TY - JOUR
T1 - gp13 (EHV-gC)
T2 - a complement receptor induced by equine herpesviruses
AU - Huemer, Hartwig P.
AU - Nowotny, Norbert
AU - Crabb, Brendan S.
AU - Meyer, Hermann
AU - Hübert, Peter H.
PY - 1995/7
Y1 - 1995/7
N2 - Equine herpesviruses type 1 (EHV-1) and type 4 (EHV-4) induce a complement receptor protein on the surface of infected cells capable of binding to the third component of complement (C3). The protein mediating the binding to the C3 component of complement was identified as glycoprotein 13 (gp13, EHV-gC), as expression of the cloned viral gene under the control of a CMV promoter induced C3 binding activity at the transfected cell surface. Comparable to glycoprotein C (gC) from herpes simplex virus type 1 (HSV-1-gC), glycoprotein III from pseudorabiesvirus (gIII, PRV-gC) and bovine herpesvirus-1 (gIII, BHV-1-gC), gp13 derived from EHV-infected cell lysates bound to C3 fixed to solid phase, showing preferential binding to the appropriate host complement component. Similar to wild-type isolates, a highly attenuated vaccine EHV-1 strain also displayed complement receptor activity despite apparent differences of the gp13 gene in restriction enzyme digest pattern and reactivity with monoclonal antibodies. In addition, other structural proteins were altered in the vaccine strain as compared to wild-type strains, which might contribute to its attenuated phenotype. In contrast to the situation observed with HSV-1-gC, the interaction of gp13 (EHV-gC) with horse complement was not inhibited by polyanionic substances like heparin or dextran sulfate. These results suggest structural differences in the particular binding mechanism of the respective viral envelope proteins.
AB - Equine herpesviruses type 1 (EHV-1) and type 4 (EHV-4) induce a complement receptor protein on the surface of infected cells capable of binding to the third component of complement (C3). The protein mediating the binding to the C3 component of complement was identified as glycoprotein 13 (gp13, EHV-gC), as expression of the cloned viral gene under the control of a CMV promoter induced C3 binding activity at the transfected cell surface. Comparable to glycoprotein C (gC) from herpes simplex virus type 1 (HSV-1-gC), glycoprotein III from pseudorabiesvirus (gIII, PRV-gC) and bovine herpesvirus-1 (gIII, BHV-1-gC), gp13 derived from EHV-infected cell lysates bound to C3 fixed to solid phase, showing preferential binding to the appropriate host complement component. Similar to wild-type isolates, a highly attenuated vaccine EHV-1 strain also displayed complement receptor activity despite apparent differences of the gp13 gene in restriction enzyme digest pattern and reactivity with monoclonal antibodies. In addition, other structural proteins were altered in the vaccine strain as compared to wild-type strains, which might contribute to its attenuated phenotype. In contrast to the situation observed with HSV-1-gC, the interaction of gp13 (EHV-gC) with horse complement was not inhibited by polyanionic substances like heparin or dextran sulfate. These results suggest structural differences in the particular binding mechanism of the respective viral envelope proteins.
KW - Complement receptor
KW - Equine herpesvirus (EHV)
KW - Glycoprotein
KW - Heparin
KW - gp13
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U2 - 10.1016/0168-1702(95)00027-N
DO - 10.1016/0168-1702(95)00027-N
M3 - Article
C2 - 7483825
AN - SCOPUS:0028979932
SN - 0168-1702
VL - 37
SP - 113
EP - 126
JO - Virus Research
JF - Virus Research
IS - 2
ER -