Dandi Li, Mengxuan Wang, Tongyao Mao, Mingwen Wang, Qing Zhang, Hong Wang, Lili Pang, Xiaoman Sun and Zhaojun Duan. The Functional Characterization of Bat and Human P[3] Rotavirus VP8*s[J]. Virologica Sinica, 2021, 36(5): 1187-1196. doi: 10.1007/s12250-021-00400-z
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

蝙蝠和人P[3]轮状病毒VP8*蛋白的功能研究

cstr: 32224.14.s12250-021-00400-z
  • 通讯作者: 孙晓曼, sunxiaoman88@163.com, ORCID: http://orcid.org/0000-0002-2601-8239
    ; 段招军, zhaojund@126.com, ORCID: http://orcid.org/0000-0003-3090-4150
  • 收稿日期: 2021-01-06
    录用日期: 2021-04-12
    出版日期: 2021-05-31
  • P[3]型轮状病毒在许多物种中都有发现,包括人、猴、狗和蝙蝠等。关于轮状病毒的受体已有很多研究,据报导多种聚糖可以作为轮状病毒进入宿主细胞的粘附分子,包括唾液酸、组织血型抗原(HBGAs)。本研究对不同物种P[3]型轮状病毒VP8*s的多糖结合特性进行探索。研究发现人HCR3A和狗P[3]型轮状病毒VP8*结合唾液酸以及末端带有唾液酸的聚糖。,同时,人和狗P[3]型轮状病毒VP8*还可以凝集不同物种红细胞,而蝙蝠P[3]型轮状病毒VP8*既不与聚糖结合,也不发生血凝。进一步研究显示蝙蝠P[3]型轮状病毒P[3] VP8* C189Y突变体可以凝集红细胞,而人P[3] HCR3A/M2-102 Y189C突变体则不再凝集红细胞。序列比对和结构分析表明,VP8*蛋白189位氨基酸在轮状病毒VP8*配体识别中起着重要作用,氨基酸的改变可能促进轮状病毒跨物种传播。结构比对显示蝙蝠P[3]型 VP8*的模拟结构与RRV 猴P[3]型VP8*有很大差异,尤其糖结合位点区域构象也呈现不同特征,表明蝙蝠P[3]型轮状病毒相对与其他P[3]型轮状病毒是不同的明显不同,一定程度上解释了蝙蝠P[3]轮状病毒VP8*不结合唾液酸多糖。这些研究促进了我们对P[3]型轮状病毒VP8*与多糖相互作用以及蝙蝠和人P[3]轮状病毒传播的认识,为探索轮状病毒的感染和流行提供了更多的信息。

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

  • Corresponding author: Xiaoman Sun, sunxiaoman88@163.com Zhaojun Duan, zhaojund@126.com
  • ORCID: http://orcid.org/0000-0002-2601-8239; http://orcid.org/0000-0003-3090-4150
  • Received Date: 06 January 2021
    Accepted Date: 12 April 2021
    Published Date: 31 May 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

    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.