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

Journal of Virology- United States

doi 10.1128/jvi.78.15.8015-8025.2004

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Abstract

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Date

August 1, 2004

Authors

Gabriella Campadelli-Fiume

Publisher

American Society for Microbiology

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Mutations Within the Pathogenic Region of Herpes Simplex Virus 1 gK Signal Sequences Alter Cell Surface Expression and Neurovirulence

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

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Amanote Research

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

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

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

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

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.

Mutations Within the Pathogenic Region of Herpes Simplex Virus 1 gK Signal Sequences Alter Cell Surface Expression and Neurovirulence

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

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