Abstract
Hypodermins A (HA), B (HB) and C (HC) are the major proteases secreted by first-instar larvae of Hypoderma lineatum (Diptera: Oestridae). These proteases are involved in the larval migration in the tissue, and prevent the activation of the host immune response. We previously showed that the recombinant HA functions as an immunosuppressive agent which could inhibit the rejection of xenotransplants. In the current study, we cloned the cDNA sequence of HC, which was transfected in Cos7 cells using the pEF1α-IRES-AcGFP expression vector. The Cos7 cells stably expressed HC, and were more resistant to lysis by guinea pig C3 than the control cells. The HC protease degraded the guinea pig C3, and inhibited the complement pathway in vitro. The DNA binding sites of HC were identified using an electrophoretic mobility shift assay. Our findings suggest that the recombinant HC might be useful as an immunosuppressive agent for the inhibition of the xenotransplant rejection.
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