Rotavirus contains integrin ligand sequences and a disintegrin-like domain that are implicated in virus entry into cells

被引:176
作者
Coulson, BS
Londrigan, SL
Lee, DJ
机构
[1] Dept. of Microbiology and Immunology, University of Melbourne, Parkville
关键词
D O I
10.1073/pnas.94.10.5389
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Rotavirus contains two outer capsid viral proteins, the spike protein VP4 and major capsid component VP7, both of which are implicated in cell entry. We show that VP4 and VP7 contain tripeptide sequences previously shown to act as recognition sites far integrins in extracellular matrix proteins. VP4 contains the alpha 2 beta 1 integrin ligand site DGE. In VP7, the alpha x beta 2 integrin ligand site GPR and the alpha 4 beta 1 integrin ligand site LDV are embedded in a novel disintegrin-like domain that also shows sequence similarity to fibronectin and the tie receptor tyrosine kinase. Microorganism sequence homology to these ligand motifs and to disintegrins has not been reported previously. In our experiments, peptides including these rotaviral tripeptides and mAbs directed to these integrins specifically blocked rotavirus infection of cells shown to express alpha 2 beta 1 and beta 2 integrins. Rotavirus VP4-mediated cell entry may involve the alpha 2 beta 1 integrin, whereas VP7 appears to interact with alpha x beta 2 and alpha 4 beta 1 integrins.
引用
收藏
页码:5389 / 5394
页数:6
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