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Journal of Virology, March 2005, p. 3841-3845, Vol. 79, No. 6
0022-538X/05/$08.00+0 doi:10.1128/JVI.79.6.3841-3845.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Department of Microbiology and Immunology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois
Received 13 August 2004/ Accepted 26 October 2004
Nectin-1 is an immunoglobulin (Ig)-like entry receptor for herpes simplex virus (HSV). Like other nectins, nectin-1 forms dimers and mediates cell adhesion through interactions with other nectins. We constructed a second-domain deletion mutant of nectin-1 (nectin-1-
2) to examine the role of the second Ig-like domain in HSV entry. Nectin-1-
2 exhibited a severely reduced ability to mediate HSV entry and accumulated in the endoplasmic reticulum but retained the ability to interact with its HSV ligand, gD. The failure of nectin-1-
2 to mediate HSV entry probably resulted from its failure to be transported to a membrane targeted by HSV for viral entry.
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