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腺病毒衣壳蛋白在进入人或啮齿动物细胞后与热休克蛋白70(HSP70)相互作用。

Adenovirus capsid proteins interact with HSP70 proteins after penetration in human or rodent cells.

作者信息

Niewiarowska J, D'Halluin J C, Belin M T

机构信息

Laboratoire de Virologie Moléculaire, INSERM U.233, Lille, France.

出版信息

Exp Cell Res. 1992 Aug;201(2):408-16. doi: 10.1016/0014-4827(92)90290-o.

DOI:10.1016/0014-4827(92)90290-o
PMID:1639138
Abstract

Soon after penetration of adenovirus serotype 2 in BHK-21 and HeLa cells, HSP70 and HSC70 proteins become associated with the viral capsid. By analysis with a polyclonal antibody derived from a fusion protein containing the C-terminal domain, 290 amino acids of HSP70, and using both immunological methods and infected cells fractionation we observed that a significant amount of HSP70 proteins moved to the nucleus and colocalized with the adenovirus particles. HSP70 proteins of infected cells were isolated as a complex cross-linked with intracytoplasmic adenovirus type 2. By coprecipitation, using a polyclonal-specific antiserum derived from the fusion protein, or two different monoclonal-specific antisera, we showed that HSP70 and HSC70 proteins were associated with hexon, the major adenovirus capsid protein.

摘要

腺病毒血清型2侵入BHK - 21和HeLa细胞后不久,热休克蛋白70(HSP70)和热休克同源蛋白70(HSC70)就会与病毒衣壳结合。通过使用源自包含HSP70 C末端结构域(290个氨基酸)的融合蛋白的多克隆抗体进行分析,并结合免疫方法和感染细胞分级分离,我们观察到大量的HSP70蛋白转移到细胞核并与腺病毒颗粒共定位。感染细胞的HSP70蛋白以与细胞质内2型腺病毒交联的复合物形式被分离出来。通过使用源自融合蛋白的多克隆特异性抗血清或两种不同的单克隆特异性抗血清进行共沉淀,我们发现HSP70和HSC70蛋白与腺病毒主要衣壳蛋白六邻体相关联。

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