期刊
CELL
卷 132, 期 6, 页码 935-944出版社
CELL PRESS
DOI: 10.1016/j.cell.2008.01.043
关键词
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资金
- NIAID NIH HHS [R37 AI036293-14, R37 AI036293-11, R01 AI068129, R37 AI036293, AI36293, R37 AI036293-08, AI64520, P01 AI064520, R01 AI068129-07, R37 AI036293-09, R37 AI036293-10, R01 AI068129-08, R37 AI036293-15, R37 AI036293-07, R37 AI036293-12, R37 AI036293-06, R37 AI036293-13, R01 AI068129-06] Funding Source: Medline
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 PILR alpha become susceptible to HSV-1 infection. Furthermore, HSV-1 infection of human primary cells expressing both HVEM and PILR alpha was blocked by either anti-PILR alpha or anti-HVEM antibody. Our results demonstrate that cellular receptors for both gB and gD are required for HSV-1 infection and that PILR alpha 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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