HIV Entry and Its Inhibition

  title={HIV Entry and Its Inhibition},
  author={David C. Chan and Peter S. Kim},

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HIV-1 Entry and Membrane Fusion Inhibitors

The structural biology of HIV-1 Env and its complexes with the cellular receptors has provided a structural basis for the rational design of fusion inhibitors as potential antiviral therapeutics and related therapeutic strategies to block viral entry are discussed.

Escape from Human Immunodeficiency Virus Type 1 (HIV-1) Entry Inhibitors

A broad overview of entry inhibitor resistance mechanisms that inform the understanding of HIV entry and the design of new inhibitors and vaccines is provided.

Molecular Mechanism of HIV-1 Entry.

Recent Progress in the Development of HIV-1 Entry Inhibitors: From Small Molecules to Potent Anti-HIV Agents.

This review article specifically focuses on the recent progress in the development of small-molecule HIV-1 entry inhibitors and incorporates important aspects of their structural modification that lead to the discovery of new molecular scaffolds with more potency.

Cellular Pathways for Productive HIV-1 Entry and Molecular Mechanisms of its Inhibition.

The results from the study characterizing single-cycle replicative, fluorescentlylabeled HIV-1 give better understanding of HIV-2 and interpretation of data when using virions for further mechanistic studies, and suggest that endocytosis is likely to be the pathway for productive viral entry.

HIV-1 Glycoprotein Immunogenicity

The Human Immunodeficiency Virus type 1 (HIV-1) is a C-type enveloped retrovirus (classification based on morphology of retroviruses electron microscopy) of the Retroviridae family. It’s consisting

Galectin-1 and HIV-1 Infection.

Fusion mediated by the HIV-1 envelope protein.

Human immunodeficiency virus (HIV), the causative agent of acquired immune deficiency syndrome (AIDS), is a particularly well studied retrovirus and is the subject of this chapter.

Subunit Stoichiometry of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers during Virus Entry into Host Cells

The results assist the understanding of the mechanisms whereby the HIV-1 envelope glycoproteins mediate virus entry and membrane fusion and guide attempts to inhibit these processes.



Determinants of Human Immunodeficiency Virus Type 1 Resistance to gp41-Derived Inhibitory Peptides

Direct binding of DP178 to recombinant protein and synthetic peptide analogs containing the wild-type and mutant heptad repeat sequences revealed a strong correlation between DP178 binding and the biological sensitivity of the corresponding virus isolates to DP178.

Inhibition of HIV type 1 infectivity by constrained alpha-helical peptides: implications for the viral fusion mechanism.

  • J. JudiceJ. Tom R. Mcdowell
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
The results provide a direct link between the inhibition of HIV-1 infectivity by these peptides and the x-ray structures, and suggest that the conformation of gp41 observed by crystallography represents the fusogenic state.

Capture of an early fusion-active conformation of HIV-1 gp41

Using an inhibitory synthetic peptide from HIV-1 gp41, DP-178 binds gp41 and inhibits Env-mediated membrane fusion after gp120 interacts with cellular receptors, indicating that conformational changes involving the coiled coil domain of gp41 are required for entry.

A trimeric structural domain of the HIV-1 transmembrane glycoprotein

A stable, proteinase-resistant structure comprising two peptides, N-51 and C-43, derived from a recombinant protein fragment of the gp41 ectodomain is identified, suggesting that this α-helical, trimeric complex is the core of the fusion-competent state of the HIV-1 envelope.

Chemokine Receptors: Keys to AIDS Pathogenesis?

HIV vaccines: where we are and where we are going

Dilation of the Human Immunodeficiency Virus–1 Envelope Glycoprotein Fusion Pore Revealed by the Inhibitory Action of a Synthetic Peptide from gp41

The differences detected in lipid mixing versus contents mixing are maintained up to 6 h of coculture of gp120-41–expressing cells with target cells, indicating that DP178 can “clamp” the fusion complex in the lipid mixing intermediate for very long time periods.

HIV vaccines: Viral envelope fails to deliver?

In a trial of 18 people, all became infected with HIV-1 and those who had received the vaccine did not seem to deal with the infection any differently than unvaccinated patients.

Lack of induction of antibodies specific for conserved, discontinuous epitopes of HIV-1 envelope glycoprotein by candidate AIDS vaccines.

Data indicate a restriction of the immune response to linear, conserved epitopes poorly accessible on both monomeric and cell-surface expressed oligomeric gp120/gp41 and a lack of Abs specific for conformational epitopes conserved across divergent HIV-1 strains.

Atomic structure of the ectodomain from HIV-1 gp41

X-ray crystallography determines the structure of the protease-resistant part of a gp41 ectodomain solubilized with a trimeric GCN4 coiled coil in place of the amino-terminal fusion peptide, and suggests a common mechanism for initiating fusion.