Molecular cloning of porcine 2 ',5 '-oligoadenylate synthetase-like protein and its role in porcine reproductive and respiratory syndrome virus infection

Porcine 2',5'-oligoadenylate synthetase-like protein is an essential antiviral protein induced by interferons; however, its bioinformatics, genetic characteristics and immunological characteristics related to porcine reproductive and respiratory syndrome virus are still unknown. In this study, porcine 2',5'-oligoadenylate synthetase-like protein was cloned, and various attributes were predicted by bioinformatics analysis. Through RNAi depletion and overexpression methods, it was determined that porcine OASL not only inhibits porcine reproductive and respiratory virus replication but also activates interferon-beta production and the interferon-beta promoter, promoting the expression of interferon-beta mRNA. Through the depletion of different amino acids at the N and C termini, the antiviral activity and promoting the activity of interferon beta were evaluated. The results demonstrated that 31-60 amino acids at the N terminus were critical for virus replication. This study laid a theoretical foundation for exploring the characteristics of the porcine 2',5'-oligoadenylate synthetase-like protein and suggested a new strategy for the prevention and control of porcine reproductive and respiratory syndrome virus and investigation of the therapeutic mechanism of this protein.