Human rhinovirus type 89 variants use heparan sulfate proteoglycan for cell attachment

被引:57
作者
Vlasak, M [1 ]
Goester, I [1 ]
Blaas, D [1 ]
机构
[1] Med Univ Vienna, Dept Biochem Med, Vienna Bioctr, Max F Perutz Labs, A-1030 Vienna, Austria
关键词
D O I
10.1128/JVI.79.10.5963-5970.2005
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
We have previously isolated mutants of the major-group human rhinovirus type 89 that grow in cells deficient in intercellular adhesion molecule 1 (ICAM-1), the receptor used by the wild-type virus for cell entry [A. Reischl, M. Reithmayer, G. Winsauer, R. Moser, I. Goesler, and D. Blaas., J. Virol. 75:9312-9319, 2001]. We now demonstrate that one of these variants utilizes heparan sulfate proteoglycan (HSPG) as a cellular receptor. Adaptation to ICAM-1-deficient cells not only resulted in the newly acquired receptor specificity but also rendered the virus less stable at low pH and at elevated temperatures. This instability might compensate for the absence of the uncoating activity of ICAM-1. Whereas wild-type virus infection via ICAM-1 proceeded in the presence of the vesicular H+-ATPase inhibitor bafilomycin All, infection by the mutant via HSPG was prevented by the drug. This suggests that the low pH prevailing in endosomal compartments is required for uncoating in the absence of the catalytic activity of ICAM-1.
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收藏
页码:5963 / 5970
页数:8
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