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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

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

作者机构：

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

期刊名称： International Journal of Biological Macromolecules

ISSN： 0141-8130

年卷期： 2025 年 310 卷

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

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-β. Further research showed that MGF360-14L can significantly enhance the ubiquitination-mediated degradation of IRF3 and strengthen the suppression of IFN-β in DNAJA3-knockout cells. These findings suggest that the DNAJA3 played a negative regulatory role for the inhibition of MGF360-14L on the IFN-β, further study indicated that DNAJA3 plays an important antiviral role against ASFV by both degrading MGF360-14L and restoring of IFN-β.

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