Natural immunity is the body’s first line of defense against pathogen invasion. Mitochondrial protein MAVS is a key node protein in innate immune antiviral signal transduction. After the RNA virus infects the body, the signal transduction molecule MAVS forms prion protein-like aggregates, thereby activating the antiviral immune response. Moderate MAVS activation can help the body resist exogenous viral infection, but excessive activation or spontaneous aggregation of MAVS can lead to autoimmune disorders. Therefore, moderate activation of MAVS is critical for host-mediated antiviral innate immunity. However, the molecular mechanisms that inhibit spontaneous aggregation of MAVS in resting cells remain unclear.
Recently, the team of Professor Gao Chengjiang from Shandong University School of Basic Medicine published online in the journal Nature Communications the research results titled The protein arginine methyltransferase PRMT9 attenuates MAVS activation through arginine methylation .
Professor Gao Chengjiang’s team screened members of the protein arginine methyltransferase (PRMT) family and found that arginine methyltransferase PRMT9 plays a negative regulatory role in the antiviral immune response. Under physiological conditions, PMRT9 is located in mitochondria, directly binds to MAVS and catalyzes the symmetric dimethylation modification of MAVS, thereby inhibiting the aggregation and activation of MAVS. RNA virus infection weakens the mitochondrial localization of PRMT9 and its inhibitory effect on MAVS, reduces the methylation and modification of MAVS, and then promotes the aggregation and activation of MAVS, upregulating the expression of type I interferon and antiviral immune response. This study revealed a new form of post-translational modification of MAVS protein and further improved the regulatory mechanism of antiviral signaling pathways.
Bai Xuemei, a doctoral candidate in the School of Basic Medicine of Shandong University, is the first author. Professor Gao Chengjiang of the School of Basic Medicine of Shandong University and Liu Bingyu, a young teacher in the School of Basic Medicine of Shandong University are the co-corresponding authors of the paper. Shandong University is the first author. Affiliation and affiliation of the sole corresponding author.
Article link:
https://www.nature.com/articles/s41467-022-32628-y
Reprinted from:
https://www.view.sdu.edu.cn/in fo/1021/168700.htm
Publisher: Eleven
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