| Literature DB >> 27209447 |
Xiaoman Sun1, Nijun Guo2, Dandi Li1, Miao Jin1, Yongkang Zhou1, Guangcheng Xie1, Lili Pang1, Qing Zhang1, Youde Cao3, Zhao-Jun Duan4.
Abstract
RotaTeq(®) 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 1.9Å. 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.Entities:
Keywords: Crystal structure; Histo-blood group antigens; RotaTeq; Rotarix; VP8*
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Year: 2016 PMID: 27209447 DOI: 10.1016/j.virol.2016.05.010
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616