Binding specificity of P[8] VP8proteins of rotavirus vaccine strains with histo-blood group antigens
Binding specificity of P[8] VP8proteins of rotavirus vaccine strains with histo-blood group antigens
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轮状病毒疫苗株P[8]VP8蛋白与组织血型抗原的结合特异性
DOI：
10.1016/j.virol.2016.05.010
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发表时间：
2016
期刊：
影响因子：
3.7
通讯作者：
Cao YD
中科院分区：
文献类型：
--
作者：
Sun Xiaoman;Li D;i;Jin Miao;Zhou Yongkang;Xie Guangcheng;Pang Lili;Zhang Qing;Duan Zhao-Jun;Sun Xiaoman;Li D;i;Jin Miao;Zhou Yongkang;Xie Guangcheng;Pang Lili;Zhang Qing;Duan Zhao-Jun;Guo Nijun;Cao Youde;Duan ZJ;Cao YD
RotaTeq®和Rotarix™是目前全球市场上两种常见的人轮状病毒（RV）疫苗。最近的研究表明，组织血型抗原（HBGAs）可能是RV的附着因子。表达和纯化RotaTeq和Rotarix的P[8] VP 8 * 蛋白，并评估其结合特异性。唾液结合试验表明，VP 8 * 蛋白结合的唾液样本的分泌ABO血型无关。然而，在寡糖结合试验中，VP 8 * 蛋白未显示与所测试的HBGA（包括刘易斯B和H1）的特异性结合。RotaTeq P[8] VP 8 * 的结构在1.9 ℃下解析。结构比较表明，推定的受体结合位点是不同的其他基因型，并显示一个新的潜在的结合区域。这些发现表明RotaTeq和Rotarix在分泌细胞比例高的区域可能具有更好的效率。
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 1.9 Å. 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.