Fusion Mediated by the HIV-1 Envelope Protein

McManus, Carrie M.; Doms, Robert W.

doi:10.1007/0-306-46824-7_12

Cited by 4 publications

(2 citation statements)

References 136 publications

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“…It is thought that after CD4 and subsequent coreceptor binding, the fusion peptide is inserted into the target cell membrane and then undergoes conformational changes in order to bring the viral and cellular lipid bilayers into proximity, allowing their external leaflets to merge, thereby forming a hemi-fusion intermediate. Next, an aqueous connection, termed the fusion pore, opens across the internal leaflets of the merged membranes and expands to form an open passage through which the viral core enters the cellular cytoplasm (for review, see (Colman and Lawrence 2003;Doms and Moore 2000;McManus and Doms 2000)). …”

Section: General Introductionmentioning

confidence: 99%

Early Events of HIV-1 Infection: Can Signaling be the Next Therapeutic Target?

Jones

Smyth

Pereira

et al. 2011

J Neuroimmune Pharmacol

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Intracellular signaling events are signposts of biological processes, which govern the direction and action of biological activities. Through millions of years of evolution, pathogens, such as viruses, have evolved to hijack host cell machinery to infect their targets and are therefore dependent on host cell signaling for replication. This review will detail our current understanding of the signaling events that are important for the early steps of HIV-1 replication. More specifically, the therapeutic potential of signaling events associated with chemokine coreceptors, virus entry, viral synapses, and post-entry processes will be discussed. We argue that these pathways may represent novel targets for antiviral therapy.

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Section: General Introductionmentioning

confidence: 99%

Early Events of HIV-1 Infection: Can Signaling be the Next Therapeutic Target?

Jones

Smyth

Pereira

et al. 2011

J Neuroimmune Pharmacol

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“…The natural infection cycle of this enveloped virus involves the fusion of the viral membrane with the host cell membrane upon entry and the envelopment of the viral capsid/core upon assembly leading to budding at the plasma membrane [ 1 , 2 ]. The envelope glycoproteins (Env) on the surface of HIV-1 facilitate infection by mediating the fusion between the viral and cellular membranes [ 3 ]. The trimeric Env glycoprotein complexes are made up of two subunits, the surface subunit gp120 and membrane-spanning subunit gp41 [ 4 , 5 ].…”

Section: Introductionmentioning

confidence: 99%

SERINC5-Mediated Restriction of HIV-1 Infectivity Correlates with Resistance to Cholesterol Extraction but Not with Lipid Order of Viral Membrane

Raghunath

Chen

Marin

et al. 2022

Viruses

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Serine incorporator 5 (SER5) is a protein that upon incorporation into virions inhibits HIV-1 infectivity by interfering with the ability of the Env glycoprotein to promote viral fusion. The mechanisms by which SER5 antagonizes HIV-1 fusion are not well understood. A recent study of SER5’s structure revealed a lipid-binding pocket, suggesting the ability to sequester lipids. This finding, along with the well-documented modulation of HIV-1 infectivity by viral lipids, especially cholesterol, prompted our examination of SER5′s effect on the general lipid order of the HIV-1 membrane. Pseudoviruses bearing the SER5-sensitive HXB2-Env and containing SER5 or SER2, a control protein that lacks antiviral activity, were analyzed using two distinct lipid-order probes. We show that SER5 incorporation does not noticeably affect the lipid order of pseudoviruses. Although viral cholesterol extraction reduces HIV-1 infectivity, SER5+ viruses are less sensitive to cholesterol extraction than the control samples. In contrast, the virus’ sensitivity to cholesterol oxidation was not affected by SER5 incorporation. The hydrolytic release of sphingomyelin-sequestered cholesterol had a minimal impact on the apparent resistance to cholesterol extraction. Based on these results, we propose that a subpopulation of more stable Env glycoproteins responsible for the residual infectivity of SER5+ viruses is less sensitive to the cholesterol content of the viral membrane.

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HIV-1 entry and how to block it

Brelot¹,

Alizon²

2001

AIDS

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Fusion Mediated by the HIV-1 Envelope Protein

Cited by 4 publications

References 136 publications

Early Events of HIV-1 Infection: Can Signaling be the Next Therapeutic Target?

Early Events of HIV-1 Infection: Can Signaling be the Next Therapeutic Target?

SERINC5-Mediated Restriction of HIV-1 Infectivity Correlates with Resistance to Cholesterol Extraction but Not with Lipid Order of Viral Membrane

HIV-1 entry and how to block it

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