(PDF) Mutations in the Amino Terminus of Herpes Simplex

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

Journal of Virology - United States

doi 10.1128/jvi.02383-13

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Date

October 23, 2013

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American Society for Microbiology

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

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

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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

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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

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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

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

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Contribution of Endocytic Motifs in the Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein B to Virus Replication and Cell-Cell Fusion

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Mapping the N-Terminal Residues of Epstein-Barr Virus Gp42 That Bind gH/gL by Using Fluorescence Polarization and Cell-Based Fusion Assays

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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

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

Journal of Virology - United States

doi 10.1128/jvi.02383-13

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

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

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

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

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

Contribution of Endocytic Motifs in the Cytoplasmic Tail of Herpes Simplex Virus Type 1 Glycoprotein B to Virus Replication and Cell-Cell Fusion

Mapping the N-Terminal Residues of Epstein-Barr Virus Gp42 That Bind gH/gL by Using Fluorescence Polarization and Cell-Based Fusion Assays

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