skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion

Abstract

Cell fusion mediated by Epstein-Barr virus requires three conserved glycoproteins, gB and gHgL, but activation is cell type specific. B cell fusion requires interaction between MHC class II and a fourth virus glycoprotein, gp42, which complexes non-covalently with gHgL. Epithelial cell fusion requires interaction between gHgL and a novel epithelial cell coreceptor and is blocked by excess gp42. We show here that gp42 interacts directly with gH and that point mutations in the region of gH recognized by an antibody that differentially inhibits epithelial and B cell fusion significantly impact both the core fusion machinery and cell-specific events. Substitution of alanine for glycine at residue 594 completely abrogates fusion with either B cells or epithelial cells. Substitution of alanine for glutamic acid at residue 595 reduces fusion with epithelial cells, greatly enhances fusion with B cells and allows low levels of B cell fusion even in the absence of gL.

Authors:
 [1];  [1]
  1. Department of Microbiology and Immunology, Center for Molecular and Tumor Virology and Feist-Weiller Cancer Center, Louisiana State University Health Sciences Center, 1501 Kings Highway, Shreveport, LA 71130 (United States)
Publication Date:
OSTI Identifier:
20977036
Resource Type:
Journal Article
Journal Name:
Virology
Additional Journal Information:
Journal Volume: 363; Journal Issue: 1; Other Information: DOI: 10.1016/j.virol.2007.01.025; PII: S0042-6822(07)00056-6; Copyright (c) 2007 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0042-6822
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; ALANINES; ANTIBODIES; GENE MUTATIONS; GLUTAMIC ACID; GLYCINE; GLYCOPROTEINS; MUTAGENESIS; ONCOGENIC VIRUSES

Citation Formats

Liguo, Wu, and Hutt-Fletcher, Lindsey M. Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion. United States: N. p., 2007. Web.
Liguo, Wu, & Hutt-Fletcher, Lindsey M. Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion. United States.
Liguo, Wu, and Hutt-Fletcher, Lindsey M. 2007. "Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion". United States.
@article{osti_20977036,
title = {Point mutations in EBV gH that abrogate or differentially affect B cell and epithelial cell fusion},
author = {Liguo, Wu and Hutt-Fletcher, Lindsey M},
abstractNote = {Cell fusion mediated by Epstein-Barr virus requires three conserved glycoproteins, gB and gHgL, but activation is cell type specific. B cell fusion requires interaction between MHC class II and a fourth virus glycoprotein, gp42, which complexes non-covalently with gHgL. Epithelial cell fusion requires interaction between gHgL and a novel epithelial cell coreceptor and is blocked by excess gp42. We show here that gp42 interacts directly with gH and that point mutations in the region of gH recognized by an antibody that differentially inhibits epithelial and B cell fusion significantly impact both the core fusion machinery and cell-specific events. Substitution of alanine for glycine at residue 594 completely abrogates fusion with either B cells or epithelial cells. Substitution of alanine for glutamic acid at residue 595 reduces fusion with epithelial cells, greatly enhances fusion with B cells and allows low levels of B cell fusion even in the absence of gL.},
doi = {},
url = {https://www.osti.gov/biblio/20977036}, journal = {Virology},
issn = {0042-6822},
number = 1,
volume = 363,
place = {United States},
year = {Wed Jun 20 00:00:00 EDT 2007},
month = {Wed Jun 20 00:00:00 EDT 2007}
}