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Structural basis of glycan recognition in globally predominant human P[8] rotavirus
Structural highlights
FunctionPublication Abstract from PubMedRotavirus (RV) causes acute gastroenteritis in infants and children worldwide. Recent studies showed that glycans such as histo-blood group antigens (HBGAs) function as cell attachment factors affecting RV host susceptibility and prevalence. P[8] is the predominant RV genotype in humans, but the structural basis of how P[8] RVs interact with glycan ligands remains elusive. In this study, we characterized the interactions between P[8] VP8*s and glycans which showed that VP8*, the RV glycan binding domain, recognized both mucin core 2 and H type 1 antigens according to the ELISA-based oligosaccharide binding assays. Importantly, we determined the structural basis of P[8] RV-glycans interaction from the crystal structures of a Rotateq P[8] VP8* in complex with core 2 and H type 1 glycans at 1.8 A and 2.3 A, respectively, revealing a common binding pocket and similar binding mode. Structural and sequence analysis demonstrated that the glycan binding site is conserved among RVs in the P[II] genogroup, while genotype-specific amino acid variations determined different glycan binding preference. Our data elucidated the detailed structural basis of the interactions between human P[8] RVs and different host glycan factors, shedding light on RV infection, epidemiology, and development of anti-viral agents. Structural Basis of Glycan Recognition in Globally Predominant Human P[8] Rotavirus.,Sun X, Dang L, Li D, Qi J, Wang M, Chai W, Zhang Q, Wang H, Bai R, Tan M, Duan Z Virol Sin. 2019 Oct 16. pii: 10.1007/s12250-019-00164-7. doi:, 10.1007/s12250-019-00164-7. PMID:31620994[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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