Adaptive Mutations in the V3 Loop of Gp120 Enhance Fusogenicity of Human Immunodeficiency Virus Type 1 and Enable Use of a CCR5 Coreceptor That Lacks the Amino-Terminal Sulfated Region

Journal of Virology- United States

doi 10.1128/jvi.75.24.12266-12278.2001

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December 15, 2001

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American Society for Microbiology

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Amanote Research

Adaptive Mutations in the V3 Loop of Gp120 Enhance Fusogenicity of Human Immunodeficiency Virus Type 1 and Enable Use of a CCR5 Coreceptor That Lacks the Amino-Terminal Sulfated Region

Journal of Virology- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

The Crown and Stem of the V3 Loop Play Distinct Roles in Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Interactions With the CCR5 Coreceptor

Effect of Amino Acid Substitution of the V3 and Bridging Sheet Residues in Human Immunodeficiency Virus Type 1 Subtype C Gp120 on CCR5 Utilization

Sensitivity of Human Immunodeficiency Virus Type 1 to the Fusion Inhibitor T-20 Is Modulated by Coreceptor Specificity Defined by the V3 Loop of Gp120

An Aptamer That Neutralizes R5 Strains of Human Immunodeficiency Virus Type 1 Blocks Gp120-Ccr5 Interaction

Short Communication: HIV-1 Variants That Use Mouse CCR5 Reveal Critical Interactions of Gp120's V3 Crown With CCR5 Extracellular Loop 1

Anti-Human Immunodeficiency Virus Type 1 Activity of an Oligocationic Compound Mediated via Gp120 V3 Interactions.

N-Linked Glycosylation of the V3 Loop and the Immunologically Silent Face of Gp120 Protects Human Immunodeficiency Virus Type 1 SF162 From Neutralization by Anti-Gp120 and Anti-Gp41 Antibodies

Convergent Evolution Within the V3 Loop Domain of Human Immunodeficiency Virus Type 1 in Association With Disease Progression.

Tyrosine-Sulfated Peptides Functionally Reconstitute a CCR5 Variant Lacking a Critical Amino-Terminal Region