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Title of Journal: Parasitol Res

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Abbravation: Parasitology Research

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Springer-Verlag

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DOI

10.1007/s12613-011-0470-5

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1432-1955

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Extracellular release of the surface metalloprotea

Authors: Charles L Jaffe Dennis M Dwyer
Publish Date: 2003/08/16
Volume: 91, Issue: 3, Pages: 229-237
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Abstract

Protease activity was found in spent culture medium collected from Leishmania donovani L mexicana L major as well as the insect trypanosomatids Crithidia luciliae and Leptomonas seymouri Released protease activity increased linearly over time and was correlated to promastigote density In SDSPAGE zymogram gels showed that the proteases molecular weight ranged from 43–100 kDa Spent culture medium proteases were blocked by the metalloprotease inhibitors 110phenanthroline and ZTyrLeuNHOH but not by bestatin leupeptin ABESF pepstatin A E64 or aprotinin Monoclonal and/or polyclonal antibodies to the leishmanial gp63 reacted with the released Crithidia Leptomonas L major and L donovani proteases Cell surface biotinylation and immune precipitation using gp63specific antibodies showed that 34 of the released protease originated from the surface Antibodies against the Trypanosoma brucei variable surface glycoprotein crossreactive determinant CRD did not recognize this activity suggesting that the gp63 is not cleaved from the cell surface by a parasite phospholipase but is released by an alternative mechanism

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