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作 者:徐嘉欣 武雪宁 王显赫 徐梧皓 高鑫誉 郑亮[1,2] 吴志军 张华[1,2,3] 曹宏伟 Xu Jiaxin;Wu Xuening;Wang Xianhe;Xu Wuhao;Gao Xinyu;Zheng Liang;Wu Zhijun;Zang hua;Cao Hongwei(College of Life Science and Technology,Heilongjiang Bayi Agricultural University,Daqing 163319;College of Animal Science and Technology,Heilongjiang Bayi Agricultural University;Biotechnology Center,Heilongjiang Bayi Agricultural University)
机构地区:[1]黑龙江八一农垦大学生命科学技术学院,大庆163319 [2]黑龙江八一农垦大学动物科技学院 [3]黑龙江八一农垦大学生物技术中心
出 处:《黑龙江八一农垦大学学报》2021年第5期80-85,共6页journal of heilongjiang bayi agricultural university
基 金:黑龙江八一农垦大学校内培育课题重点项目(XA2017-02)。
摘 要:Nsp6是PEDV编码的非结构蛋白,目前关于Nsp6蛋白的结构和功能研究尚不清楚。为了更加清晰了解PEDV Nsp6的功能,通过无缝克隆技术、Western blot和间接免疫荧光等方法验证Nsp6蛋白的表达和细胞定位。此外,研究发现Nsp6能与内质网膜关键蛋白PDI共定位,并能引起内质网应激相关蛋白GRP78表达上调。初步证明了Nsp6蛋白能够引起内质网应激反应,为拓展Nsp6蛋白的结构和功能研究提供理论依据。Nsp6 was a non-structural protein encoded by PEDV,and its structure and function were still unclear.In order to understand the function of PEDV Nsp6 protein more clearly,Expression and cellular localization of Nsp6 protein were verified through seamless cloning technology,Western blot and indirect immunofluorescence methods.In addition,studies had found that Nsp6 protein could co-localize with the key endoplasmic reticulum membrane protein PDI,and cause the expression of the endoplasmic reticulum stress-related protein GRP78 to increase.It preliminarily proved that Nsp6 protein could cause endoplasmic reticulum stress response,which would provide a theoretical basis for expanding the structure and function of Nsp6 protein.
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