Multiple Tandemly Repeated Binding Sites for the YY1 Repressor and Transcription Factors AP-1 and SP-1 Are Clustered within lntron-1 of the Gene Encoding the IE110 Transacti vator of Herpes simplex Virus Type 1

1995 ◽  
Vol 2 (3) ◽  
pp. 203-226
Author(s):  
Gary S. Hayward ◽  
Qi Huang ◽  
Wei Gu
Keyword(s):  
Transcription Factors ◽  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Binding Sites ◽  
Gene Encoding ◽  
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.

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