期刊
JOURNAL OF VIROLOGY
卷 81, 期 17, 页码 9596-9600出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.00758-07
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资金
- NATIONAL CANCER INSTITUTE [R01CA117794, R01CA093444] Funding Source: NIH RePORTER
- NCI NIH HHS [CA93444, R01 CA093444, CA117794, R01 CA117794] Funding Source: Medline
To test the importance of the hydrophobic residues within the putative Epstein-Barr virus (EBV) glycoprotein B (gB) fusion loops in membrane fusion, WY (112-113) and WLIW193-196 were mutated into alanine, glutamic acid, or the analogous residues from herpes simplex virus type 1 (HSV-1) gB (HR and RVEA). All gB variants exhibited cell surface expression, demonstrating that the substitutions did not perturb gB trafficking. None of six gB variants was, however, capable of mediating fusion with either epithelial or B cells. These data demonstrate that the bulky and hydrophobic EBV loop residues, which differ from the more hydrophilic HSV-1 residues and appear more compatible with membrane insertion, are essential for EBV gB-dependent fusion.
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