Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2052519 | FEBS Letters | 2005 | 5 Pages |
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.
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Authors
Andreas Nicodemou, Martina Petsch, Tunde Konecsni, Leopold Kremser, Ernst Kenndler, José M. Casasnovas, Dieter Blaas,