Rhinovirus-stabilizing activity of artificial VLDL-receptor variants defines a new mechanism for virus neutralization by soluble receptors

被引:21
作者
Nicodemou, A
Petsch, M
Konecsni, T
Krernser, L
Kenndler, E
Casasnovas, JM
Blaas, D
机构
[1] Univ Vienna, Dept Biochem Med, Max F Perutz Labs, Vienna Bioctr,Univ Dept, A-1030 Vienna, Austria
[2] Univ Vienna, Inst Analyt Chem, A-1090 Vienna, Austria
[3] CSIC, Ctr Nacl Biotecnol, E-28049 Madrid, Spain
来源
FEBS LETTERS | 2005年 / 579卷 / 25期
关键词
rhinovirus; concatemer; picornavirus; receptor; VLDL-receptor; breathing;
D O I
10.1016/j.febslet.2005.09.013
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Members of the low-density lipoprotein receptor family possess various numbers of ligand binding repeats that non-equally contribute to binding of minor group human rhinoviruses. Using an artificial concatemer of five copies of repeat 3 of the human very-low density lipoprotein receptor, we demonstrate protection of HRV2 against low-pH mediated uncoating and inhibition of penetration of an RNA-specific fluorescent dye into the intact virion. This indicates that the recombinant receptor inhibits viral breathing and irreversible conformational modifications of the capsid that precede RNA release, providing a new mechanism for rhinovirus neutralization by soluble receptor molecules. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
引用
收藏
页码:5507 / 5511
页数:5
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