[The Expression and Purification of P[4],P[6] and P[8] Rotavirus VP8 * core Proteins].

Xiaoman Sun, Nijun Guo, Dandi Li, Xin Ma, Zhaojun Duan
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Abstract

P[4], P[6] and P[8] rotaviruses (RVs) are the most prevalent RV genotypes in the population. In order to further investigate the receptor binding and structural character of P[4], P[6] and P[8] RVs, VP8 * core proteins of the P[4], P[6] and P[8] RV strains isolated directly in the stool samples in China were expressed and purified with the GST and His-tag respectively. The GST-fusion protein was approximately 46 kDa while the His-tag proteins approximately 20 kDa. In conclusion, the recombinant plasmids of PGEX4T-1-VP8 * core and pET30a-VP8 * core were constructed and the VP8 * core proteins were successfully expressed in the soluble form by using E.coli expression system. These findings provide the basis for the futhure functional and structural studies of VP8 * proteins.

P[4]、P[6]、P[8]轮状病毒VP8 *核心蛋白的表达与纯化[j]。
P[4]、P[6]和P[8]轮状病毒(RV)是人群中最常见的RV基因型。为了进一步研究P[4]、P[6]和P[8] RV的受体结合和结构特征,我们分别用GST和His-tag对中国直接分离的P[4]、P[6]和P[8] RV菌株的VP8 *核心蛋白进行了表达和纯化。gst融合蛋白约为46 kDa,而His-tag蛋白约为20 kDa。综上所述,构建了PGEX4T-1-VP8 * core和pET30a-VP8 * core重组质粒,并利用大肠杆菌表达系统成功表达了VP8 * core蛋白的可溶性形式。这些发现为VP8 *蛋白的功能和结构研究奠定了基础。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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