A recombinant, arginine-glycine-aspartic acid (RGD) motif from foot-and-mouth disease virus binds mammalian cells through vitronectin and, to a lower extent, fibronectin receptors

被引:20
作者
Villaverde, A
Feliu, JX
Harbottle, RP
Benito, A
Coutelle, C
机构
[1] UNIV AUTONOMA BARCELONA,DEPT GENET & MICROBIOL,BELLATERRA 08193,BARCELONA,SPAIN
[2] ST MARYS HOSP,SCH MED,DEPT BIOCHEM & MOL GENET,LONDON W2 1PG,ENGLAND
基金
英国医学研究理事会;
关键词
cellular receptor; fusion protein; integrin; picornavirus; protein VP1; antigenic site;
D O I
10.1016/S0378-1119(96)00413-1
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The cell-binding abilities of a recombinant, RGD-containing peptide from foot-and-mouth disease virus (FMDV) have been characterized in HeLa and BHK cells. This peptide represents the aa sequence of the solvent-exposed G-H loop of protein VP1 which is involved in cell recognition and infection. The efficiency of the viral motif in promoting cell attachment and spreading is comparable to that shown by fibronectin or vitronectin. Cell binding is inhibited by a monoclonal antibody directed against a viral, RGD-involving B-cell epitope and also by sera against vitronectin (alpha(v) beta(3)/beta(5)) and fibronectin (alpha(5) beta(1)) receptors. In addition, a synthetic RGD peptide, which is a ligand for both integrins, prevents the cell binding mediated by the FMDV domain. These data demonstrate that the FMDV RGD motif is a potent ligand for cell-receptor integrins and sufficient to promote cell attachment to susceptible cells mainly through the vitronectin receptor.
引用
收藏
页码:101 / 106
页数:6
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