Pathogenicity of Glycoprotein C-Negative Herpes Simplex Virus Type 1 in Herpetic Keratitis

1994 ◽  
pp. 33-42
Author(s):  
Yasushi Toh ◽  
Yasufumi Hidaka ◽  
Yuji Kumano ◽  
Hiroko Minagawa ◽  
Ryoichi Mori
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Herpetic Keratitis ◽  
Glycoprotein C ◽  
Simplex Virus

Sialylated oligosaccharides O-glycosidically linked to glycoprotein C from herpes simplex virus type 1.

1985 ◽  
Vol 56 (1) ◽  
pp. 127-134 ◽  
Author(s):  
F Dall'Olio ◽  
N Malagolini ◽  
V Speziali ◽  
G Campadelli-Fiume ◽  
F Serafini-Cessi
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein C ◽  
Simplex Virus

scholarly journals Demonstration and Mapping of Highly Carbohydrate-dependent Epitopes in the Herpes Simplex Virus Type 1-Specified Glycoprotein C

1987 ◽  
Vol 68 (2) ◽  
pp. 545-554 ◽  
Author(s):  
I. Sjoblom ◽  
M. Lundstrom ◽  
E. Sjogren-Jansson ◽  
J. C. Glorioso ◽  
S. Jeansson ◽  
...  
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein C ◽  
Simplex Virus

Glycoprotein C of herpes simplex virus type 1 is required to cause keratitis at low infectious doses in intact rabbit corneas

2004 ◽  
Vol 29 (2-3) ◽  
pp. 181-189 ◽  
Author(s):  
Barbra Drolet ◽  
Kevin Mott ◽  
Andrew Lippa ◽  
Steven Wechsler ◽  
Guey-Chuen Perng
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein C ◽  
Intact Rabbit ◽  
Simplex Virus

Genotyping of herpes simplex virus type 1 strains isolated from ocular materials of patients with herpetic keratitis

2003 ◽  
Vol 71 (1) ◽  
pp. 75-81 ◽  
Author(s):  
Kenichi Umene ◽  
Tomoyuki Inoue ◽  
Yoshitsugu Inoue ◽  
Yoshikazu Shimomura
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Herpetic Keratitis ◽  
Simplex Virus

Characterization of glycoprotein C-negative mutants of herpes simplex virus type 1 isolated from a patient with keratitis

1990 ◽  
Vol 113-113 (3-4) ◽  
pp. 195-207 ◽  
Author(s):  
Y. Hidaka ◽  
S. Sakuma ◽  
Y. Kumano ◽  
H. Minagawa ◽  
R. Mori
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein C ◽  
Simplex Virus

Baculovirus expressed herpes simplex virus type 1 glycoprotein C protects mice from lethal HSV-1 infection

1992 ◽  
Vol 18 (3-4) ◽  
pp. 291-302 ◽  
Author(s):  
Homayon Ghiasi ◽  
Ravi Kaiwar ◽  
Anthony B. Nesburn ◽  
Steven L. Wechsler
Keyword(s):  
Herpes Simplex Virus ◽  
Herpes Simplex ◽  
Virus Type ◽  
Herpes Simplex Virus Type ◽  
Glycoprotein C ◽  
Simplex Virus ◽  
Hsv 1

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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