HYDROLYSIS OF HEMOGLOBIN BY SCHISTSOMA MANSONI CATHEPSIN B-LIKE CYSTEINE PROTEA

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. In the initial analysis for this project, purified recombinant Schistosome cathepsin B was incubated with hemoglobin, and fragments of hemoglobin degradation identified. Initial cleavage appeared to be in a "weak link" of the hemoglobin chain known to be cleaved by other hemoglobin degrading proteases. Subsequent degradation was rapid and yielded only small peptide fragments. This study confirmed the efficacy of the schistosome cathepsin B as a "hemoglobinase". We will now turn our attention to validating hemoglobin and other host-serum proteins as substrates for schistosome digestive proteases in a more "in vivo" setting. Contents of schistosome guts regurgitated following development in mouse models of infection are being separated and analyzed for specific protein fragments. We are planning to identify both what substrates are cleaved, as well as the sites of cleavage so that we can use this information to identify putative proteases from the schistosome gut that may be responsible for specific cleavage fragments.