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Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies

The human immunodeficiency virus type 1 (HIV-1) external envelope glycoprotein gp120 presents conserved binding sites for binding to the primary virus receptor CD4 as well as the major HIV chemokine coreceptors, CCR5 and CXCR4. Concerted efforts are underway to understand the specific interactions b...

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Detalles Bibliográficos
Autores principales: Tagliamonte, Maria, Tornesello, Maria Lina, Buonaguro, Franco M, Buonaguro, Luigi
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3105500/
https://www.ncbi.nlm.nih.gov/pubmed/21284899
http://dx.doi.org/10.1186/1479-5876-9-S1-S1
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author Tagliamonte, Maria
Tornesello, Maria Lina
Buonaguro, Franco M
Buonaguro, Luigi
author_facet Tagliamonte, Maria
Tornesello, Maria Lina
Buonaguro, Franco M
Buonaguro, Luigi
author_sort Tagliamonte, Maria
collection PubMed
description The human immunodeficiency virus type 1 (HIV-1) external envelope glycoprotein gp120 presents conserved binding sites for binding to the primary virus receptor CD4 as well as the major HIV chemokine coreceptors, CCR5 and CXCR4. Concerted efforts are underway to understand the specific interactions between gp120 and coreceptors as well as their contribution to the subsequent membrane fusion process. The present review summarizes the current knowledge on this biological aspect, which represents one of the key and essential points of the HIV-host cell interplay and HIV life cycle. The relevance of conformational HIV-1 Envelope proteins presented on Virus-like Particles for appropriate assessment of this molecular interaction, is also discussed.
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spelling pubmed-31055002011-06-02 Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies Tagliamonte, Maria Tornesello, Maria Lina Buonaguro, Franco M Buonaguro, Luigi J Transl Med Review The human immunodeficiency virus type 1 (HIV-1) external envelope glycoprotein gp120 presents conserved binding sites for binding to the primary virus receptor CD4 as well as the major HIV chemokine coreceptors, CCR5 and CXCR4. Concerted efforts are underway to understand the specific interactions between gp120 and coreceptors as well as their contribution to the subsequent membrane fusion process. The present review summarizes the current knowledge on this biological aspect, which represents one of the key and essential points of the HIV-host cell interplay and HIV life cycle. The relevance of conformational HIV-1 Envelope proteins presented on Virus-like Particles for appropriate assessment of this molecular interaction, is also discussed. BioMed Central 2011-01-27 /pmc/articles/PMC3105500/ /pubmed/21284899 http://dx.doi.org/10.1186/1479-5876-9-S1-S1 Text en Copyright ©2011 Tagliamonte et al; licensee BioMed Central Ltd. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Tagliamonte, Maria
Tornesello, Maria Lina
Buonaguro, Franco M
Buonaguro, Luigi
Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies
title Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies
title_full Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies
title_fullStr Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies
title_full_unstemmed Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies
title_short Conformational HIV-1 Envelope on particulate structures: a tool for chemokine coreceptor binding studies
title_sort conformational hiv-1 envelope on particulate structures: a tool for chemokine coreceptor binding studies
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3105500/
https://www.ncbi.nlm.nih.gov/pubmed/21284899
http://dx.doi.org/10.1186/1479-5876-9-S1-S1
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