Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Crithidia fasciculata, and Herpetomonas samuelpessoai.
Promastigotes of thirteen species of Leishmania isolated from human patients, as well as L. enriettii, Crithidia fasciculata and Herpetomonas samuelpessoai, were examined for the expression of an amphiphilic, surface-oriented metalloproteinase by surface radioiodination of living cells, fractionation by Triton X-114 extraction and phase separation, and zymogram analysis by fibrinogen-SDS-PAGE. In all species of Leishmania, and the two monoxenous trypanosomatid parasites of insects, an ectoproteinase similar to the Promastigote Surface Protease, or PSP, was observed. In contrast, neither Phytomonas sp. nor 'Leishmania tarentolae' express a detectable surface metalloproteinase. The presence of the functionally conserved metalloproteinase at the surface of Crithidia and Herpetomonas suggest the enzyme may not be involved in the infection of the mammalian host by Leishmania, but rather contributes to the survival of the protozoan in the environment of the insect midgut.
Institut de Biochimie, Université de Lausanne, Epalinges, Switzerland.
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Etges
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D016831:Crithidia fasciculata / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D005340:Fibrinogen / Q000378:metabolism; D006801:Humans; D007891:Leishmania / Q000201:enzymology*; D008666:Metalloendopeptidases / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D010449:Peptide Mapping; D011480:Protease Inhibitors / Q000494:pharmacology; D014351:Trypanosomatina / Q000201:enzymology*
D011480:Protease Inhibitors; D005340:Fibrinogen; D008666:Metalloendopeptidases