| Literature DB >> 33453651 |
Dandi Li1, Mengxuan Wang1, Jianxun Qi2, Qing Zhang1, Hong Wang1, Lili Pang1, Xiaoman Sun3, Zhaojun Duan4.
Abstract
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.Entities:
Keywords: Crystal structure; Glycan binding specificity; Histo-blood group antigen (HBGA); Human P[25] rotavirus; VP8*
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Year: 2021 PMID: 33453651 DOI: 10.1016/j.virol.2020.12.016
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616