Rhinovirus-stabilizing activity of artificial VLDL-receptor variants defines a new mechanism for virus neutralization by soluble receptors |
| |
Authors: | Nicodemou Andreas Petsch Martina Konecsni Tunde Kremser Leopold Kenndler Ernst Casasnovas José M Blaas Dieter |
| |
Affiliation: | Institute of Analytical Chemistry, University of Vienna, Austria. |
| |
Abstract: | 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. |
| |
Keywords: | Rhinovirus Concatemer Picornavirus Receptor VLDL-receptor Breathing |
本文献已被 ScienceDirect PubMed 等数据库收录! |