Identification of the glycosaminoglycan-binding site on the glycoprotein Erns of bovine viral diarrhoea virus by site-directed mutagenesis

被引:32
作者
Iqbal, M [1 ]
McCauley, JW [1 ]
机构
[1] Inst Anim Hlth, Compton Lab, Div Mol Biol, Newbury RG20 7NN, Berks, England
关键词
D O I
10.1099/0022-1317-83-9-2153
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Bovine viral diarrhoea virus (BVDV) envelope glycoprotein E-rns interacts with highly sulphated heparin-like glycosaminoglycans (GAGs) located on the cell surface as an early step in virus infection of cells. Site-directed mutagenesis of recombinant E-rns was undertaken and analysis of mutants by heparin-affinity chromatography and cell surface binding showed that a cluster of basic amino acids ((KKLENKSK487)-K-480) near the C terminus of E-rns was essential for binding. Mutants with amino acid substitutions of lysine residues 481 and 485 in Ems reduced the binding of E-rns to immobilized heparin and cellular GAGs but retained ribonuclease activity. In contrast to normal E-rns, E-rns that was unable to bind to cells also failed to inhibit BVDV infection of cells when the cells were pre-incubated with E-rns. It is proposed that the cluster of basic residues ((KKLENKSK487)-K-480.) localized at the C-terminal end of E-rns constitutes a GAG-binding site.
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页码:2153 / 2159
页数:7
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