Cell-Surface Expression of a Mutated Epstein-Barr Virus Glycoprotein B Allows Fusion Independent of Other Viral Proteins

Epstein-Barr virus (EBV) infects human B lymphocytes and epithelial cells. We have compared the requirements for EBV glycoprotein-induced cell fusion between Chinese hamster ovary effecter cells and human B lymphoblasts or epithelial cells by using a virus-free cell fusion assay. EBV-encoded gB, gH,...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2004-12, Vol.101 (50), p.17474-17479
Main Authors: McShane, Marisa P., Longnecker, Richard, Kieff, Elliott D.
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antibodies - immunology
B lymphocytes
Biological Sciences
Cell Fusion
Cell Line
Cell lines
Cell Membrane - metabolism
Cells
Cricetinae
Epithelial cells
Epithelial Cells - cytology
Epithelial Cells - virology
Epstein Barr virus infections
Epstein-Barr virus
Fusion
Gene Expression
Glycoproteins
HeLa cells
Herpes viruses
Herpesvirus 4, Human - genetics
Herpesvirus 4, Human - physiology
Humans
Kidney cells
Membrane Fusion - physiology
Mutation
Mutation - genetics
Protein Structure, Tertiary
Proteins
Vero cells
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
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Summary:Epstein-Barr virus (EBV) infects human B lymphocytes and epithelial cells. We have compared the requirements for EBV glycoprotein-induced cell fusion between Chinese hamster ovary effecter cells and human B lymphoblasts or epithelial cells by using a virus-free cell fusion assay. EBV-encoded gB, gH, gL, and gp42 glycoproteins were required for efficient B cell fusion, whereas EBV gB, gH, and gL glycoproteins were required for Chinese hamster ovary effecter cell fusion with epithelial cell lines (AGS and SCC68) or the human embryonic kidney cell line 293-P. Fusion with human embryonic kidney 293-P cells was greater than fusion observed with B cells, indicative of an important role for cell contact. An antibody directed against the gH and gL complex inhibited epithelial cell fusion. Increased surface expression of gB alone as a result of truncations or point mutants in the carboxyl-terminal tail allowed gB-mediated fusion with epithelial cells, albeit at a lower level than with coexpression of gB, gH, and gL. Overall, gB appears to be the critical component for EBV glycoprotein-mediated cell fusion.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0404535101