotoxicity may play an important role in controlling infection by human immunodeficiency virus (HIV). In order to study the ability of rationally designed antigens to induce cytolytic T lymphocytes (CTLs) we replaced stretches of 30 to 50 amino acids at the p17-MA/p24-CA cleavage site, within the p24-CA moiety and within the p6-LI portion of the HIV type 1 p55gag precursor by the third variable domain (V3) of the external glycoprotein gp120. This site is known to be a target for CTL attack in mice and humans. The chimeric antigens were recombined into highly attenuated vaccinia viruses in order to investigate class I major histocompatibility complex (MHC)-restricted presentation of antigenic V3 peptides. Immunoprecipitation and Western blot analysis of the group-specific antigen (p55gag)/V3 chimeric proteins demonstrated significant differences in the accessibility of the V3 domain for a monoclonal antibody or polyclonal V3-specific antisera, depending on the position of the V3 loop within the p55gag carrier protein. Immunization of BALB/c mice with three variants of p55gag/V3 recombinant vaccinia virus, however, resulted in a comparable priming of CD4-CD8+ CTLs in vivo irrelevant of the position of the V3 loop within p55gag. Local conformational changes, including the V3 domain within the p55gag/V3 chimeras, did not demonstrate a significant effect on V3-specific lysis of the target cells when compared to the authentic gp120 envelope protein. Class I MHC-restricted CTLs induced by a V3 consensus sequence cross-reacted perfectly with the LAI strain-derived V3 loop sequence. These data indicate that the combination of selected epitopes (V3) with immunologically relevant complex carrier proteins (p55gag) can be accomplished without the loss of biological activity.

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Metadata last modified: 03 Jun 2018 02:52

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