DNAJA3 interacts with ASFV MGF360-14L protein and reduces MGF360-14L antagonistic role on Beta interferon production

文献类型： 外文期刊

第一作者： Wang, Zhen

作者： Wang, Zhen;Wang, Yang;Cui, Shuai;Tao, Chunhao;Huang, Ying;Zhu, Hongfei;Jia, Hong;Wang, Zhen;Zhao, Peng

作者机构：

关键词： African swine fever virus; MGF360-14L; Interferon; DNAJA3; Lysosomal degradation

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.5； 五年影响因子：8.7 ）

ISSN： 0141-8130

年卷期： 2025 年 310 卷

页码：

收录情况： SCI

摘要： African swine fever (ASF) is a devastating infectious disease caused by African swine fever virus (ASFV). Many multiple structural and non-structural proteins of ASFV have been confirmed to evade the host's immune response. In this study, the interaction of non-structural protein MGF360-14L with DnaJ heat shock protein family (Hsp40) member A3 (DNAJA3) were firstly detected by yeast two-hybrid screening, further confirmed by communoprecipitation and colocalization, meanwhile we also found that MGF360-14L was localized in the cytoplasm. The DNAJA3 (amino acids 296 to 453) and the MGF360-14L (amino acids 1 to 119) were shown to be critical for the interaction of DNAJA3 with MGF360-14L. Over-expression of DNAJA3 dramatically dampened MGF360-14L expression, and induced lysosomal degradation of MGF360-14L. Our study have previously demonstrated that the MGF360-14L induced ubiquitin degradation of IRF3 and thus inhibited the production of IFN-beta. Further research showed that MGF360-14L can significantly enhance the ubiquitination-mediated degradation of IRF3 and strengthen the suppression of IFN-beta in DNAJA3-knockout cells. These findings suggest that the DNAJA3 played a negative regulatory role for the inhibition of MGF360-14L on the IFN-beta, further study indicated that DNAJA3 plays an important antiviral role against ASFV by both degrading MGF360-14L and restoring of IFN-beta.

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