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

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• 作者：Andreas Nicodemou ; Martina Petsch ; Tunde Konecsni ; Leopold Kremser ; Ernst Kenndler ; José ; M. Casasnovas and Dieter Blaas
• 关键词：Rhinovirus ; Concatemer ; Picornavirus ; Receptor ; VLDL-receptor ; Breathing
• 刊名：FEBS Letters
• 出版年：2005
• 出版时间：2005
• 年：2005
• 卷：579
• 期：25
• 页码：5507-5511
• 全文大小：198 K

文摘

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.