Characterization and expression of proteases during Trypanosoma cruzi metacyclogenesis.

Abstract:

:Investigation of protease activities during the transformation of Trypanosoma cruzi epimastigotes into metacyclic trypomastigoes (metacyclo-genesis) revealed three major components with apparent molecular weights of 65, 52, and 40 kDa. The 65-kDa protease is a metacyclic trypomastigote stage-specific protease with an isoelectric point of 5.2 whose activity is inhibited by 1,10-phenanthroline, suggesting that it might be a metalloprotease. The 52-kDa component is also a metalloprotease which is constitutively expressed in epimastigotes and metacyclic trypomastigoes. On the other hand, the 40-kDa component is apparently made up of several isoforms of a cysteine protease which is expressed in much higher levels in epimastigotes than in metacyclic trypomastigote forms. The fact that the 65- and 40-kDa proteases are developmentally regulated suggests that proteases might be important for T. cruzi differentiation. Accordingly, T. cruzi metacyclogenesis is blocked by metallo- and cysteine-protease inhibitors.

journal_name

Exp Parasitol

authors

Bonaldo MC,d'Escoffier LN,Salles JM,Goldenberg S

doi

10.1016/0014-4894(91)90006-i

subject

Has Abstract

pub_date

1991-07-01 00:00:00

pages

44-51

issue

1

eissn

0014-4894

issn

1090-2449

pii

0014-4894(91)90006-I

journal_volume

73

pub_type

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