TY - JOUR
T1 - Porcine HveC, a member of the highly conserved HveC/nectin 1 family, is a functional alphaherpesvirus receptor
AU - Milne, Richard S.B.
AU - Connolly, Sarah A.
AU - Krummenacher, Claude
AU - Eisenberg, Roselyn J.
AU - Cohen, Gary H.
N1 - Funding Information:
We thank L. Enquist, P. Spear, and S. Weller for reagents and Chuck Whitbeck and Isabelle Baribaud for helpful advice. This work was supported by Public Health Service Grant AI-18289 to G.H.C. and R.J.E. from the National Institute of Allergy and Infectious Diseases and Grants NS-30606 and NS-36731 to R.J.E. and G.H.C. from the National Institute of Neurologic Diseases and Stroke. C.K. was supported by a fellowship (823A-053464) from the Swiss National Science Foundation. S.A.C. is a predoctoral trainee supported by Grant AI-07325 from the National Institute of Allergy and Infectious Diseases.
PY - 2001/3/15
Y1 - 2001/3/15
N2 - 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.
AB - 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.
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U2 - 10.1006/viro.2000.0798
DO - 10.1006/viro.2000.0798
M3 - Article
C2 - 11277703
AN - SCOPUS:0035866662
SN - 0042-6822
VL - 281
SP - 315
EP - 328
JO - Virology
JF - Virology
IS - 2
ER -