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 102comprising 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 162comprising the complete ectodomain failed to mediate infection. Both sHveA 102and sHveA 162blocked 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.
| Original language | English |
|---|---|
| Article number | 15 |
| Journal | Virology Journal |
| Volume | 9 |
| DOIs | |
| Publication status | Published - 2012 Jan 16 |
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Keywords
- gD
- HSV-1
- HVEM/HveA
- Soluble entry receptor
ASJC Scopus subject areas
- Virology
- Infectious Diseases
Cite this
The soluble amino-terminal region of HVEM mediates efficient herpes simplex virus type 1 infection of gD receptor-negative cells. / Baek, Hyunjung; Kim, Jae-Hong; Noh, Yoon Tae; Kwon, Heechung.
In: Virology Journal, Vol. 9, 15, 16.01.2012.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - The soluble amino-terminal region of HVEM mediates efficient herpes simplex virus type 1 infection of gD receptor-negative cells
AU - Baek, Hyunjung
AU - Kim, Jae-Hong
AU - Noh, Yoon Tae
AU - Kwon, Heechung
PY - 2012/1/16
Y1 - 2012/1/16
N2 - 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 102comprising 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 162comprising the complete ectodomain failed to mediate infection. Both sHveA 102and sHveA 162blocked 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.
AB - 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 102comprising 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 162comprising the complete ectodomain failed to mediate infection. Both sHveA 102and sHveA 162blocked 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.
KW - gD
KW - HSV-1
KW - HVEM/HveA
KW - Soluble entry receptor
UR - http://www.scopus.com/inward/record.url?scp=84855721024&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84855721024&partnerID=8YFLogxK
U2 - 10.1186/1743-422X-9-15
DO - 10.1186/1743-422X-9-15
M3 - Article
C2 - 22239829
AN - SCOPUS:84855721024
VL - 9
JO - Virology Journal
JF - Virology Journal
SN - 1743-422X
M1 - 15
ER -