The activation of complement on the surface of Leishmania promastigotes appears to be an important factor for parasite infectivity in the mammalian host, allowing their attachment and the invasion of macrophages via complement receptors. Mannose-binding lectin (MBL) is a well-known complement activator and an efficient opsonine. We have investigated here whether serum and purified MBL bind to and promote lysis of live promastigotes of L. braziliensis; and evaluated the deposition of MBL, C1q, C4 and C3 on the parasite surface after interaction with non-immune normal human serum (NHS). We observed that both serum MBL and the purified MBL-MASP complex bind to the surface of L. braziliensis and that this binding occurred via the carbohydrate recognition domains of MBL. The binding of MBL, however, did not affect the lytic effect of complement on the parasites. The deposition of C1q, C4, C3 and parasite lysis was observed after incubation with NHS. EDTA but not EGTA abolished C3 deposition on the parasite surface, indicating the involvement of the alternative pathway in this process. Our results indicate that MBL binds to L. braziliensis and that this is mediated by a specific carbohydrate on the surface of parasites and provides evidence for antibody-independent mechanisms that complement activation on the parasite surface.