The soluble amino-terminal region of HVEM mediates efficient herpes simplex virus type 1 infection of gD receptor-negative cells
- Authors
- Baek, Hyunjung; Kim, Jae Hong; Noh, Yoon Tae; Kwon, Heechung
- Issue Date
- 13-1월-2012
- Publisher
- BMC
- Keywords
- HSV-1; HVEM/HveA; gD; Soluble entry receptor
- Citation
- VIROLOGY JOURNAL, v.9
- Indexed
- SCIE
SCOPUS
- Journal Title
- VIROLOGY JOURNAL
- Volume
- 9
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/109082
- DOI
- 10.1186/1743-422X-9-15
- ISSN
- 1743-422X
- 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, sHveA(102) 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 sHveA(162) comprising the complete ectodomain failed to mediate infection. Both sHveA(102) and sHveA(162) 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 sHveA(102)-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.
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Collections - College of Life Sciences and Biotechnology > Division of Life Sciences > 1. Journal Articles
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