人和动物C组轮状病毒VP8*蛋白糖结合特征的研究

Glycan binding specificity of VP8^* proteins of human and animal group C rotavirus

目的研究人和动物C组轮状病毒VP8^*蛋白与糖的结合特征,为人和动物C组轮状病毒感染机制提供基础和依据.方法利用原核表达系统表达并纯化人和动物病毒毒株的VP8^*蛋白,通过糖点阵实验、寡糖结合实验及血凝实验等方法研究其糖结合特征.结果人C组轮状病毒sz94 VP8^*蛋白不仅与A糖结合,还与黏蛋白核心mucin core 4糖结合.狗C组轮状病毒糖点阵实验显示,可以结合A糖,人和狗C组轮状病毒可以凝集A型红细胞,猪P[5]、P[8]、P[19]、P[21]与实验中的寡糖都没有结合,也都没有凝集各型红细胞.结论黏蛋白核心在人C组轮状病毒可能是潜在的粘附分子,A型组织血型抗原可能也是某些动物C组轮状病毒的粘附分子,猪C组轮状病毒具体结合的糖类型还需进一步探索.

Objective To explore the glycan binding specificity of VP8^* protein of human and some animal group C rotavirus (RVC), so as to provide certain basis and evidence for illustrating the mechanism of human and animal RVC infection and epidemiology. Methods The VP8^* proteins of human and animal RVC were expressed with prokaryotic expression system and were purified. Interactions between RVC VP8^* proteins and glycans were explored by the glycan microarray assay, oligosaccharide binding assay and hemagglutination assay. Results Human RVC sz94 VP8^* protein bound to type A glycan, and mucin core 4 oligosaccharide. Dog RVC VP8* showed binding to type A glycan in the glycan microarray assay. Human RVC and dog RVC hemagglutinated type A blood cells. Porcine RVCs P[5], P[8], P[19] and P[21] VP8^*s showed no binding to all tested oligosaccharides and no hemagglutination on all types of blood cells. Conclusions Mucin core maybe a potential attachment factor of human RVC while type A glycans may be potential cell attachment factors for some animal RVCs. Glycan binding patterns of procine RVC need further exploration.