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

Tagliamonte M, Tornesello ML, Buonaguro FM, Buonaguro L - J Transl Med (2011)

Bottom Line: 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.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Lab, of Molecular Biology and Viral Oncogenesis & AIDS Reference Center, Istituto Nazionale Tumori Fond, G, Pascale, Naples, Italy.

ABSTRACT
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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Related in: MedlinePlus

Schematic representation of HIV-1 gp120 binding to cellular receptor and coreceptors. The binding of HIV Envelope protein to CD4 receptor and chemokines coreceptors on the host cell surface is represented showing the gp120 in its monomeric form (A) and trimeric form as soluble (B) or bound to virus like particles (VLPs) (C).
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Figure 2: Schematic representation of HIV-1 gp120 binding to cellular receptor and coreceptors. The binding of HIV Envelope protein to CD4 receptor and chemokines coreceptors on the host cell surface is represented showing the gp120 in its monomeric form (A) and trimeric form as soluble (B) or bound to virus like particles (VLPs) (C).

Mentions: Considering the biological and structural properties of HIV gp140 trimers presented on the VLP surface, they can be even more strategic for binding studies, providing an invaluable tool for evaluating and dissecting the whole virus-host cell interaction leading to and ending with membrane fusion [163,164] (Fig. 2).


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

Tagliamonte M, Tornesello ML, Buonaguro FM, Buonaguro L - J Transl Med (2011)

Schematic representation of HIV-1 gp120 binding to cellular receptor and coreceptors. The binding of HIV Envelope protein to CD4 receptor and chemokines coreceptors on the host cell surface is represented showing the gp120 in its monomeric form (A) and trimeric form as soluble (B) or bound to virus like particles (VLPs) (C).
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3105500&req=5

Figure 2: Schematic representation of HIV-1 gp120 binding to cellular receptor and coreceptors. The binding of HIV Envelope protein to CD4 receptor and chemokines coreceptors on the host cell surface is represented showing the gp120 in its monomeric form (A) and trimeric form as soluble (B) or bound to virus like particles (VLPs) (C).
Mentions: Considering the biological and structural properties of HIV gp140 trimers presented on the VLP surface, they can be even more strategic for binding studies, providing an invaluable tool for evaluating and dissecting the whole virus-host cell interaction leading to and ending with membrane fusion [163,164] (Fig. 2).

Bottom Line: 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.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Lab, of Molecular Biology and Viral Oncogenesis & AIDS Reference Center, Istituto Nazionale Tumori Fond, G, Pascale, Naples, Italy.

ABSTRACT
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.

Show MeSH
Related in: MedlinePlus