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Structural Basis of glycan Recognition in Globally Predominant Human P[8]Rotavirus

Virologica Sinica 2020年第2期35卷 156-170页

作者： Xiaoman Sun Lei Dang Dandi Li Jianxun Qi Mengxuan Wang Wengang Chai Qing Zhang Hong Wang Ruixia Bai Ming Tan Zhaojun Duan National Health Commission Key Laboratory for Medical Virology and Viral Diseases Beijing 102206China National Institute for Viral Disease Control and Prevention China CDC.Beijing 102206China Inner Mongolia Medical University Huhehaote 010059China Institute of Microbiology Chinese Academy of SciencesBeijing 100101China Glycosciences Laboratory Department of MedicineImperial College LondonLondonUK Division of Infectious Diseases University of Cincinnati College of MedicineCincinnatiOHUSA

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 1.82.3?,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.

关键词： Rotavirus(RV)·P glycan binding specificity VPS*structure Mucin core 2 Lacto-N-fucopentaose 1(LNFPl)

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The Functional Characterization of Bat and Human P[3] Rotavirus VP8*s

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Virologica Sinica 2021年第5期36卷 1187-1196页

作者： Dandi Li Mengxuan Wang Tongyao Mao Mingwen Wang Qing Zhang Hong Wang Lili Pang Xiaoman Sun Zhaojun Duan National Health Commission Key Laboratory for Medical Virology and Viral Diseases Beijing 102206China National Institute for Viral Disease Control and Prevention China CDCBeijing 102206China

P[3]rotavirus(RV)has been identified in many species,including human,simian,dog,and bat.Several glycans,including sialic acid,histo-blood group antigens(HBGAs)are reported as RV attachment factors.The glycan binding specificity of different P[3]RV VP8*s were investigated in this study.Human HCR3 A and dog P[3]RV VP8*s recognized glycans with terminal sialic acid and hemagglutinated the red blood cells,while bat P[3]VP8*showed neither binding to glycans nor hemagglutination.However,the bat P[3]VP8*mutant of C189 Y obtained the ability to hemagglutinate the red blood cells,while human P[3]HCR3 A/M2-102 mutants of Y189 C lost the ability.Sequence alignment and structural analysis indicated that residue 189 played an important role in the ligand recognition and may contribute to the cross-species transmission.Structural superimposition exhibited that bat P[3]VP8*model was quite different from the simian P[3]Rhesus rotavirus(RRV)P[3]VP8*,indicating that bat P[3]RV was relatively distinct and partially contributed to the no binding to tested glycans.These results promote our understanding of P[3]VP8*/glycans interactions and the potential transmission of bat/human P[3]RVs,offering more insight into the RV infection and prevalence.

关键词： Bat rotavirus PVP8* glycan binding specificity Hemagglutination Sialic acid

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