Journal
VIROLOGY
Volume 281, Issue 2, Pages 315-328Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1006/viro.2000.0798
Keywords
HveC; HSV; PrV; glycoprotein D; virus entry; receptor
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Funding
- NIAID NIH HHS [AI-07325, AI-18289] Funding Source: Medline
- NINDS NIH HHS [NS-36731, NS-30606] Funding Source: Medline
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Human herpesvirus entry mediator C (HveC) is an alphaherpesvirus receptor which binds to virion glycoprotein D (gD). We identified porcine HveC and studied its interaction with pseudorabies virus (PrV) and herpes simplex virus type 1 (HSV-1) gD. Porcine and human HveC have 96% amino acid identity and HveC from African green monkey, mouse, hamster, and cow are similarly conserved. Porcine HveC mediates entry of HSV-1, HSV-2, PrV, and bovine herpesvirus type 1. Truncated soluble forms of HSV-1 and PrV gD bind competitively to porcine HveC. Biosensor analysis shows that PrV gD binds with a 10-fold higher affinity than HSV-1 gD. Monoclonal antibodies against human HveC recognize the porcine homologue and can block gD binding and entry of HSV-1 and PrV. Porcine HveC is functionally indistinguishable from human HveC. Our results are consistent with the suggestion that HveC is a pan-alphaherpesvirus receptor that interacts with a conserved structural domain of gD. (C) 2001 Academic Press.
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