Back to Search
Start Over
Trypanosoma brucei brucei oligopeptidase B null mutants display increased prolyl oligopeptidase-like activity.
- Source :
-
Molecular and biochemical parasitology [Mol Biochem Parasitol] 2012 Mar-Apr; Vol. 182 (1-2), pp. 7-16. Date of Electronic Publication: 2011 Nov 22. - Publication Year :
- 2012
-
Abstract
- African trypanosomosis is a parasitic disease in man and animals caused by protozoan parasites of the genus Trypanosoma. Nagana, the cattle form of the disease, is caused by Trypanosoma congolense, Trypanosoma vivax and Trypanosoma brucei brucei. An option for developing vaccines and chemotherapeutic agents against trypanosomosis is to target pathogenic factors released by the parasite during infection, namely an "anti-disease" approach. One such pathogenic factor is oligopeptidase B (TbOPB), a trypanosome peptidase that hydrolyses Arg/Lys containing peptides smaller than 30 amino acid residues and is suspected to be involved in the hormonal deregulation associated with the disease. To better understand the role TbOPB plays in parasite physiology and host pathogenesis, oligopeptidase B null mutant parasites (Δopb) were generated in the T. b. brucei Lister 427 strain. Δopb Trypanosoma brucei parasites grew at a significantly faster rate in vitro, and were as virulent as wild type strains during infection in mice. Immunohistopatholgy of infected mouse testes revealed Δopb parasites in extra vascular regions showing that TbOPB is not involved in assisting T. brucei parasites to cross microvascular endothelial cells. Gelatine gel analysis of Δopb null mutants showed an increase in discrete cysteine peptidase activities when compared to wild type strains. Enzymatic activity assays were carried out to identify how closely related oligopeptidases are affected by TbOPB gene deletion. A significant increase of T. brucei prolyl oligopeptidase (TbPOP) activity was observed, but no concomitant increase in TbPOP protein levels, suggesting that a POP-like enzyme might compensate for a loss in OPB activity in Δopb null mutants.<br /> (© 2011 Elsevier B.V. All rights reserved.)
- Subjects :
- Animals
Capillary Permeability
Disease Models, Animal
Enzyme Activation
Female
Gene Deletion
Genes, Protozoan
Immunohistochemistry
Male
Mice
Mice, Inbred BALB C
Prolyl Oligopeptidases
Protozoan Proteins genetics
Serine Endopeptidases genetics
Testis parasitology
Testis pathology
Trypanosoma brucei brucei genetics
Trypanosoma brucei brucei pathogenicity
Trypanosomiasis, African parasitology
Virulence
Protozoan Proteins metabolism
Serine Endopeptidases metabolism
Trypanosoma brucei brucei enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1872-9428
- Volume :
- 182
- Issue :
- 1-2
- Database :
- MEDLINE
- Journal :
- Molecular and biochemical parasitology
- Publication Type :
- Academic Journal
- Accession number :
- 22123425
- Full Text :
- https://doi.org/10.1016/j.molbiopara.2011.11.007