Heat shock protein A1 inhibits the replication of foot-and-mouth disease virus by degrading viral RNA polymerase 3D through chaperone-mediated autophagy

Viral RNA replication is the key stage in understanding the pathogenic mechanisms of foot-and-mouth disease virus (FMDV). During this process, the viral non-structural protein 3D serves as an RNA-dependent RNA polymerase (RdRp) to synthesize progeny RNA using the viral genomic RNA as a template. However, the regulatory effect of host cells on FMDV 3D proteins has not yet been studied. In this study, we find that heat shock protein A1 (HSPA1) degrades the viral 3D protein through the chaperone-mediated autophagy (CMA) pathway, thereby inhibiting the RNA replication of FMDV and interfering with virus infection. This study, for the first time, demonstrates that HSPA1 employs its chaperone function to mediate the degradation of the FMDV RdRp.

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Publication Details

Journal
Journal of Virology
Published
2025-03-31
DOI
https://doi.org/10.1128/jvi.00168-25
Citations
1
Primary Topic
Animal Disease Management and Epidemiology
Type
article
Field-Weighted Citation Impact
1.90

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Heat shock protein A1 inhibits the replication of foot-and-mouth disease virus by degrading viral RNA polymerase 3D through chaperone-mediated autophagy

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1 citations
Journal of Virology
Animal Disease Management and Epidemiology
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article

Heat shock protein A1 inhibits the replication of foot-and-mouth disease virus by degrading viral RNA polymerase 3D through chaperone-mediated autophagy

Mei Ren, Huan Zhou, Shiqi Sun, Sahibzada Waheed Abdullah, Xuefei Wang, Jin’en Wu, Jianing Wang, Huichen Guo
article en
1 citations

Abstract

Viral RNA replication is the key stage in understanding the pathogenic mechanisms of foot-and-mouth disease virus (FMDV). During this process, the viral non-structural protein 3D serves as an RNA-dependent RNA polymerase (RdRp) to synthesize progeny RNA using the viral genomic RNA as a template. However, the regulatory effect of host cells on FMDV 3D proteins has not yet been studied. In this study, we find that heat shock protein A1 (HSPA1) degrades the viral 3D protein through the chaperone-mediated autophagy (CMA) pathway, thereby inhibiting the RNA replication of FMDV and interfering with virus infection. This study, for the first time, demonstrates that HSPA1 employs its chaperone function to mediate the degradation of the FMDV RdRp.

Journal of VirologyVol. 99(5)
University of Liège (BE), Gembloux Agro-Bio Tech (BE), Government of Khyber Pakhtunkhwa (PK), Lanzhou Veterinary Research Institute (CN), Chinese Academy of Agricultural Sciences (CN), Lanzhou University (CN)
National Natural Science Foundation of China, Natural Science Foundation of Gansu Province
Good health and well-being
Openalex Percentile: Top 18%
Animal Disease Management and Epidemiology
1.90
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