7c8p

Structural and functional characterization of human group A rotavirus P[25] VP8*

spinqualitylabelsall models 7c8p, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7c8p is a 2 chain structure with sequence from Rotavirus A. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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