Heparin-binding domain of bovid herpesvirus 1 glycoprotein gIII.
Bovid herpesvirus 1 (BHV-1) glycoprotein gIII functions as a major virus attachment protein through binding to a heparin-like moiety on the host cells. To identify the functional domain, a panel of gIII deletion mutants was constructed, expressed in COS-7 cells, and examined for heparin-binding activity. Mutants with deletion of amino acid residues 103-173 and 324-443 bound to heparin as well as full-length gIII, whereas a mutant with residues 172-337 deleted showed no binding to heparin. In another mutant, with residues 172-211 deleted, the activity was reduced by one-third. These data suggest that the amino acid sequence between residues 172 and 323 contains the functional domain of BHV-1 gIII for heparin-binding and that especially the sequence between residues 212-323 includes a critical site for the activity.
Okazaki
K
K
Department of Veterinary Medicine, Faculty of Agriculture, Tokyo University of Agriculture, Technology, Japan.
Honda
E
E
Kono
Y
Y
D000595:Amino Acid Sequence; D001665:Binding Sites; D002460:Cell Line; D004563:Electrochemistry; D006493:Heparin / Q000378:metabolism*; D007242:Herpesvirus 1, Bovine / Q000378:metabolism*; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D017384:Sequence Deletion; D014162:Transfection; D014764:Viral Proteins / Q000737:chemistry / Q000378:metabolism*
D011994:Recombinant Proteins; D014764:Viral Proteins; C046998:bovine herpesvirus type-1 glycoproteins; D006493:Heparin