title: The soluble amino-terminal region of HVEM mediates efficient herpes simplex virus type 1 infection of gD receptor-negative cells.
abstract: BACKGROUND
  Previous studies from our own and other labs reported the surprising finding that the soluble V domain of the herpes simplex virus type 1 (HSV-1) entry receptor nectin-1 can both block HSV infection of receptor-bearing cells and mediate infection of receptor-deficient cells. Here we show that this property is not unique to nectin-1. We generated a pair of truncated, soluble forms of the other major HSV-1 entry receptor, herpes virus entry mediator (HVEM or HveA), and examined its effects on HSV-1 infection of receptor-deficient cells.
  
  
  RESULTS
  In cultures of CHO-K1 cells, sHveA102 comprising the two amino-terminal cysteine-rich pseudorepeats (CRPs) of HVEM enabled infection of greater than 80% of the cells at an MOI of 3, while sHveA162 comprising the complete ectodomain failed to mediate infection. Both sHveA102 and sHveA162 blocked infection of CHO-K1 cells stably expressing HVEM in a dose-dependent manner, indicating that both were capable of binding to viral gD. We found that sHveA102-mediated infection involves pH-independent endocytosis whereas HSV infection of HVEM-expressing CHO-K1 cells is known to be pH-dependent.
  
  
  CONCLUSIONS
  Our results suggest that the C-terminal portion of the soluble HVEM ectodomain inhibits gD activation and that this effect is neutralized in the full-length form of HVEM in normal infection.
authors.affiliation: Division of Radiation Oncology, Korea Institute of Radiological and Medical Sciences, 215-4, Gongneung-Dong, Nowon-Ku, Seoul 139-706, South Korea.
authors.forename: Hyunjung
authors.initials: H
authors.lastname: Baek
authors.forename: Jae Hong
authors.initials: JH
authors.lastname: Kim
authors.forename: Yoon Tae
authors.initials: YT
authors.lastname: Noh
authors.forename: Heechung
authors.initials: H
authors.lastname: Kwon
mesh_terms: D000818:Animals; D016466:CHO Cells; D002522:Chlorocebus aethiops; D006224:Cricetinae; D003412:Cricetulus; D018259:Herpesvirus 1, Human / Q000502:physiology*; D006801:Humans; D011485:Protein Binding; D053240:Receptors, Tumor Necrosis Factor, Member 14 / Q000378:metabolism*; D011991:Receptors, Virus / Q000378:metabolism*; D014709:Vero Cells; D014759:Viral Envelope Proteins / Q000378:metabolism*; D053586:Virus Internalization
chemical_list: D053240:Receptors, Tumor Necrosis Factor, Member 14; D011991:Receptors, Virus; C506028:TNFRSF14 protein, human; D014759:Viral Envelope Proteins; C077970:glycoprotein J, herpesvirus simiae