5jdb

Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens

spinqualitylabelsall models 5jdb, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5jdb is a 6 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 1.901Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function E2EA82_9VIRU Publication Abstract from PubMed RotaTeq((R)) and Rotarix are two common human rotavirus (RV) vaccines currently on the market worldwide. Recent studies indicate histo-blood group antigens (HBGAs) may be attachment factors for RVs. The P[8] VP8* proteins of RotaTeq and Rotarix were expressed and purified, and their binding specificities were evaluated. Saliva-based binding assays showed that the VP8* proteins bound to the saliva samples of secretors irrespective of ABO blood types. However, in the oligosaccharide binding assay, the VP8* proteins displayed no specific binding to the HBGAs tested, including Lewis b and H1. The structure of RotaTeq P[8] VP8* was solved at 1.9A. Structural comparisons revealed that the putative receptor binding site was different to that of other genotypes and displayed a novel potential binding region. These findings indicate RotaTeq and Rotarix may have better efficiency in areas with a high percentage of secretors. Binding specificity of P[8] VP8* proteins of rotavirus vaccine strains with histo-blood group antigens.,Sun X, Guo N, Li D, Jin M, Zhou Y, Xie G, Pang L, Zhang Q, Cao Y, Duan ZJ Virology. 2016 Aug;495:129-35. doi: 10.1016/j.virol.2016.05.010. Epub 2016 May, 19. PMID:27209447 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat proteins 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA