Modeling the Role of Epitope Arrangement on Antibody Binding Stoichiometry in Flaviviruses.

ABSTRACT: Cryo-electron-microscopy (cryo-EM) structures of flaviviruses reveal significant variation in epitope occupancy across different monoclonal antibodies that have largely been attributed to epitope-level differences in conformation or accessibility that affect antibody binding. The consequences of these variations for macroscopic properties such as antibody binding and neutralization are the results of the law of mass action-a stochastic process of innumerable binding and unbinding events between antibodies and the multiple binding sites on the flavivirus in equilibrium-that cannot be directly imputed from structure alone. We carried out coarse-grained spatial stochastic binding simulations for nine flavivirus antibodies with epitopes defined by cryo-EM or x-ray crystallography to assess the

SUBMITTER: Ripoll DR 

PROVIDER: S-EPMC5071605 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature