Abstract
Papain family cysteine proteases are key factors in the pathogenesis of cancer invasion, arthritis, osteoporosis, and microbial infections. Targeting this enzyme family is therefore one strategy in the development of new chemotherapy for a number of diseases. Little is known, however, about the efficacy, selectivity, and safety of cysteine protease inhibitors in cell culture or in vivo. We now report that specific cysteine protease inhibitors kill Leishmania parasites in vitro, at concentrations that do not overtly affect mammalian host cells. Inhibition of Leishmania cysteine protease activity was accompanied by defects in the parasite's lysosome/endosome compartment resembling those seen in lysosomal storage diseases. Colocalization of anti-protease antibodies with biotinylated surface proteins and accumulation of undigested debris and protease in the flagellar pocket of treated parasites were consistent with a pathway of protease trafficking from flagellar pocket to the lysosome/endosome compartment. The inhibitors were sufficiently absorbed and stable in vivo to ameliorate the pathology associated with a mouse model of Leishmania infection.
MeSH Terms
Animals
Antiprotozoal Agents/pharmacology
Cells, Cultured
Cysteine Proteinase Inhibitors/pharmacology,therapeutic use,toxicity
Female
Leishmania major/drug effects,ultrastructure
Leishmaniasis, Cutaneous/drug therapy
Mice
Mice, Inbred BALB C
Microscopy, Electron
Chemicals
Antiprotozoal Agents
Cysteine Proteinase Inhibitors
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Selzer P M
Department of Pathology, University of California, San Francisco, CA 94143, USA.
Pingel S
Hsieh I
Ugele B
Chan V J
Engel J C
Bogyo M
Russell D G
Sakanari J A
McKerrow J H
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