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PMID: 10482562 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The first immunoglobulin-like domain of HveC is sufficient to bind herpes simplex virus gD with full affinity, while the third domain is involved in oligomerization of HveC.

Journal of virology ·Vol. 73 ·No. 10 ·1999-10-00 ·Pages 8127-37

Krummenacher C, Rux AH, Whitbeck JC, Ponce-de-Leon M, Lou H, Baribaud I, Hou W, Zou C, Geraghty RJ, Spear PG, Eisenberg RJ, Cohen GH

Abstract

The human herpesvirus entry mediator C (HveC/PRR1) is a member of the immunoglobulin family used as a cellular receptor by the alphaherpesviruses herpes simplex virus (HSV), pseudorabies virus, and bovine herpesvirus type 1. We previously demonstrated direct binding of the purified HveC ectodomain to purified HSV type 1 (HSV-1) and HSV-2 glycoprotein D (gD). Here, using a baculovirus expression system, we constructed and purified truncated forms of the receptor containing one [HveC(143t)], two [HveC(245t)], or all three immunoglobulin-like domains [HveC(346t)] of the extracellular region. All three constructs were equally able to compete with HveC(346t) for gD binding. The variable domain bound to virions and blocked HSV infection as well as HveC(346t). Thus, all of the binding to the receptor occurs within the first immunoglobulin-like domain, or V-domain, of HveC. These data confirm and extend those of Cocchi et al. (F. Cocchi, M. Lopez, L. Menotti, M. Aoubala, P. Dubreuil, and G. Campadelli-Fiume, Proc. Natl. Acad. Sci. USA 95:15700, 1998). Using biosensor analysis, we measured the affinity of binding of gD from HSV strains KOS and rid1 to two forms of HveC. Soluble gDs from the KOS strain of HSV-1 had the same affinity for HveC(346t) and HveC(143t). The mutant gD(rid1t) had an increased affinity for HveC(346t) and HveC(143t) due to a faster rate of complex formation. Interestingly, we found that HveC(346t) was a tetramer in solution, whereas HveC(143t) and HveC(245t) formed dimers, suggesting a role for the third immunoglobulin-like domain of HveC in oligomerization. In addition, the stoichiometry between gD and HveC appeared to be influenced by the level of HveC oligomerization.

MeSH Terms
Animals Cattle Cell Line Dimerization Humans Immunoglobulins Protein Binding Receptors, Tumor Necrosis Factor Receptors, Tumor Necrosis Factor, Member 14 Receptors, Virus/chemistry,metabolism Simplexvirus/physiology Viral Envelope Proteins/metabolism Virus Replication
Chemicals
Immunoglobulins Receptors, Tumor Necrosis Factor Receptors, Tumor Necrosis Factor, Member 14 Receptors, Virus TNFRSF14 protein, human Viral Envelope Proteins glycoprotein D, Human herpesvirus 1
Authors & Affiliations
12 authors, click to expand affiliations / ORCID
Krummenacher C
Department of Microbiology, School of Dental Medicine, Philadelphia, Pennsylvania 19104, USA. krumm@biochem.dental.upenn.edu
Rux A H
Whitbeck J C
Ponce-de-Leon M
Lou H
Baribaud I
Hou W
Zou C
Geraghty R J
Spear P G
Eisenberg R J
Cohen G H
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Article Info
Journal
Journal of virology
Abbr.
J Virol
ISSN
0022-538X
DOI
10.1128/JVI.73.10.8127-8137.1999
Email
krumm@biochem.dental.upenn.edu
Published
1999-10-00
Pages
8127-37
Language
English
Region
United States
NLM ID
0113724
PMCID
PMC112829
Subset
IM
Grants
NINDS NIH HHS · P01 NS030606 · United States
NIAID NIH HHS · F32 AI009471 · United States
NIAID NIH HHS · AI-3629 · United States
NIAID NIH HHS · R01 AI018289 · United States
NIAID NIH HHS · AI-18289 · United States
NIAID NIH HHS · R37 AI018289 · United States
NIAID NIH HHS · R37 AI036293 · United States
NCI NIH HHS · P30 CA016520 · United States
NINDS NIH HHS · NS-30606 · United States
NCI NIH HHS · R01 CA021776 · United States
NIDDK NIH HHS · P30 DK019525 · United States
External Links
PubMed source DOI: 10.1128/JVI.73.10.8127-8137.1999 PMC Full Text View journal details
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