دورية أكاديمية

HSP70 positively regulates translation by interacting with the IRES and stabilizes the viral structural proteins VP1 and VP3 to facilitate duck hepatitis A virus type 1 replication

التفاصيل البيبلوغرافية
العنوان: HSP70 positively regulates translation by interacting with the IRES and stabilizes the viral structural proteins VP1 and VP3 to facilitate duck hepatitis A virus type 1 replication
المؤلفون: Yurui Jiang, Chenxia Xu, Anchun Cheng, Mingshu Wang, Wei Zhang, Xinxin Zhao, Qiao Yang, Ying Wu, Shaqiu Zhang, Bin Tian, Juan Huang, Xumin Ou, Di Sun, Yu He, Zhen Wu, Dekang Zhu, Renyong Jia, Shun Chen, Mafeng Liu
المصدر: Veterinary Research, Vol 55, Iss 1, Pp 1-14 (2024)
بيانات النشر: BMC, 2024.
سنة النشر: 2024
المجموعة: LCC:Veterinary medicine
مصطلحات موضوعية: DHAV-1, HSP70, IRES, VP1, VP3, translation, Veterinary medicine, SF600-1100
الوصف: Abstract The maintenance of viral protein homeostasis depends on the interaction between host cell proteins and viral proteins. As a molecular chaperone, heat shock protein 70 (HSP70) has been shown to play an important role in viral infection. Our results showed that HSP70 can affect translation, replication, assembly, and release during the life cycle of duck hepatitis A virus type 1 (DHAV-1). We demonstrated that HSP70 can regulate viral translation by interacting with the DHAV-1 internal ribosome entry site (IRES). In addition, HSP70 interacts with the viral capsid proteins VP1 and VP3 and promotes their stability by inhibiting proteasomal degradation, thereby facilitating the assembly of DHAV-1 virions. This study demonstrates the specific role of HSP70 in regulating DHAV-1 replication, which are helpful for understanding the pathogenesis of DHAV-1 infection and provide additional information about the role of HSP70 in infection by different kinds of picornaviruses, as well as the interaction between picornaviruses and host cells.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1297-9716
Relation: https://doaj.org/toc/1297-9716
DOI: 10.1186/s13567-024-01315-9
URL الوصول: https://doaj.org/article/eaf6e7ad05e24e839e5d610d313a9577
رقم الأكسشن: edsdoj.f6e7ad05e24e839e5d610d313a9577
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:12979716
DOI:10.1186/s13567-024-01315-9