Recombinant Serine Protease Inhibitors Alter Macrophage Polarization .

During parasite infection, serine protease inhibitors secreted by parasites play important roles in suppressing host defenses. However, the mechanism of immune regulation is unclear. In this study, a serpin gene from , named -Serpin, was cloned and expressed, in order to reveal its role in the regulation of the host immune response in infection. The results showed that -Serpin encodes a 43 kDa protein that was recognized by serum from infected mice at 60 days post-infection (dpi). -Serpin was found to be expressed at all developmental stages of . Inhibitory activity analysis showed that recombinant -Serpin (r-Serpin) effectively inhibited the hydrolytic activity of porcine pancreatic elastase (elastase P), human neutrophil elastase (elastase H), and mouse mast cell protease-1, but showed little inhibitory for human neutrophil cathepsin G (cathepsin G). Furthermore, r-Serpin induced polarization of macrophages toward the alternatively activated phenotype (M2) alone by activation of the signal transducer and activator of transcription 3 signaling pathway, and inhibited lipopolysaccharide-induced classically activation (M1) . These data preliminarily demonstrate that -Serpin may play an important role in the immunoregulation of infection by activating the M2-polarized signaling pathway.