Rotavirus (RV) is the leading cause of severe gastroenteritis in infants and young children. The VP8* domain of RV surface protein VP4 attaches to host surface cell glycans, which is an important first step in infection. Human histo-blood group antigens (HBGA’s) have been shown to bind certain strains of RV. Genotypes P[4] and P[8] of the P[II] lineage bind both Lewis b and H type 1 antigens, while P[6], which is also a member of the P[II] lineage, only binds the H type 1 antigen. The molecular basis for this difference was previously unknown. In this study, Nuclear Magnetic Resonance (NMR) and NMR- based high ambiguity driven docking (HADDOCK) methods were used to determine the molecular structure of the VP8* domain in genotypes P[6] and P[8]. While the P[6] genotype binds the H-1 antigen in a binding site formed by an α-helix and a β sheet, known as “βα binding domain,” the P[8] genotype was found to bind the Lewis b antigen in a newly discovered binding pocket composed of two β sheets, known as a “ββ binding domain”. The observation of this second binding site supports the hypothesis that host genetic diversity plays a role in RV evolution, and understanding this role is important in developing new treatments and vaccines against rotavirus.

Molecular basis of P[6] and P[8] major human rotavirus VP8* domain interactions with histo-blood group antigens

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.