Cloning, overexpression and characterization of Leishmania donovani triosephosphate isomerase

Experimental Parasitology

Volumn 130, Issue 4, 2012, Pages 430-436

  Kumar, Kishore ^a   Bhargava, Prachi ^a   Roy, Uma ^a  

^a CENTRAL DRUG RESEARCH INSTITUTE   (India)

Author keywords

Biochemical characterization; Leishmania donovani; Triosephosphate isomerase

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE; RECOMBINANT ENZYME; THIOMESYLIC ACID METHYL ESTER; TRIOSEPHOSPHATE ISOMERASE;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME PURIFICATION; ENZYME STABILITY; LEISHMANIA DONOVANI; MICHAELIS MENTEN KINETICS; MOLECULAR CLONING; MOLECULAR PROBE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN EXPRESSION; SEQUENCE ANALYSIS; TEMPERATURE; THERMOSTABILITY;

AMINO ACID SEQUENCE; BLOTTING, WESTERN; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME INHIBITORS; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROGEN-ION CONCENTRATION; LEISHMANIA DONOVANI; METHYL METHANESULFONATE; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; SEQUENCE ALIGNMENT; TRIOSE-PHOSPHATE ISOMERASE;

LEISHMANIA DONOVANI;

EID: 84859109633     PISSN: 00144894     EISSN: 10902449     Source Type: Journal    
DOI: 10.1016/j.exppara.2012.01.016     Document Type: Article

References (33)

1. Alvar J., Aparicio P., Aseffa A., Den Boer M., Canavate C., Dedet J.P., Gradoni L., Ter Horst R., Lopez-Velez R., Moreno J. The relationship between leishmaniasis and AIDS: the second 10 years. Clin. Microbiol. Rev. 2008, 21(2):334-359.
2. Bhargava P., Kumar K., Chaudhaery S.S., Saxena A.K., Roy U. Cloning, overexpression and characterization of Leishmania donovani squalene synthase. FEMS Microbiol. Lett. 2010, 311(1):82-92.
3. Borchert T.V., Pratt K., Zeelen J.P., Callens M., Noble M.E., Opperdoes F.R., Michels P.A., Wierenga R.K. Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. Eur. J. Biochem. 1993, 211(3):703-710.
4. den Boer M.L., Alvar J., Davidson R.N., Ritmeijer K., Balasegaram M. Developments in the treatment of visceral leishmaniasis. Expert. Opin. Emerg. Drugs 2009, 14(3):395-410.
5. Enriquez-Flores S., Rodriguez-Romero A., Hernandez-Alcantara G., De la Mora I., Gutierrez-Castrellon P., Carvajal K., Lopez-Velazquez G., Reyes-Vivas H. Species-specific inhibition of Giardia lamblia triosephosphate isomerase by localized perturbation of the homodimer. Mol. Biochem. Parasitol. 2008, 157(2):179-186.
6. Faraut-Gambarelli F., Piarroux R., Deniau M., Giusiano B., Marty P., Michel G., Faugere B., Dumon H. In vitro and in vivo resistance of Leishmania infantum to meglumine antimoniate: a study of 37 strains collected from patients with visceral leishmaniasis. Antimicrob. Agents Chemother. 1997, 41(4):827-830.
7. Garza-Ramos G., Cabrera N., Saavedra-Lira E., Tuena de Gomez-Puyou M., Ostoa-Saloma P., Perez-Montfort R., Gomez-Puyou A. Sulfhydryl reagent susceptibility in proteins with high sequence similarity-triosephosphate isomerase from Trypanosoma brucei, Trypanosoma cruzi and Leishmania mexicana. Eur. J. Biochem. 1998, 253(3):684-691.
8. Garza-Ramos G., Perez-Montfort R., Rojo-Dominguez A., de Gomez-Puyou M.T., Gomez-Puyou A. Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase. Eur. J. Biochem. 1996, 241(1):114-120.
9. Gomez-Puyou A., Saavedra-Lira E., Becker I., Zubillaga R.A., Rojo-Dominguez A., Perez-Montfort R. Using evolutionary changes to achieve species-specific inhibition of enzyme action - studies with triosephosphate isomerase. Chem. Biol. 1995, 2(12):847-855.
10. Gracy R.W. Triosephosphate isomerase from human erythrocytes. Methods Enzymol. 1975, 41:442-447.
11. Grogl M., Thomason T.N., Franke E.D. Drug resistance in leishmaniasis: its implication in systemic chemotherapy of cutaneous and mucocutaneous disease. Am. J. Trop. Med. Hyg. 1992, 47(1):117-126.
12. Helfert S., Estevez A.M., Bakker B., Michels P., Clayton C. Roles of triosephosphate isomerase and aerobic metabolism in Trypanosoma brucei. Biochem J. 2001, 357(Pt 1):117-125.
13. Jimenez L., Vibanco-Perez N., Navarro L., Landa A. Cloning, expression and characterisation of a recombinant triosephosphate isomerase from Taenia solium. Int. J. Parasitol. 2000, 30(9):1007-1012.
14. Kohl L., Callens M., Wierenga R.K., Opperdoes F.R., Michels P.A. Triose-phosphate isomerase of Leishmania mexicana mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein. Eur. J. Biochem. 1994, 220(2):331-338.
15. Kumar K., Bhargava P., Roy U. In vitro refolding of triosephosphate isomerase from L. donovani. Appl. Biochem. Biotechnol. 2011, 164(7):1207-1214.
16. Landa A., Rojo-Dominguez A., Jimenez L., Fernandez-Velasco D.A. Sequencing, expression and properties of triosephosphate isomerase from Entamoeba histolytica. Eur. J. Biochem. 1997, 247(1):348-355.
17. Lira R., Sundar S., Makharia A., Kenney R., Gam A., Saraiva E., Sacks D. Evidence that the high incidence of treatment failures in Indian kala-azar is due to the emergence of antimony-resistant strains of Leishmania donovani. J. Infect. Dis. 1999, 180(2):564-567.
18. Maithal K., Ravindra G., Balaram H., Balaram P. Inhibition of plasmodium falciparum triose-phosphate isomerase by chemical modification of an interface cysteine. Electrospray ionization mass spectrometric analysis of differential cysteine reactivities. J. Biol. Chem. 2002, 277(28):25106-25114.
19. Maldonado E., Soriano-Garcia M., Moreno A., Cabrera N., Garza-Ramos G., de Gomez-Puyou M., Gomez-Puyou A., Perez-Montfort R. Differences in the intersubunit contacts in triosephosphate isomerase from two closely related pathogenic trypanosomes. J. Mol. Biol. 1998, 283(1):193-203.
20. Mande S.C., Mainfroid V., Kalk K.H., Goraj K., Martial J.A., Hol W.G. Crystal structure of recombinant human triosephosphate isomerase at 2.8å resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 1994, 3(5):810-821.
21. Mathur D., Malik G., Garg L.C. Biochemical and functional characterization of triosephosphate isomerase from Mycobacterium tuberculosis H37Rv. FEMS Microbiol. Lett. 2006, 263(2):229-235.
22. Michels P.A. Compartmentation of glycolysis in trypanosomes: a potential target for new trypanocidal drugs. Biol Cell 1988, 64(2):157-164.
23. Moyersoen J., Choe J., Fan E., Hol W.G., Michels P.A. Biogenesis of peroxisomes and glycosomes: trypanosomatid glycosome assembly is a promising new drug target. FEMS Microbiol. Rev. 2004, 28(5):603-643.
24. Murray H.W. Treatment of visceral leishmaniasis (kala-azar): a decade of progress and future approaches. Int. J. Infect. Dis. 2000, 4(3):158-177.
25. Olivares-Illana V., Rodriguez-Romero A., Becker I., Berzunza M., Garcia J., Perez-Montfort R., Cabrera N., Lopez-Calahorra F., de Gomez-Puyou M.T., Gomez-Puyou A. Perturbation of the dimer interface of triosephosphate isomerase and its effect on Trypanosoma cruzi. PLoS Negl. Trop. Dis. 2007, 1(1):e1.
26. Ostoa-Saloma P., Garza-Ramos G., Ramirez J., Becker I., Berzunza M., Landa A., Gomez-Puyou A., Tuena de Gomez-Puyou M., Perez-Montfort R. Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi. Eur. J. Biochem. 1997, 244(3):700-705.
27. Perez-Pertejo Y., Reguera R.M., Villa H., Garcia-Estrada C., Balana-Fouce R., Pajares M.A., Ordonez D. Leishmania donovani methionine adenosyltransferase. Role of cysteine residues in the recombinant enzyme. Eur. J. Biochem. 2003, 270(1):28-35.
28. Repiso A., Boren J., Ortega F., Pujades A., Centelles J., Vives-Corrons J.L., Climent F., Cascante M., Carreras J. Triosephosphate isomerase deficiency. Genetic, enzymatic and metabolic characterization of a new case from Spain. Haematologica 2002, 87(4):ECR12.
29. Sundar S., More D.K., Singh M.K., Singh V.P., Sharma S., Makharia A., Kumar P.C., Murray H.W. Failure of pentavalent antimony in visceral leishmaniasis in India: report from the center of the Indian epidemic. Clin. Infect. Dis. 2000, 31(4):1104-1107.
30. Tao H., Liu W., Simmons B.N., Harris H.K., Cox T.C., Massiah M.A. Purifying natively folded proteins from inclusion bodies using sarkosyl, Triton X-100, and CHAPS. Biotechniques 2010, 48(1):61-64.
31. Villa H., Perez-Pertejo Y., Garcia-Estrada C., Reguera R.M., Requena J.M., Tekwani B.L., Balana-Fouce R., Ordonez D. Molecular and functional characterization of adenylate kinase 2 gene from Leishmania donovani. Eur. J. Biochem. 2003, 270(21):4339-4347.
32. Wierenga R.K., Noble M.E., Vriend G., Nauche S., Hol W.G. Refined 1.83å structure of trypanosomal triosephosphate isomerase crystallized in the presence of 2.4M-ammonium sulphate. A comparison with the structure of the trypanosomal triosephosphate isomerase-glycerol-3-phosphate complex. J. Mol. Biol. 1991, 220(4):995-1015.
33. Williams J.C., Zeelen J.P., Neubauer G., Vriend G., Backmann J., Michels P.A., Lambeir A.M., Wierenga R.K. Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Eng. 1999, 12(3):243-250.