Zhanhao Lu,Rui Luo,Jing Lan,Shengmei Chen,Hua-Ji Qiu,Tao Wang,Yuan Sun

Viruses.2024 Jun 12;16(6):949.doi: 10.3390/v16060949.

Abstract

African swine fever (ASF) is an acute, hemorrhagic, highly contagious disease in pigs caused by African swine fever virus (ASFV). Our previous study identified that the ASFV MGF300-2R protein functions as a virulence factor and found that MGF300-2R degrades IKK β  via selective autophagy. However, the E3 ubiquitin ligase responsible for IKK β  ubiquitination during autophagic degradation still remains unknown. In order to solve this problem, we first pulled down 328 proteins interacting with MGF300-2R through immunoprecipitation-mass spectrometry. Next, we analyzed and confirmed the interaction between the E3 ubiquitin ligase TRIM21 and MGF300-2R and demonstrated the catalytic role of TRIM21 in IKK β  ubiquitination. Finally, we indicated that the degradation of IKK β  by MGF300-2R was dependent on TRIM21. In summary, our results indicate TRIM21 is the E3 ubiquitin ligase involved in the degradation of IKK β  by MGF300-2R, thereby augmenting our understanding of the functions of MGF300-2R and offering insights into the rational design of live attenuated vaccines and antiviral strategies against ASF.

Keywords: African swine fever virus; E3 ubiquitin ligase; IKKβ; MGF300-2R; TRIM21; ubiquitin.