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Host cell protein PSMB10 interacts with viral NS3 protein and inhibits the growth of classical swine fever virus

机译:宿主细胞蛋白PSMB10与病毒NS3蛋白相互作用,抑制古典猪瘟病毒的生长

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摘要

Classical swine fever (CSF) is a major infectious disease of pigs caused by classical swine fever virus (CSFV). NS3 is one of the non-structural proteins of CSFV and plays an important role in the infection process. However, the NS3-interacting cellular proteins involved in viral replication are poorly documented. In this study, proteasome subunit beta 10 (PSMB10) was identified as a novel NS3-interacting partner using yeast two-hybrid screening of a porcine peripheral blood mononuclear cell (PBMC) cDNA library. The PSMB10-NS3 interaction was confirmed by co-immunoprecipitation, glutathione S-transferase pulldown, and laser confocal microscopy. Overexpression of PSMB10 inhibited CSFV replication. Conversely, CSFV infection inhibited PSMB10 expression. Furthermore, we demonstrated that NS3 is degraded by PSMB10 through the ubiquitin-proteasome system and that CSFV inhibits the expression of MHC class I antigen presentation-related transporter proteins, whereas PSMB10 can restore the function of MHC class I antigen presentation and inhibit CSFV proliferation.
机译:古典猪瘟(CSF)是由古典猪瘟病毒(CSFV)引起的猪的主要传染病。 NS3是CSFV的非结构蛋白之一,在感染过程中起重要作用。然而,参与病毒复制的NS3相互作用蛋白质记录不佳。在该研究中,使用猪外周血单核细胞(PBMC)cDNA文库的酵母双杂交筛选鉴定蛋白酶体亚基β10(PSMB10)作为新的NS3相互作用伴侣。通过共免疫沉淀,谷胱甘肽S-转移酶下拉和激光共聚焦显微镜证实了PSMB10-NS3相互作用。 PSMB10的过度表达抑制了CSFV复制。相反,CSFV感染抑制了PSMB10表达。此外,我们证明NS3通过泛素 - 蛋白酶体系通过PSMB10降解,并且CSFV抑制MHC I类抗原呈递相关的转运蛋白的表达,而PSMB10可以恢复MHC I类抗原呈递和抑制CSFV增殖的功能。

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