【摘 要】
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Rotavirus (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 pre
【机 构】
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National Health Commission Key Laboratory for Medical Virology and Viral Diseases, Beijing 102206, C
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Rotavirus (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.
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