Heat shock protein (HSP90) affects the replication of rotavirus

被引：0

作者：

Hu, Siman ^{[1
]}

Tao, Xiao-Li ^{[1
]}

Zhao, Wei ^{[1
]}

Luo, Like ^{[1
]}

Li, Runli ^{[1
]}

Ma, Zhuping ^{[1
]}

Sun, Lvyin ^{[1
]}

Li, Yong-Gang ^{[1
]}

机构：

[1] Jinzhou Med Univ, Dept Pathogen Microbiol, Jinzhou 121000, Liaoning, Peoples R China

来源：

FUTURE VIROLOGY | 2024年 / 19卷 / 6-7期

关键词：

17-AAG; HSP90; NSP2; proteasome pathway; RV; NONSTRUCTURAL PROTEIN; ACTIVE PARTICIPATION; CHAPERONE HSP90; NSP2; RNA; COMPLEX; DEGRADATION; INHIBITION; MULTIMERS; APOPTOSIS;

D O I：

10.1080/17460794.2024.2362016

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Aim: To explore the effects of HSP90 on rotavirus (RV) replication. Materials & methods: The interaction between NSP2 and HSP90 was analyzed by immunoprecipitation assay, and co-localization confirmed by an immunofluorescence assay. The viral titer was measured by immunofluorescence assay and viral protein expression investigated by western blotting. Results: The interaction between NSP2 and HSP90 was confirmed. Knockdown of HSP90 using siRNA resulted in a decrease in NSP2 expression and virus titer. HSP90 inhibitor 17-AAG significantly decreased NSP2 and NSP5 expression, as well as the virus titer, while proteasome inhibitor MG132 restored the protein amount and the viral titer. Conclusion: HSP90 is involved in rotavirus replication, and inhibition of HSP90 promotes the degradation of NSP2 through the proteasome pathway.

引用

页码：263 / 272

页数：10

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