Specific Residue Interactions Regulate the Binding of Dengue Antigens to Broadly Neutralizing EDE Antibodies.

ABSTRACT: Antibodies binding to antigens present on the dengue virus (DENV) represent the main defense mechanism of the host organism against the pathogen. Among the antibodies elicited by DENV and that bind to DII of protein E, EDE1-C8 can bind all DENV serotypes. Our analysis reveals the key residues in this interaction as well as structurally conserved hydrogen bonds located at the binding interface. They stabilize the dengue antigen-antibody complex among the EDE1 group of antibodies (Abs). Combining structural alignments with molecular dynamics simulations in the EDE1 Abs, we identified the critical elements that provide a major energetic contribution to the association of antigens from protein E with Abs. We discuss possible molecular insights into the binding mechanism by using a surrogate mo

SUBMITTER: Lapelosa M 

PROVIDER: S-EPMC6099161 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature