Rhinovirus-stabilizing activity of artificial VLDL-receptor variants defines a new mechanism for virus neutralization by soluble receptors.
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.
Nicodemou
Andreas
A
Institute of Analytical Chemistry, University of Vienna, Austria.
Petsch
Martina
M
Konecsni
Tunde
T
Kremser
Leopold
L
Kenndler
Ernst
E
Casasnovas
José M
JM
Blaas
Dieter
D
D044966:Anti-Retroviral Agents / Q000737:chemistry / Q000494:pharmacology*; D005456:Fluorescent Dyes / Q000032:analysis; D006801:Humans; D012367:RNA, Viral / Q000032:analysis / Q000187:drug effects*; D011973:Receptors, LDL / Q000737:chemistry* / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000494:pharmacology*; D012229:Rhinovirus / Q000187:drug effects*; D014771:Virion / Q000737:chemistry / Q000187:drug effects
D044966:Anti-Retroviral Agents; D005456:Fluorescent Dyes; C506068:MBP-V33333 peptide; D012367:RNA, Viral; D011973:Receptors, LDL; D011993:Recombinant Fusion Proteins; C036053:VLDL receptor