Cross Talk Among the Glycoproteins Involved in Herpes Simplex Virus Entry and Fusion: The Interaction Between gB and gH/gL Does Not Necessarily Require gD

Journal of Virology- United States

doi 10.1128/jvi.01287-09

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Date

August 5, 2009

Authors

E. Avitabile

C. Forghieri

G. Campadelli-Fiume

Publisher

American Society for Microbiology

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Amanote Research

Cross Talk Among the Glycoproteins Involved in Herpes Simplex Virus Entry and Fusion: The Interaction Between gB and gH/gL Does Not Necessarily Require gD

Journal of Virology- United States

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Cascade of Events Governing Cell-Cell Fusion Induced by Herpes Simplex Virus Glycoproteins gD, gH/gL, and gB

Capturing the Herpes Simplex Virus Core Fusion Complex (gB-gH/gL) in an Acidic Environment

Substitution of Herpes Simplex Virus 1 Entry Glycoproteins With Those of Saimiriine Herpesvirus 1 Reveals a gD-gH/gL Functional Interaction and a Region Within the gD Profusion Domain That Is Critical for Fusion

Coexpression of UL20p and gK Inhibits Cell-Cell Fusion Mediated by Herpes Simplex Virus Glycoproteins gD, gH-gL, and Wild-Type gB or an Endocytosis-Defective gB Mutant and Downmodulates Their Cell Surface Expression

Novel Mutations in gB and gH Circumvent the Requirement for Known gD Receptors in Herpes Simplex Virus 1 Entry and Cell-To-Cell Spread

Amino Acid Differences in Glycoproteins B (gB), C (gC), H (gH) and L(gL) Are Associated With Enhanced Herpes Simplex Virus Type-1 (McKrae) Entry via the Paired Immunoglobulin-Like Type-2 Receptor Α

Mutations in the Amino Terminus of Herpes Simplex Virus Type 1 gL Can Reduce Cell-Cell Fusion Without Affecting gH/gL Trafficking

Immunogenicity of Herpes Simplex Virus Glycoproteins gC and gB and Their Role in Protective Immunity.

Surface Plasmon Resonance (SPR) Reveals Direct Binding of HSV Glycoproteins gH/gL to gD and Locates a gH/gL Binding Site on gD