{"title":"P[4]、P[6]、P[8]轮状病毒VP8 *核心蛋白的表达与纯化[j]。","authors":"Xiaoman Sun, Nijun Guo, Dandi Li, Xin Ma, Zhaojun Duan","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>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>","PeriodicalId":8776,"journal":{"name":"Bing du xue bao = Chinese journal of virology","volume":"32 3","pages":"256-62"},"PeriodicalIF":0.0000,"publicationDate":"2016-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"[The Expression and Purification of P[4],P[6] and P[8] Rotavirus VP8 * core Proteins].\",\"authors\":\"Xiaoman Sun, Nijun Guo, Dandi Li, Xin Ma, Zhaojun Duan\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>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>\",\"PeriodicalId\":8776,\"journal\":{\"name\":\"Bing du xue bao = Chinese journal of virology\",\"volume\":\"32 3\",\"pages\":\"256-62\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2016-05-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bing du xue bao = Chinese journal of virology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bing du xue bao = Chinese journal of virology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
[The Expression and Purification of P[4],P[6] and P[8] Rotavirus VP8 * core Proteins].
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.