Protein synthesis and release by cultured schistosomula ofSchistosoma mansoni

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Abstract
The lung schistosomulum of Schistosoma mansoni is the target of protective immunity in mice singly vaccinated with irradiated cercariae. Since the effector responses are T cell-mediated, their initiation requires the release of antigens from the intact parasite. We have used the technique of biosynthetic labelling with ‘35S’methionine, before and after transformation of the cercariae, to analyse the kinetics of protein synthesis and release by the schistosomulum. In addition, the proteins present in the soluble fraction of the parasite and those released during in vitro culture have been characterized. During a 7-day culture period schistosomula derived from labelled cercariae lost proteins most rapidly within the first 3 h after transformation. Two proteins of molecular weight 61 and 20 kDa were dominant and may correspond to areas of proteolytic activity. Analysis of the rate of protein synthesis of schistosomula labelled after transformation revealed four different phases, which may relate to the developmental processes occurring in vivo. During the first 24 h, synthesis was very low, increasing to a plateau and then rising to a peak at day 8; thereafter the rate declined rapidly. Whilst some stage-specific synthesis of proteins was detected in the soluble fractions of the parasite bodies, the pattern of proteins released by cultured larvae was remarkably uniform. At least 15 proteins were detected by autoradiography with bands at 61, 45 and 20 kDa being particularly prominent. These proteins merit further study as potential mediators of the protective immune response.