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Abstract:

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. © Copyright 2014, Mary Ann Liebert, Inc. 2014.

Registro:

Documento: Artículo
Título: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
Autor:González, S.A.; Falcón, J.I.; Affranchino, J.L.
Filiación:Laboratorio de Virología, CONICET-Facultad de Ciencias Exactas y Naturales, Universidad de Belgrano (UB), Villanueva 1324, C1426BMJ Buenos Aires, Argentina
Palabras clave:binding protein; chemokine receptor CXCR4; chimeric protein; glycoprotein E1; Influenza virus hemagglutinin; membrane protein; monoclonal antibody; plerixafor; virus envelope protein; article; binding assay; cell fusion; cell surface; controlled study; electrophoretic mobility; embryo; enzyme linked immunosorbent assay; Feline immunodeficiency virus; flow cytometry; human; human cell; Human immunodeficiency virus 1; immunoblotting; polyacrylamide gel electrophoresis; priority journal; protein expression; protein subunit; quantitative analysis; quantitative assay; site directed mutagenesis; surface property; T lymphocyte; target cell; virus entry; Western blotting; Animals; Cell Line; env Gene Products, Human Immunodeficiency Virus; Glycoproteins; HIV-1; Humans; Immunodeficiency Virus, Feline; Receptors, CXCR4; Receptors, HIV; Recombination, Genetic; Viral Envelope Proteins; Virus Attachment
Año:2014
Volumen:30
Número:3
Página de inicio:250
Página de fin:259
DOI: http://dx.doi.org/10.1089/aid.2013.0213
Título revista:AIDS Research and Human Retroviruses
Título revista abreviado:AIDS Res. Hum. Retroviruses
ISSN:08892229
CODEN:ARHRE
CAS:chemokine receptor CXCR4, 188900-71-2; plerixafor, 110078-46-1, 155148-31-5
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_08892229_v30_n3_p250_Gonzalez

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Citas:

---------- APA ----------
González, S.A., Falcón, J.I. & Affranchino, J.L. (2014) . 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. AIDS Research and Human Retroviruses, 30(3), 250-259.
http://dx.doi.org/10.1089/aid.2013.0213
---------- CHICAGO ----------
González, S.A., Falcón, J.I., Affranchino, J.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" . AIDS Research and Human Retroviruses 30, no. 3 (2014) : 250-259.
http://dx.doi.org/10.1089/aid.2013.0213
---------- MLA ----------
González, S.A., Falcón, J.I., Affranchino, J.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" . AIDS Research and Human Retroviruses, vol. 30, no. 3, 2014, pp. 250-259.
http://dx.doi.org/10.1089/aid.2013.0213
---------- VANCOUVER ----------
González, S.A., Falcón, J.I., Affranchino, J.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. AIDS Res. Hum. Retroviruses. 2014;30(3):250-259.
http://dx.doi.org/10.1089/aid.2013.0213