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Journal of Virology, September 2007, p. 9596-9600, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.00758-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Hydrophobic Residues That Form Putative Fusion Loops of Epstein-Barr Virus Glycoprotein B Are Critical for Fusion Activity{triangledown}

Marija Backovic,1 Theodore S. Jardetzky,1 and Richard Longnecker2*

Department of Biochemistry, Molecular Biology, and Cell Biology, Northwestern University, Evanston, Illinois 60208,1 Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, Chicago, Illinois 606112

Received 9 April 2007/ Accepted 30 May 2007

To test the importance of the hydrophobic residues within the putative Epstein-Barr virus (EBV) glycoprotein B (gB) fusion loops in membrane fusion, WY112-113 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.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, The Feinberg School of Medicine, Northwestern University, 303 E. Chicago Avenue, Chicago IL 60611. Phone: (312) 503-0467. Fax: (312) 503-1339. E-mail: r-longnecker{at}northwestern.edu

{triangledown} Published ahead of print on 6 June 2007.

Journal of Virology, September 2007, p. 9596-9600, Vol. 81, No. 17
0022-538X/07/$08.00+0     doi:10.1128/JVI.00758-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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