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The heat shock protein DNAJB8 inhibits pseudorabies virus replication by autophagy.
Chen, Xiaoyong; Li, Wenfeng.
Afiliação
  • Chen X; Xingzhi College, Zhejiang Normal University, Jinhua, Zhejiang, PR China. Electronic address: chenxy93@zjnu.edu.cn.
  • Li W; College of Animal Science, Wenzhou Vocational College of Technology and Science, Wenzhou, Zhejiang, PR China.
Vet Microbiol ; 295: 110165, 2024 Aug.
Article em En | MEDLINE | ID: mdl-38936156
ABSTRACT
Pseudorabies virus (PRV) effectively utilizes numerous host proteins and pathways to establish a successful infection. Consequently, it becomes imperative to investigate novel host factors implicated in viral infections to gain a deeper understanding of PRV pathogenesis. In this study, we reveal that the host heat shock protein, DNAJB8, functions as a negative regulator in PRV replication. Our findings indicated that both mRNA and protein levels of DNAJB8 were downregulated in cells infected with PRV. Further analysis demonstrated that overexpressing DNAJB8 suppressed PRV replication, whereas its knockdown enhanced viral replication. From a mechanistic perspective, DNAJB8 promoted cellular autophagy, subsequently impeding viral replication. Additionally, we discovered that the transcription factor SOX30 regulated DNAJB8 expression, thereby influencing viral replication. Collectively, these findings enhance our comprehension of the roles played by DNAJB8 and SOX30 in viral replication, broadening our knowledge of virus-host interactions.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Autofagia / Replicação Viral / Herpesvirus Suídeo 1 / Proteínas de Choque Térmico HSP40 Limite: Animals Idioma: En Revista: Vet Microbiol Ano de publicação: 2024 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Autofagia / Replicação Viral / Herpesvirus Suídeo 1 / Proteínas de Choque Térmico HSP40 Limite: Animals Idioma: En Revista: Vet Microbiol Ano de publicação: 2024 Tipo de documento: Article