Biochemical and Biophysical Research Communications, Год журнала: 2024, Номер 746, С. 151244 - 151244
Опубликована: Дек. 31, 2024
Язык: Английский
Current Opinion in Cell Biology, Год журнала: 2025, Номер 93, С. 102481 - 102481
Опубликована: Фев. 14, 2025
Язык: Английский
Процитировано
0
Journal of Virology, Год журнала: 2025, Номер unknown
Опубликована: Март 31, 2025
ABSTRACT Foot-and-mouth disease virus (FMDV), a member of the Picornaviridae family, is single-stranded, positive-sense RNA virus. Heat shock protein A1 (HSPA1) has been shown to influence entry, translation, assembly, and release enterovirus A71 (EV-A71), another family member. In this study, we demonstrate that HSPA1 plays different role in replication FMDV. By investigating various stages replication, found specifically inhibits stage which viral by degrading RNA-dependent polymerase (RdRp), 3D protein. presence specific inhibitors, find out degradation occurs through autophagy pathway. Activation blockage chaperone-mediated (CMA) degrades CMA Mutation analysis reveals 421 QEKLI 425 key motif responsible for HSPA1-mediated degradation. summary, study shows can degrade pathway, thereby inhibiting FMDV interfering with infection. This first time, demonstrates employs its chaperone function mediate RdRp, revealing crucial infection process suggesting could be potential target prevention treatment IMPORTANCE Viral understanding pathogenic mechanisms foot-and-mouth (FMDV). During process, non-structural serves as an (RdRp) synthesize progeny using genomic template. However, regulatory effect host cells on proteins not yet studied. heat RdRp.
Язык: Английский
Процитировано
0
Biochemical and Biophysical Research Communications, Год журнала: 2024, Номер 744, С. 151219 - 151219
Опубликована: Дек. 19, 2024
Язык: Английский
Процитировано
0
Biochemical and Biophysical Research Communications, Год журнала: 2024, Номер 746, С. 151244 - 151244
Опубликована: Дек. 31, 2024
Язык: Английский
Процитировано
0