Thermodynamic mechanism for the evasion of antibody neutralization in flaviviruses.

ABSTRACT: Mutations in the epitopes of antigenic proteins can confer viral resistance to antibody-mediated neutralization. However, the fundamental properties that characterize epitope residues and how mutations affect antibody binding to alter virus susceptibility to neutralization remain largely unknown. To address these questions, we used an ensemble-based algorithm to characterize the effects of mutations on the thermodynamics of protein conformational fluctuations. We applied this method to the envelope protein domain III (ED3) of two medically important flaviviruses: West Nile and dengue 2. We determined an intimate relationship between the susceptibility of a residue to thermodynamic perturbations and epitope location. This relationship allows the successful identification of the primary epit

SUBMITTER: Maillard RA 

PROVIDER: S-EPMC4111217 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature