Functional and Structural Characterization of P[19] Rotavirus VP8☆ Interaction with Histo-blood Group Antigens
Functional and Structural Characterization of P[19] Rotavirus VP8☆ Interaction with Histo-blood Group Antigens
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P[19]轮状病毒 VP8 与组织血型抗原相互作用的功能和结构特征。
DOI:
10.1128/jvi.01566-16
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发表时间:
2016-11-01
影响因子:
5.4
通讯作者:
Duan, Zhao-Jun
中科院分区:
文献类型:
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作者:
Sun, Xiaoman;Li, Dandi;Duan, Zhao-Jun
Rotaviruses (RVs) of species A (RVA) are a major causative agent of acute gastroenteritis. Recently, histo-blood group antigens (HBGAs) have been reported to interact with human RVA VP8(star) proteins. Human P[19] is a rare P genotype of porcine origin that infects humans sporadically. The functional and structural characteristics of P[19] VP8(star) interaction with HBGAs are unknown. In this study, we expressed and purified the VP8(star) proteins of human and porcine P[19] RVs. In oligosaccharide and saliva binding assays, P[19] VP8(star) proteins showed obvious binding to A-, B-, and O-type saliva samples irrespective of the secretor status, implying broad binding patterns. However, they did not display specific binding to any of the oligosaccharides tested. In addition, we solved the structure of human P[19] VP8(star) at 2.4 angstrom, which revealed a typical galectin-like fold. The structural alignment demonstrated that P[19] VP8(star) was most similar to that of P[8], which was consistent with the phylogenetic analysis. Structure superimposition revealed the basis for the lack of binding to the oligosaccharides. Our study indicates that P[19] RVs may bind to other oligosaccharides or ligands and may have the potential to spread widely among humans. Thus, it is necessary to place the prevalence and evolution of P[19] RVs under surveillance.