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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

Dissection of sequential steps occurring after engagement of receptor and coreceptor by trimeric HIV envelope proteins.
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Related In: Results  -  Collection


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Figure 1: Dissection of sequential steps occurring after engagement of receptor and coreceptor by trimeric HIV envelope proteins.

Mentions: The first step is the exposure of the hydrophobic fusion peptide at the N terminus of gp41 which interacts with the target cell membrane, generating an intermediate, pre-hairpin state bridging the virus and cell membranes. The pre-hairpin then refolds into the stable, six-helix bundle core structure [38,39], releasing sufficient energy to overcome the kinetic barrier [40,41] and catalyzing the fusion of the two membranes [42]. Whether the fusion can occur with the free energy liberated during refolding of one or several trimers, is still debated [40,43] (Fig.1).


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)

Dissection of sequential steps occurring after engagement of receptor and coreceptor by trimeric HIV envelope proteins.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

Figure 1: Dissection of sequential steps occurring after engagement of receptor and coreceptor by trimeric HIV envelope proteins.
Mentions: The first step is the exposure of the hydrophobic fusion peptide at the N terminus of gp41 which interacts with the target cell membrane, generating an intermediate, pre-hairpin state bridging the virus and cell membranes. The pre-hairpin then refolds into the stable, six-helix bundle core structure [38,39], releasing sufficient energy to overcome the kinetic barrier [40,41] and catalyzing the fusion of the two membranes [42]. Whether the fusion can occur with the free energy liberated during refolding of one or several trimers, is still debated [40,43] (Fig.1).

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