Characterization of a surface metalloprotease from Herpetomonas samuelpessoai and comparison with Leishmania major promastigote surface protease.

Details

Serval ID
serval:BIB_8650ECC5B2A6
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Characterization of a surface metalloprotease from Herpetomonas samuelpessoai and comparison with Leishmania major promastigote surface protease.
Journal
Molecular and Biochemical Parasitology
Author(s)
Schneider P., Glaser T.A.
ISSN
0166-6851 (Print)
ISSN-L
0166-6851
Publication state
Published
Issued date
1993
Volume
58
Number
2
Pages
277-282
Language
english
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
The monogenetic kinetoplastid protozoan parasite Herpetomonas samuelpessoai expresses a surface-exposed metalloprotease. Comparable to the Leishmania promastigote surface protease, or PSP, the protease of Herpetomonas is active at the surface of fixed and live organisms, and both enzymes display an identical cleavage specificity toward a nonapeptide substrate. The protease was enriched 440 times by partition into Triton X-114 followed by 2 steps of anion exchange chromatography. The 56-kDa enzyme is inhibited by the metal chelator 1,10-phenanthroline and is susceptible to cleavage by glycosyl-phosphatidylinositol phospholipase C (GPI-PLC). The conservation of an identical surface protease activity in these monogenetic and digenetic trypanosomatids suggests that the enzyme has a physiological function in the promastigote (insect) stage of these parasites.
Keywords
Amino Acid Sequence, Animals, Leishmania tropica/enzymology, Metalloendopeptidases/antagonists & inhibitors, Metalloendopeptidases/isolation & purification, Molecular Sequence Data, Oligopeptides/chemistry, Phenanthrolines/pharmacology, Species Specificity, Substrate Specificity, Trypanosomatina/enzymology
Pubmed
Web of science
Create date
19/01/2008 17:30
Last modification date
20/08/2019 14:45
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