scholarly journals Cysteine Peptidase B Regulates Leishmania mexicana Virulence through the Modulation of GP63 Expression

2016 ◽  
Vol 12 (5) ◽  
pp. e1005658 ◽  
Author(s):  
Pierre-André Casgrain ◽  
Caroline Martel ◽  
W. Robert McMaster ◽  
Jeremy C. Mottram ◽  
Martin Olivier ◽  
...  
Keyword(s):  
Leishmania Mexicana ◽  
Cysteine Peptidase

scholarly journals Inhibitor of Cysteine Peptidase Does Not Influence the Development of Leishmania mexicana in Lutzomyia longipalpis

2009 ◽  
Vol 46 (3) ◽  
pp. 605-609 ◽  
Author(s):  
Lucie Jecna ◽  
Anna Svarovska ◽  
Sebastien Besteiro ◽  
Jeremy C. Mottram ◽  
Graham H. Coombs ◽  
...  
Keyword(s):  
Lutzomyia Longipalpis ◽  
Leishmania Mexicana ◽  
Cysteine Peptidase

scholarly journals Chemical Shift Assignments of Leishmania mexicana ICP, a Novel Cysteine Peptidase Inhibitor

2006 ◽  
Vol 36 (S1) ◽  
pp. 7-7
Author(s):  
Brian O. Smith ◽  
Gareth D. Westrop ◽  
Jeremy C. Mottram ◽  
Graham H. Coombs
Keyword(s):  
Chemical Shift ◽  
Chemical Shift Assignments ◽  
Leishmania Mexicana ◽  
Cysteine Peptidase ◽  
Peptidase Inhibitor

Cysteine peptidases in Herpetomonas samuelpessoai are modulated by temperature and dimethylsulfoxide-triggered differentiation

Parasitology ◽  
2009 ◽  
Vol 136 (1) ◽  
pp. 45-54 ◽  
Author(s):  
F. M. Pereira ◽  
C. G. R. Elias ◽  
C. M. d'Avila-Levy ◽  
M. H. Branquinha ◽  
A. L. S. Santos
Keyword(s):  
Flow Cytometry ◽  
Drosophila Melanogaster ◽  
Fluorescence Microscopy ◽  
Trypanosoma Cruzi ◽  
Environmental Changes ◽  
Parasite Growth ◽  
Differentiation Process ◽  
Leishmania Mexicana ◽  
Cysteine Peptidase ◽  
Cysteine Peptidases

SUMMARYCysteine peptidases of protozoa have been implicated in a variety of biological events, and the expression of these enzymes is modulated in response to distinct stimuli, including environmental changes and differentiation. In the present work, we have examined the expression of cysteine peptidases from Herpetomonas samuelpessoai grown at distinct temperatures and during dimethylsulfoxide (DMSO)-elicited differentiation. We demonstrated that a 45 kDa cysteine peptidase had its activity reduced during the parasite growth at 37°C in comparison to 26°C, and when cultured up to 72 h in the presence of DMSO. The modulation in the 45 kDa cysteine peptidase expression is connected to the differentiation process, since both temperature and DMSO are able to trigger the promastigote to paramastigote transformation in H. samuelpessoai. The possible immunological similarity of H. samuelpessoai proteins with well-known cysteine peptidases produced by trypanosomatid pathogens, including cruzipain (Trypanosoma cruzi) and cysteine peptidase b (cpb) from Leishmania mexicana, was also investigated, as well as with calpain molecules. The protein cellular lysate of H. samuelpessoai reacted with antibodies raised against cpb of L. mexicana and calpain of Drosophila melanogaster; however, no reaction was observed against cruzipain. The 35 kDa cpb-like protein had its expression diminished in DMSO-treated parasites, while the 80 kDa calpain-like molecule was enhanced and an additional 30 kDa calpain-related polypeptide was exclusively observed in these cells. Fluorescence microscopy and flow cytometry analyses corroborated these data. The results described above add H. samuelpessoai to the list of parasites whose differentiation seems to be correlated with cysteine peptidase expression.

Cysteine Peptidase Inhibitors in Trypanosomatid Parasites

2013 ◽  
Vol 20 (25) ◽  
pp. 3152-3173 ◽  
Author(s):  
A. Lima ◽  
F. Reis ◽  
T. Costa
Keyword(s):  
Peptidase Inhibitors ◽  
Cysteine Peptidase ◽  
Trypanosomatid Parasites

Design of Inhibitors for Glyceraldehyde-3-phosphate Dehydrogenase (GAPDH) Enzyme of Leishmania mexicana

2020 ◽  
Vol 16 (6) ◽  
pp. 784-795
Author(s):  
Krisnna M.A. Alves ◽  
Fábio José Bonfim Cardoso ◽  
Kathia M. Honorio ◽  
Fábio A. de Molfetta
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Binding Site ◽  
Point Of View ◽  
New Drugs ◽  
Leishmania Mexicana ◽  
Receptor Complexes ◽  
Starting Point ◽  
Dynamics Simulations ◽  
Selection Of

Background:: Leishmaniosis is a neglected tropical disease and glyceraldehyde 3- phosphate dehydrogenase (GAPDH) is a key enzyme in the design of new drugs to fight this disease. Objective:: The present study aimed to evaluate potential inhibitors of GAPDH enzyme found in Leishmania mexicana (L. mexicana). Methods: A search for novel antileishmanial molecules was carried out based on similarities from the pharmacophoric point of view related to the binding site of the crystallographic enzyme using the ZINCPharmer server. The molecules selected in this screening were subjected to molecular docking and molecular dynamics simulations. Results:: Consensual analysis of the docking energy values was performed, resulting in the selection of ten compounds. These ligand-receptor complexes were visually inspected in order to analyze the main interactions and subjected to toxicophoric evaluation, culminating in the selection of three compounds, which were subsequently submitted to molecular dynamics simulations. The docking results showed that the selected compounds interacted with GAPDH from L. mexicana, especially by hydrogen bonds with Cys166, Arg249, His194, Thr167, and Thr226. From the results obtained from molecular dynamics, it was observed that one of the loop regions, corresponding to the residues 195-222, can be related to the fitting of the substrate at the binding site, assisting in the positioning and the molecular recognition via residues responsible for the catalytic activity. Conclusion:: he use of molecular modeling techniques enabled the identification of promising compounds as inhibitors of the GAPDH enzyme from L. mexicana, and the results obtained here can serve as a starting point to design new and more effective compounds than those currently available.

scholarly journals Inhibition of glycosylphosphatidylinositol biosynthesis in Leishmania mexicana by mannosamine

1993 ◽  
Vol 268 (13) ◽  
pp. 9570-9577
Author(s):  
M.C. Field ◽  
E. Medina-Acosta ◽  
G.A. Cross
Keyword(s):  
Leishmania Mexicana
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