scholarly journals Coagulation factor VIIa binds to herpes simplex virus 1‐encoded glycoprotein C forming a factor X‐enhanced tenase complex oriented on membranes

2020 ◽  
Vol 18 (6) ◽  
pp. 1370-1380 ◽  
Author(s):  
Bryan H. Lin ◽  
Michael R. Sutherland ◽  
Federico I. Rosell ◽  
James H. Morrissey ◽  
Edward L. G. Pryzdial
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Factor Viia ◽  
Coagulation Factor ◽  
Factor X ◽  
Herpes Simplex Virus 1 ◽  
Glycoprotein C ◽  
Simplex Virus

Pathogenicity of Glycoprotein C-Deficient Herpes Simplex Virus 1 Strain TN-1 Which Encodes Truncated Glycoprotein C

1997 ◽  
Vol 41 (7) ◽  
pp. 545-551 ◽  
Author(s):  
Hiroko Minagawa ◽  
Ying Liu Tetsuhiko Yoshida ◽  
Yasufumi Hidaka ◽  
Yasushi Toh ◽  
Ryoichi Mori
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Herpes Simplex Virus 1 ◽  
Glycoprotein C ◽  
Simplex Virus

scholarly journals Herpes simplex virus type 1-encoded glycoprotein C contributes to direct coagulation Factor X–virus binding

2005 ◽  
Vol 393 (2) ◽  
pp. 529-535 ◽  
Author(s):  
Joel R. Livingston ◽  
Michael R. Sutherland ◽  
Harvey M. Friedman ◽  
Edward L. G. Pryzdial
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Binding Sites ◽  
Factor X ◽  
Wild Type ◽  
Glycoprotein C ◽  
Simplex Virus

The HSV1 (herpes simplex virus type 1) surface has been shown recently to initiate blood coagulation by FVIIa (activated Factor VII)-dependent proteolytic activation of FX (Factor X). At least two types of direct FX–HSV1 interactions were suggested by observing that host cell-encoded tissue factor and virus-encoded gC (glycoprotein C) independently enhance FVIIa function on the virus. Using differential sedimentation to separate bound from free 125I-ligand, we report in the present study that, in the presence of Ca2+, FX binds directly to purified wild-type HSV1 with an apparent dissociation constant (Kd) of 1.5±0.4 μM and 206±24 sites per virus at saturation. The number of FX-binding sites on gC-deficient virus was reduced to 43±5, and the remaining binding had a lower Kd (0.7±0.2 μM), demonstrating an involvement of gC. Engineering gC back into the deficient strain or addition of a truncated soluble recombinant form of gC (sgC), increased the Kd and the number of binding sites. Consistent with a gC/FX stoichiometry of approximately 1:1, 121±6 125I-sgC molecules were found to bind per wild-type HSV1. In the absence of Ca2+, the number of FX-binding sites on the wild-type virus was similar to the gC-deficient strain in the presence of Ca2+. Furthermore, in the absence of Ca2+, direct sgC binding to HSV1 was insignificant, although sgC was observed to inhibit the FX–virus association, suggesting a Ca2+-independent solution-phase FX–sgC interaction. Cumulatively, these data demonstrate that gC constitutes one type of direct FX–HSV1 interaction, possibly providing a molecular basis for clinical correlations between recurrent infection and vascular pathology.

Herpes simplex virus type 1-encoded glycoprotein C enhances coagulation factor VIIa activity on the virus

2004 ◽  
Vol 92 (11) ◽  
pp. 947-955 ◽  
Author(s):  
Michael Sutherland ◽  
Harvey Friedman ◽  
Edward Pryzdial
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Specific Antibody ◽  
Herpes Simplex Virus Type ◽  
Factor Viia ◽  
Virus Surface ◽  
Glycoprotein C ◽  
Simplex Virus

SummaryTissue factor (TF) is the blood coagulation initiator, whose cofactor function is required for physiological factor VIIa (FVIIa)-mediated activation of factor X (FX) to FXa. A previous study reported TF on herpes simplex virus type 1 (HSV1), but this explained only part of FVIIa-dependent FXa generation observed on the virus surface (Sutherland et al. (1997) Proc. Natl. Acad. Sci. USA. 94:13510-14). In the current study, we investigated the role of HSV1-encoded glycoprotein C (gC) in this process. Purified gC-deficient HSV1 facilitated several fold less FX activation by FVIIa than either wild type or gC-rescued strains.To confirm the implication of gC in FVIIa-dependent FX activation, purified soluble gC (sgC) enhanced FXa production in the absence of TF. sgC required FVIIa, calcium and anionic phospholipid to participate in FX activation, suggesting similarity to TF. When purified virus was combined with sgC, the sgC-dependent FXa generation was enhanced three orders of magnitude, suggesting synergy with an additional HSV1 component and explaining the relatively low activity of purified sgC compared to the viral counterpart. FX activation on gC-competent HSV1 was inhibited 20% by a gC-specific antibody, inhibited 40% by a TF-specific antibody, inhibited 65% by combining the gCand TF-specific antibodies, and nearly completely inhibited by the TF antibody alone on gC-deficient HSV-1. Cumulatively, these observations show that two pathways initiating FX activation function in parallel on the virus surface. In addition to the previously described TF-dependent pathway, HSV-1-encoded gC also enhances FXa generation, and like TF, requires FVIIa.

Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells

Nature ◽  
1984 ◽  
Vol 309 (5969) ◽  
pp. 633-635 ◽  
Author(s):  
Harvey M. Friedman ◽  
Gary H. Cohen ◽  
Roselyn J. Eisenberg ◽  
Cynthia A. Seidel ◽  
Douglas B. Cines
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Complement Component ◽  
Herpes Simplex Virus 1 ◽  
Glycoprotein C ◽  
Infected Cells ◽  
Simplex Virus

scholarly journals Widely Used Herpes Simplex Virus 1 ICP0 Deletion Mutant Strain dl1403 and Its Derivative Viruses Do Not Express Glycoprotein C Due to a Secondary Mutation in the gC Gene

PLoS ONE ◽  
2015 ◽  
Vol 10 (7) ◽  
pp. e0131129 ◽  
Author(s):  
Cristina W. Cunha ◽  
Kathryne E. Taylor ◽  
Suzanne M. Pritchard ◽  
Mark G. Delboy ◽  
Tri Komala Sari ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Mutant Strain ◽  
Deletion Mutant ◽  
Secondary Mutation ◽  
Herpes Simplex Virus 1 ◽  
Glycoprotein C ◽  
Simplex Virus ◽  
Gc Gene

scholarly journals Expression and regulation of glycoprotein C gene of herpes simplex virus 1 resident in a clonal L-cell line.

1986 ◽  
Vol 58 (2) ◽  
pp. 367-376 ◽  
Author(s):  
M Arsenakis ◽  
L F Tomasi ◽  
V Speziali ◽  
B Roizman ◽  
G Campadelli-Fiume
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Cell Line ◽  
Herpes Simplex Virus 1 ◽  
Glycoprotein C ◽  
L Cell ◽  
Simplex Virus
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