Herpes Research Today is a free monthly online journal that collates and summarizes the latest research about Herpes, including details on herpes simplex virus (hsv), genital, oral, symptoms, treatment.

Deletion of the second immunoglobulin-like domain of nectin-1 alters its intracellular processing and localization and ability to mediate entry of herpes simplex virus.

Struyf F, Plate AE, Spear PG

Northwestern University, The Feinberg School of Medicine, Department of Microbiology and Immunology, Searle 6-447, 320 E. Superior St., Chicago, IL 60611, USA.

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-Delta2) to examine the role of the second Ig-like domain in HSV entry. Nectin-1-Delta2 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-Delta2 to mediate HSV entry probably resulted from its failure to be transported to a membrane targeted by HSV for viral entry.

Published 25 February 2005 in J Virol, 79(6): 3841-5.
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