【摘 要】
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Cyclophilin A (CypA) is a peptidyl-prolyl cis/trans isomerase that interacts with the matrix protein (M1) of influenza A virus (IAV) and restricts virus replication by regulating the ubiquitin-proteasome-mediated degradation of M1.However,the mechanism by
【机 构】
：
CAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Aca
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Cyclophilin A (CypA) is a peptidyl-prolyl cis/trans isomerase that interacts with the matrix protein (M1) of influenza A virus (IAV) and restricts virus replication by regulating the ubiquitin-proteasome-mediated degradation of M1.However,the mechanism by which CypA regulates M1 ubiquitination remains unknown.In this study,we reported that E3 ubiquitin ligase AIP4 promoted K48-1inked ubiquitination of M1 at K102 and K104,and accelerated ubiquitin-proteasome-mediated degradation of M1.The recombinant IAV with mutant M1 (K102R/K104R) could not be rescued,suggesting that the ubiquitination of M1 at K102/K104 was essential for IAV replication.Furthermore,CypA inhibited AIP4-mediated M1 ubiquitination by impairing the interaction between AIP4 and M1.More importantly,both the mutations of M1 (K102R/K104R) and CypA inhibited the nuclear export of M1,indicating that CypA regulates the cellular localization of M1 via inhibition of AIP4-mediated M1 ubiquitination at K102 and K104,which results in the reduced replication of IAV.Collectively,our findings reveal a novel ubiquitination-based mechanism by which CypA regulates the replication of IAV.
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