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The MGF300-2R Protein of African Swine Fever Virus Promotes IKKβ Ubiquitination by Recruiting the E3 Ubiquitin Ligase TRIM21
по: Zhanhao Lu, Rui Luo, Jing Lan, Shengmei Chen, Hua-Ji Qiu, Tao Wang, Yuan Sun
Формат: | Article |
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Опубликовано: | MDPI AG 2024-06-01 |
Описание
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<i>β</i> via selective autophagy. However, the E3 ubiquitin ligase responsible for IKK<i>β</i> 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<i>β</i> ubiquitination. Finally, we indicated that the degradation of IKK<i>β</i> by MGF300-2R was dependent on TRIM21. In summary, our results indicate TRIM21 is the E3 ubiquitin ligase involved in the degradation of IKK<i>β</i> 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.