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Volume 36 Issue 5
October 2021
    Citation: Dandi Li, Mengxuan Wang, Tongyao Mao, Mingwen Wang, Qing Zhang, Hong Wang, Lili Pang, Xiaoman Sun, Zhaojun Duan. The Functional Characterization of Bat and Human P[3] Rotavirus VP8*s .VIROLOGICA SINICA, 2021, 36(5) : 1187-1196.  http://dx.doi.org/10.1007/s12250-021-00400-z
    shu

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

    • 1.

      National Health Commission Key Laboratory for Medical Virology and Viral Diseases, Beijing, 102206, China

    • 2.

      National Institute for Viral Disease Control and Prevention, China CDC, Beijing, 102206, China

    • Corresponding author: Xiaoman Sun, sunxiaoman88@163.com, ORCID: http://orcid.org/0000-0002-2601-8239
      Zhaojun Duan, zhaojund@126.com, ORCID: http://orcid.org/0000-0003-3090-4150
    • Dandi Li and Mengxuan Wang have contributed equally to this work.
    • Received Date: 06 January 2021
      Accepted Date: 12 April 2021
      Published Date: 31 May 2021
      Available online: 01 October 2021

    • 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 HCR3A 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 C189Y obtained the ability to hemagglutinate the red blood cells, while human P[3] HCR3A/M2-102 mutants of Y189C 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.

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

        Corresponding author: Xiaoman Sun, sunxiaoman88@163.com
        Corresponding author: Zhaojun Duan, zhaojund@126.com
      • 1. National Health Commission Key Laboratory for Medical Virology and Viral Diseases, Beijing, 102206, China
      • 2. National Institute for Viral Disease Control and Prevention, China CDC, Beijing, 102206, China
      • Received Date: 06 January 2021
      • Accepted Date: 12 April 2021
      • Published Date: 31 May 2021

      Abstract: 

      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 HCR3A 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 C189Y obtained the ability to hemagglutinate the red blood cells, while human P[3] HCR3A/M2-102 mutants of Y189C 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.

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