Structural highlights
Function
M1GR78_9VIRU
Publication Abstract from PubMed
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 A, 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.
Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen.,Li D, Wang M, Qi J, Zhang Q, Wang H, Pang L, Sun X, Duan Z Virology. 2021 Mar;555:56-63. doi: 10.1016/j.virol.2020.12.016. Epub 2021 Jan 5. PMID:33453651[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li D, Wang M, Qi J, Zhang Q, Wang H, Pang L, Sun X, Duan Z. Human group A rotavirus P[25] VP8* specifically binds to A-type histo-blood group antigen. Virology. 2021 Mar;555:56-63. PMID:33453651 doi:10.1016/j.virol.2020.12.016
