Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4

Feline immunodeficiency virus (FIV) and the T cell-tropic strains of human immunodeficiency virus type 1 (HIV-1) share the use of the chemokine receptor CXCR4 for cell entry. To study this process further we developed a cell surface binding assay based on the expression of a soluble version of the F...

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Autores principales: González, Silvia A., Falcón, Juan I., Affranchino, José L.
Formato: Artículo
Lenguaje:Inglés
Publicado: Universidad de Belgrano - Facultad de Ciencias Exactas y Naturales - Proyectos de Investigación 2014
Materias:
Feline Immunodeficiency Virus
Virus de la inmunodeficiencia felina
Chimeric Surface Protein
Proteína de superficie quimérico
Envelope Glycoprotein
glicoproteína de la envoltura
Acceso en línea:http://repositorio.ub.edu.ar/handle/123456789/2716
Aporte de:
Repositorio Institucional - Universidad de Belgrano (UB) de Universidad de Belgrano
id I36-R142-123456789-2716
record_format dspace
institution Universidad de Belgrano
institution_str I-36
repository_str R-142
collection Repositorio Institucional - Universidad de Belgrano (UB)
language Inglés
topic Feline Immunodeficiency Virus
Virus de la inmunodeficiencia felina
Chimeric Surface Protein
Proteína de superficie quimérico
Envelope Glycoprotein
glicoproteína de la envoltura
spellingShingle Feline Immunodeficiency Virus
Virus de la inmunodeficiencia felina
Chimeric Surface Protein
Proteína de superficie quimérico
Envelope Glycoprotein
glicoproteína de la envoltura
González, Silvia A.
Falcón, Juan I.
Affranchino, José L.
Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4
topic_facet Feline Immunodeficiency Virus
Virus de la inmunodeficiencia felina
Chimeric Surface Protein
Proteína de superficie quimérico
Envelope Glycoprotein
glicoproteína de la envoltura
description Feline immunodeficiency virus (FIV) and the T cell-tropic strains of human immunodeficiency virus type 1 (HIV-1) share the use of the chemokine receptor CXCR4 for cell entry. To study this process further we developed a cell surface binding assay based on the expression of a soluble version of the FIV SU C-terminally tagged with the influenza virus hemagglutinin epitope (HA). The specificity of the assay was demonstrated by the following evidence: (1) the SU-HA protein bound to HeLa cells that express CXCR4 but not to MDCK cells that lack this chemokine receptor; and (2) binding of the SU-HA to HeLa cells was blocked by incubation with the CXCR4 antagonist AMD3100 as well as with the anti-CXCR4 monoclonal antibody (MAb) 12G5. Deletion of the V3 region from the FIV SU glycoprotein abolished its ability to bind CXCR4-expressing cells. Remarkably, substitution of the V3 domain of the FIV SU by the equivalent region of the HIV-1 NL4-3 isolate resulted in efficient cell surface binding of the chimeric SU protein to CXCR4. Moreover, transfection of MDCK cells with a plasmid encoding human CXCR4 allowed the association of the chimeric SU-HA glycoprotein to the transfected cells. Interestingly, while cell binding of the chimeric FIV-HIV SU was inhibited by an anti-HIV-1 V3 MAb, its association with CXCR4 was found to be resistant to AMD3100. Of note, the chimeric FIV-HIV Env glycoprotein was capable of promoting CXCR4-dependent cell-to-cell fusion.
format Article
author González, Silvia A.
Falcón, Juan I.
Affranchino, José L.
author_facet González, Silvia A.
Falcón, Juan I.
Affranchino, José L.
author_sort González, Silvia A.
title Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4
title_short Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4
title_full Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4
title_fullStr Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4
title_full_unstemmed Replacement of the V3 Domain in the Surface Subunit of the Feline Immunodeficiency Virus Envelope Glycoprotein with the Equivalent Region of a T Cell-Tropic Human Immunodeficiency Virus Type 1 Results in a Chimeric Surface Protein That Efficiently Binds to CXCR4
title_sort replacement of the v3 domain in the surface subunit of the feline immunodeficiency virus envelope glycoprotein with the equivalent region of a t cell-tropic human immunodeficiency virus type 1 results in a chimeric surface protein that efficiently binds to cxcr4
publisher Universidad de Belgrano - Facultad de Ciencias Exactas y Naturales - Proyectos de Investigación
publishDate 2014
url http://repositorio.ub.edu.ar/handle/123456789/2716
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