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Virology. 2012 Jan 20;422(2):174-84. doi: 10.1016/j.virol.2011.10.023. Epub 2011 Nov 12.

Hepatitis C virus epitope exposure and neutralization by antibodies is affected by time and temperature.

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  • 1Department of Pathology & Immunology, Washington University School of Medicine, St. Louis, MO 63110, USA.

Abstract

A recent study with flaviviruses suggested that structural dynamics of the virion impact antibody neutralization via exposure of ostensibly cryptic epitopes. To determine whether this holds true for the distantly related hepatitis C virus (HCV), whose neutralizing epitopes may be obscured by a glycan shield, apolipoprotein interactions, and the hypervariable region on the E2 envelope protein, we assessed how time and temperature of pre-incubation altered monoclonal antibody (MAb) neutralization of HCV. Notably, several MAbs showed increased inhibitory activity when pre-binding was performed at 37°C or after longer pre-incubation periods, and a corresponding loss-of-neutralization was observed when pre-binding was performed at 4°C. A similar profile of changes was observed with acute and chronic phase sera from HCV-infected patients. Our data suggest that time and temperature of incubation modulate epitope exposure on the conformational ensembles of HCV virions and thus, alter the potency of antibody neutralization.

Copyright © 2011 Elsevier Inc. All rights reserved.

PMID:
22078164
[PubMed - indexed for MEDLINE]
PMCID:
PMC3356770
Free PMC Article

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