PILRalpha is a Herpes Simplex Virus-1 Entry Coreceptor That Associates with Glycoprotein B

Overview

Journal Cell

Publisher Cell Press

Specialty Cell Biology

Date 2008 Mar 25

PMID 18358807

Citations 185

Authors

Takeshi Satoh

Jun Arii

Tadahiro Suenaga

Jing Wang

Amane Kogure

Junji Uehori

Noriko Arase

Ikuo Shiratori

Shinya Tanaka

Yasushi Kawaguchi

Patricia G Spear

Lewis L Lanier

Hisashi Arase

Affiliations

Soon will be listed here.

Abstract

Glycoprotein B (gB) is one of the essential components for infection by herpes simplex virus-1 (HSV-1). Although several cellular receptors that associate with glycoprotein D (gD), such as herpes virus entry mediator (HVEM) and Nectin-1, have been identified, specific molecules that mediate HSV-1 infection by associating with gB have not been elucidated. Here, we found that paired immunoglobulin-like type 2 receptor (PILR) alpha associates with gB, and cells transduced with PILRalpha become susceptible to HSV-1 infection. Furthermore, HSV-1 infection of human primary cells expressing both HVEM and PILRalpha was blocked by either anti-PILRalpha or anti-HVEM antibody. Our results demonstrate that cellular receptors for both gB and gD are required for HSV-1 infection and that PILRalpha plays an important role in HSV-1 infection as a coreceptor that associates with gB. These findings uncover a crucial aspect of the mechanism underlying HSV-1 infection.

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