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Rhinovirus‐stabilizing activity of artificial VLDL‐receptor variants defines a new mechanism for virus neutralization by soluble receptors
Author(s) -
Nicodemou Andreas,
Petsch Martina,
Konecsni Tunde,
Kremser Leopold,
Kenndler Ernst,
Casasnovas José M.,
Blaas Dieter
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.09.013
Subject(s) - neutralization , receptor , capsid , rhinovirus , recombinant dna , rna , ldl receptor , biology , virology , virus , chemistry , microbiology and biotechnology , lipoprotein , biochemistry , cholesterol , gene
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.