Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen.

Dandi Li, Mengxuan Wang, Jianxun Qi, Qing Zhang, Hong Wang, Lili Pang, Xiaoman Sun, Zhaojun Duan

Virology 2021 Mar

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Rotavirus (RV) is a common cause of acute gastroenteritis in young children. While P[8] and P[4] are the most prevalent RV genotypes in humans, other genotypes are also reported in human infections occasionally, including human P[25]. The glycan binding and structural characteristics of human P[25] were explored in our study. Human P[25] VP8* recognized type A histo-blood group antigen (HBGA) in the glycan microarray/oligosaccharide binding assay and could specifically hemagglutinate type A blood cells. Moreover, the P[25] VP8* structure was determined at 2.6 Å, revealing a similar conformation and a conserved putative glycan binding site as that of P[14] VP8*. This study provided further knowledge of the glycan binding and structural features of P[25] RV VP8*, promoting our understanding of the infection, prevalence, and host range of the P[III] RVs. Copyright © 2021 Elsevier Inc. All rights reserved.

Citation

Dandi Li, Mengxuan Wang, Jianxun Qi, Qing Zhang, Hong Wang, Lili Pang, Xiaoman Sun, Zhaojun Duan. Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen. Virology. 2021 Mar;555:56-63