Adaptation of equine herpesvirus 1 to unnatural host led to mutation of the gC resulting in increased susceptibility of the virus to heparin.
Heparin extensively inhibited infection of MDBK cells by equine herpesvirus 1 (EHV-1) strains adapted to bovine cells or hamsters, while the reagent merely reduced infectivity of strains passaged only in equine cells. The gC of two strains adapted to non-equine cells seemed to have higher affinity for heparin, although the reagent bound to both the gC and gB of all strains tested. Amino acid substitutions of the gC of the EHV-1 strains adapted to non-equine cells converged on the hydrophilic regions, amino acid residues 92 to 175, resulting in the glycoprotein becoming more cationic. These results indicate that these hydrophilic regions of the gC may be responsible for binding to heparin.
Sugahara
Y
Y
Department of Disease Control, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, Japan.
Matsumura
T
T
Kono
Y
Y
Honda
E
E
Kida
H
H
Okazaki
K
K
D000222:Adaptation, Physiological; D019943:Amino Acid Substitution; D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D002460:Cell Line; D006224:Cricetinae; D005814:Genes, Viral; D006493:Heparin / Q000378:metabolism / Q000494:pharmacology*; D004861:Herpesvirus 1, Equid / Q000187:drug effects* / Q000235:genetics / Q000502:physiology; D006736:Horses; D009154:Mutation; D014759:Viral Envelope Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015678:Viral Structural Proteins / Q000235:genetics; D014776:Virus Cultivation
D014759:Viral Envelope Proteins; D015678:Viral Structural Proteins; C040495:glycoprotein B, Simplexvirus; C080410:glycoprotein C, Equid herpesvirus 1; D006493:Heparin