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Functional and structural diversity of the cathepsin L peptidase from the human blood fluke Schistosoma mansoni

Funding: 2005: $95,000
2006: $95,000
2007: $90,000

Funding or Partner Organisation: Australian Research Council (Other funds for ARC projects)
Australian Research Council (ARC Discovery Projects)

Start year: 2005

Summary: Two enzymes, cathepsin L1 and cathepsin L2, are used to digest haemoglobin in host blood from which the human parasite Schistosoma mansoni obtains its nutrient. The two enzymes arose early in evolution from a common ancestor and since then have diverged in structure and biochemistry. We aim to understand how the changes that took place over time endowed each enzyme with its particular properties. These studies will help us understand how enzymes evolved to perform specific functions and will aid future programmes in the design of new parasite treatments directed at peptidases that are essential to parasite survival.


Donnelly, S, Stack, CM, O'Neill, SM, Sayed, AA, Williams, DL & Dalton, JP 2008, 'Helminth 2-Cys peroxiredoxin drives Th2 responses through a mechanism involving alternatively activated macrophages', FASEB JOURNAL, vol. 22, no. 11, pp. 4022-4032.
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Keywords: proteases, parasites, helminths, enzymes, 3D structure, biochemical,

FOR Codes: Medical Parasitology, Genetic Engineering and Enzyme Technology, Enzymes, Infectious diseases, Prevention-biologicals (e.g. vaccines), Biocatalysis and Enzyme Technology, Human Biological Preventatives (e.g. Vaccines), Veterinary Biological Preventatives (e.g. Vaccines), Medical parasitology , Clinical health, Veterinary pharmaceutical products, Human pharmaceutical products