Literature DB >> 33453651

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

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.
Copyright © 2021 Elsevier Inc. All rights reserved.

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


  2 in total

Review 1.  Rotavirus Interactions With Host Intestinal Epithelial Cells.

Authors:  Joshua Oluoch Amimo; Sergei Alekseevich Raev; Juliet Chepngeno; Alfred Omwando Mainga; Yusheng Guo; Linda Saif; Anastasia N Vlasova
Journal:  Front Immunol       Date:  2021-12-22       Impact factor: 7.561

Review 2.  Structural Basis of Glycan Recognition of Rotavirus.

Authors:  Xiaoman Sun; Dandi Li; Zhaojun Duan
Journal:  Front Mol Biosci       Date:  2021-07-08
  2 in total

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