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Journal of Virology, September 2003, p. 9695-9699, Vol. 77, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.17.9695-9699.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Differences in the N Termini of Herpes Simplex Virus Type 1 and 2 gDs That Influence Functional Interactions with the Human Entry Receptor Nectin-2 and an Entry Receptor Expressed in Chinese Hamster Ovary Cells

Anna Zago and Patricia G. Spear*

Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611

Received 12 March 2003/ Accepted 3 June 2003

Amino acid differences at seven positions in the N termini of the glycoproteins D (gDs) specified by herpes simplex virus type 1 (HSV-1) and HSV-2 are largely responsible for the significantly higher cell fusion activity of HSV-2 gD with Chinese hamster ovary cells expressing human nectin-2 or only an endogenous hamster receptor.

* Corresponding author. Mailing address: Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Mail Code S213, 320 East Superior St., Chicago, IL 60611. Phone: (312) 503-8230. Fax: (312) 503-1339. E-mail: p-spear{at}northwestern.edu.

Journal of Virology, September 2003, p. 9695-9699, Vol. 77, No. 17
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.17.9695-9699.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

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  • Fusco, D., Forghieri, C., Campadelli-Fiume, G. (2005). The pro-fusion domain of herpes simplex virus glycoprotein D (gD) interacts with the gD N terminus and is displaced by soluble forms of viral receptors. Proc. Natl. Acad. Sci. USA 102: 9323-9328 [Abstract] [Full Text]  
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