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© Research
Publication : Journal of virology

Hydrophobic residues that form putative fusion loops of Epstein-Barr virus glycoprotein B are critical for fusion activity.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Journal of virology - 01 Sep 2007

Backovic M, Jardetzky TS, Longnecker R,

Link to Pubmed [PMID] – 17553877

J Virol 2007 Sep; 81(17): 9596-600

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 WLIW(193-196) 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.

https://pubmed.ncbi.nlm.nih.gov/17553877