Novel approaches for the identification of inhibitors of leishmanial dipeptidylcarboxypeptidase

Bibliography

• Alvar J, Croft S, Olliaro P. Chemotherapy in the treatment and control of leishmaniasis. Adv Parasitol 2006;61:223-74
   PubMed Web of Science ®Google Scholar
• Murray HW, Berman JD, Davies CR, et al. Advances in leishmaniasis. Lancet 2005;366:1561-77
   PubMed Web of Science ®Google Scholar
• Available from: http:/www.who.int/leishmaniasis/burden/en
   Google Scholar
• Murray HW. Leishmaniasis in the United States: treatment in 2012. Am J Trop Med Hyg 2012;86(3):434-40
   PubMed Web of Science ®Google Scholar
• Available from: http://www.who.int/vaccine_research/diseases/soa_parasitic/en/index3.html
   Google Scholar
• Kedzierski L, Sakthianandeswaren A, Curtis JM, et al. Leishmaniasis: current treatment and prospects for new drugs and vaccines. Curr Med Chem 2009;16:599-614
   PubMed Web of Science ®Google Scholar
• Berman J. Clinical status of agents being developed for leishmaniasis. Expert Opin Investig Drugs 2005;14:1337-46
   PubMed Web of Science ®Google Scholar
• Sundar S. Drug resistance in Indian visceral leishmaniasis. Trop Med Int Health 2001;6:849-54
   PubMed Web of Science ®Google Scholar
• Hadighi R, Mohebali M, Boucher P, et al. Unresponsiveness to glucantime treatment in Iranian cutaneous leishmaniasis due to drug-resistant Leishmania tropica parasites. PLoS Med 2006;3(5):e162
   PubMed Web of Science ®Google Scholar
• Rojas R, Valderrama L, Valderrama M, et al. Resistance to antimony and treatment failure in human Leishmania (Viannia) infection. J Infect Dis 2006;193:1375-83
   PubMed Web of Science ®Google Scholar
• Yardley V, Ortuno N, Llanos-Cuentas A, et al. American tegumentary leishmaniasis: is antimonial treatment outcome related to parasite drug susceptibility? J Infect Dis 2006;194:1168-75
   PubMed Web of Science ®Google Scholar
• Sundar S, Gupta LB, Makharia MK, et al. Oral treatment of visceral leishmaniasis with miltefosine. Ann Trop Med Parasitol 1999;93:589-97
   PubMed Web of Science ®Google Scholar
• Sundar S, Murray HW. Availability of miltefosine for the treatment of kala-azar in India. Bull World Health Organ 2005;83:394-5
   PubMed Web of Science ®Google Scholar
• Sundar S, Chakravarty J. Recent advances in the diagnosis and treatment of kala-azar. Natl Med J India 2012;25(2):85-9
   PubMed Web of Science ®Google Scholar
• Molyneux DH, Killick-Kendrick R. Morphology, ultrastructure and life cycles. In: Peters W, Killick-Kendrick R, editors. The Leishmaniases in biology and medicine. Volume 1. Academic Press, London; 1987. p. 121-76
   Google Scholar
• Alexander J, Russel DG. The interaction of Leishamania species with macrophages. Adv Parasitol 1992;32:175-254
   Google Scholar
• Garlapati S, Dahan E, Shapira M. Effect of acidic pH on heat shock gene expression in Leishmania. Mol Biochem Parasitol 1999;100:95-101
   PubMed Web of Science ®Google Scholar
• Degrossoli A, Colhone MC, Arrais-Silva WW, et al. Hypoxia modulates expression of the 70-kD heat shock protein and reduces Leishmania infection in macrophages. J Biomed Sci 2004;11:847-54
   PubMed Web of Science ®Google Scholar
• Barak E, Amin-Spector S, Gerliak E, et al. Differentiation of Leishmania donovani in host free system: analysis of signal perception and response. Mol Biochem Parasitol 2005;141:99-108
   PubMed Web of Science ®Google Scholar
• Li Q, Zhao Y, Ni B, et al. Comparison of the expression profiles of promastigotes and axenic amastigotes in Leishmania donovani using serial analysis of gene expression. Parasitol Res 2008;103(4):821-8
   PubMed Web of Science ®Google Scholar
• Saxena A, Lahav T, Holland N, et al. Analysis of the Leishmania donovani transcriptome reveals an ordered progression of transient and permanent changes in gene expression during differentiation. Mol Biochem Parasitol 2008;152(1):53-65
   Web of Science ®Google Scholar
• Ivens AC, Peacock CS, Worthey EA, et al. The genome of the kinetoplastid parasite, Leishmania major. Science 2005;309:436-42
   PubMed Web of Science ®Google Scholar
• McNicoll F, Drummelsmith J, Müller M, et al. A combined proteomic and transcriptomic approach to the study of stage differentiation in Leishmania infantum. Proteomics 2006;6(12):3567-81
   PubMed Web of Science ®Google Scholar
• Leifso K, Cohen-Freue G, Dogra N, et al. Genomic and proteomic expression analysis of Leishmania promastigote and amastigote life stages: the Leishmania genome is constitutively expressed. Mol Biochem Parasitol 2007;152(1):35-46
   PubMed Web of Science ®Google Scholar
• Depledge DP, Evans KJ, Ivens AC, et al. Comparative expression profiling of Leishmania: modulation in gene expression between species and in different host genetic backgrounds. PLoS Negl Trop Dis 2009;3(7):e476
   PubMedGoogle Scholar
• Myler PJ. Searching the Tritryp genomes for drug targets. Adv Exp Med Biol 2008;625:133-40
   PubMed Web of Science ®Google Scholar
• Caffrey CR, Lima AP, Steverding D. Cysteine peptidases of kinetoplastid parasites. Adv Exp Med Biol 2011;712:84-99
   PubMed Web of Science ®Google Scholar
• Silva-Almeida M, Pereira BA, Ribeiro-Guimarães ML, et al. Proteinases as virulence factors in Leishmania spp. infection in mammals. Parasit Vectors 2012;7(5):160
   Google Scholar
• Castanys-Muñoz E, Brown E, Coombs GH, et al. Leishmania mexicana metacaspase is a negative regulator of amastigote proliferation in mammalian cells. Cell Death Dis 2012;3:e385
   PubMed Web of Science ®Google Scholar
• Toledo JS, Ferreira TR, Defina TP, et al. Cell homeostasis in a Leishmania major mutant over-expressing the spliced leader RNA is maintained by an increased proteolytic activity. Int J Biochem Cell Biol 2010;42(10):1661-71
   PubMed Web of Science ®Google Scholar
• Rawlings ND, Tolle DP, Barrett AJ. MEROPS: the peptidase database. Nucleic Acids Res 2004;32:D160-4; Database issue
   PubMed Web of Science ®Google Scholar
• Rosenthal FJ. Proteases of protozoan parasites. Adv Parasitol 1999;43:105-59
   PubMed Web of Science ®Google Scholar
• Besteiro S, Williams RAM, Coombs GH, et al. Protein turnover and differentiation in Leishmania. Int J Parasitol 2007;37:1063-75
   PubMed Web of Science ®Google Scholar
• Mottram JC, Coombs GH, Alexander J. Cysteine peptidase as virulence factors of Leishmania. Curr Opin Microbiol 2004;7:375-81
   PubMed Web of Science ®Google Scholar
• Bouvier J, Schneider P, Etges R. Leishmanolysin: surface metalloproteinase of Leishmania. Methods Enzymol 1995;248:614-33
   PubMed Web of Science ®Google Scholar
• Andrade Ribeirode AS, Santero MM, de Melo MN, et al. Leishmania (Leishmania) amazonensis: purification and enzymatic characterization of soluble serine oligopeptidase. Exp Parasitol 1998;89:153-60
   PubMed Web of Science ®Google Scholar
• Brooks DR, Denise H, Westrop GD, et al. The stage regulated expression of Leishmania mexicana CPB cysteine proteases is mediated by an intercistronic sequence element. J Biol Chem 2001;276(50):47061-9
   PubMed Web of Science ®Google Scholar
• Williams RAM, Tetley L, Mottram JC, et al. Cysteine peptidases CPA and CPB are vital for autophagy and differentiation in Leishmania mexicana. Mol Microbiol 2006;61:655-74
   PubMed Web of Science ®Google Scholar
• Morty RE, Morehead J. Cloning and characterization of leucylaminopeptidase from three pathogenic Leishmania species. J Biol Chem 2002;277:26057-65
   PubMed Web of Science ®Google Scholar
• Judice WAS, Puzer L, Cortin SS, et al. Carboxy dipeptidase activities of recombinant cysteine peptidase cruzain of Trypanosoma cruzi and CPB of Leishmania mexicana. Eur J Biochem 2004;271:1046-53
   PubMedGoogle Scholar
• Alvarez VE, Niemirowicz GT, Cazzulo JJ. The peptidases of Trypanosoma cruzi: digestive enzymes, virulence factors, and mediators of autophagy and programmed cell death. Biochim Biophys Acta 2012;1824(1):195-206
   PubMed Web of Science ®Google Scholar
• Goyal N, Duncan R, Selvapandiyan A, et al. Cloning and characterization of angiotensin converting enzyme related peptidylcarboxypeptidase from Leishmania donovani. Mol Biochem Parasitol 2006;145:147
   PubMed Web of Science ®Google Scholar
• Yaron A, Mlynar D, Berger A. A dipeptidylcarboxypeptidase from Escherichia coli. Biochem Biophys Res Commun 1972;47:897-902
   PubMed Web of Science ®Google Scholar
• Henrich B, Becker S, Schroeder U, et al. dcp Gene of Escherichia coli: cloning, sequencing, transcript mapping and characterization of the gene product. J Bacteriol 1993;175:7290-300
   PubMed Web of Science ®Google Scholar
• Barrett AJ. Bioinformatics of proteases in the MEROPS database. Curr Opin Drug Discov Devel 2004;7:334-41
   PubMed Web of Science ®Google Scholar
• Chu TG, Orlowski M. Active site directed N-carboxymethyl peptide inhibitors of a soluble metalloendopeptidase from rat brain. Biochemistry 1984;23:3598-603
   PubMed Web of Science ®Google Scholar
• Soffer RL. Angiotensin converting enzyme and the regulation of vasoactive peptides. Annu Rev Biochem 1976;45:73-94
   PubMed Web of Science ®Google Scholar
• Skeggs LT, Kahn JR, Shumway NP. The purification of hypertension II. J Exp Med 1956;103:301-7
   PubMed Web of Science ®Google Scholar
• Yang HYT, Erdos EG, Levin Y. A dipeptidyl carboxypeptidase that converts angiotensin I and inactivates bradykinin. Biochim Biophys Acta 1970;214:374-6
   PubMed Web of Science ®Google Scholar
• Wei L, Alhenc-Gelas F, Soubrier F. Expression and characterization of recombinant human angiotensin I-converting enzyme. Evidence for a C-terminal transmembrane anchor and for a proteolytic processing of the secreted recombinant and plasma enzymes. J Biol Chem 1991;266:5540-6
   PubMed Web of Science ®Google Scholar
• Ehlers MRW, Fox EA, Strydom DJ, Riordan JF. Molecular cloning of human testicular angiotensinconverting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme. Proc Natl Acad Sci USA 1989;86:7741-5
   PubMed Web of Science ®Google Scholar
• Kumar RS, Kusari J, Roy SN, et al. Structure of testicular angiotensin-converting enzyme. A segmental mosaic isozyme. J Biol Chem 1989;264:16754-8
   PubMed Web of Science ®Google Scholar
• Lattion AL, Soubrier F, Allegrini J, et al. The testicular transcript of the angiotensin I-converting enzyme encodes for the ancestral, nonduplicated form of the enzyme. FEBS Lett 1989;252:99-104
   PubMed Web of Science ®Google Scholar
• Natesh R, Schwager SL, Sturrock ED, et al. Crystal structure of the human angiotensin-converting enzyme-lisinopril complex. Nature 2003;421:551-4
   PubMed Web of Science ®Google Scholar
• DeLong EF, Pace NR. Environmental diversity of bacteria and archaea. Syst Biol 2001;50:470-8
   PubMed Web of Science ®Google Scholar
• Rivière G, Michaud A, Corradi HR, et al. Characterization of the first angiotensin-converting like enzyme in bacteria: ancestor ACE is already active. Gene 2007;399:81-90
   PubMed Web of Science ®Google Scholar
• Hamilton S, Miller CG. Cloning and nucleotide sequence of Salmonella typhimurium dcp gene encoding dipeptidyl carboxypaptidase. J Bacteriol 1992;174:1626-30
   PubMed Web of Science ®Google Scholar
• Kawamura T, Kikuno K, Oda T, et al. Some molecular and inhibitory specifications of a dipeptidyl carboxypeptidase from the polychaete Neanthes virens resembling angiotensin I converting enzyme. Biosci Biotechnol Biochem 2000;64(10):2193-200
   PubMed Web of Science ®Google Scholar
• Ogasawara W, Abe N, Hagio T, et al. Purification and characterization of a dipeptidyl carboxypeptidase from Pseudomonas sp. WO24. Biosci Biotechnol Biochem 1997;61(5):858-63
   PubMed Web of Science ®Google Scholar
• Miyoshi S, Nomura G, Suzuki M. Purification and characterization of a novel dipeptidyl carboxypeptidasefrom a Streptomyces species. J Biochem 1992;112(2):253-7
   PubMed Web of Science ®Google Scholar
• Rivière G, Michaud A, Deloffre L, et al. Characterization of the first non-insect invertebrate functional angiotensin-converting enzyme (ACE): leech TtACE resembles the N-domain of mammalian ACE. Biochem J 2004;382(Pt 2):565-73
   PubMedGoogle Scholar
• Akif M, Masuyer G, Schwager SL, et al. Structural characterization of angiotensin I-converting enzyme in complex with a selenium analogue of captopril. FEBS J 2011;278(19):3644-50
   PubMed Web of Science ®Google Scholar
• Rainey PM, Spithill TW, McMahon-Pratt D, Pan AA. Biochemical and molecular characterization of L. pifanoi amastigotes in continous axenic culture. Mol Biochem Parasitol 1991;49:111-18
   PubMed Web of Science ®Google Scholar
• Yaron A. Dipeptidyl carboxypeptidase from Escherichia coli. Methods Enzymol 1976;50:599-610
   Google Scholar
• Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun 1967;27:157-62
   PubMed Web of Science ®Google Scholar
• Araujo MC, Melo RL, Cesari MH, et al. Peptidase specificity characterization of C- and N-terminal catalytic sites of angiotensin I converting enzyme. Biochemistry 2000;39:8519-25
   PubMed Web of Science ®Google Scholar
• Bersanetti PA, Andrade MC, Casarini DE, et al. Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides for defining substrate specificity of the angiotensin I-converting enzyme and development of selective C-domain substrates. Biochemistry 2004;50:21-43
   Google Scholar
• Baig MS, Kumar A, Siddiqi MI, Goyal N. Characterization of dipeptidylcarboxypeptidase of Leishmania donovani: a molecular model for structure based design of antileishmanials. J Comput Aided Mol Des 2011;24:77-87
   Web of Science ®Google Scholar
• Lanzillo JJ, Dasarathy Y, Stevens J, et al. Human testicular angiotensin-converting enzyme is a mixture of two molecular weight forms, only one is similar to the seminal plasma enzyme. Biochem Biophys Res Commun 1985;128:457-62
   PubMed Web of Science ®Google Scholar
• Deddish PA, Wang LX, Jackman HL, et al. Single-domain angiotensin I converting enzyme (kininase II): characterization and properties. J Pharmacol Exp Ther 1996;279:1582
   PubMed Web of Science ®Google Scholar
• Deutch CE, Soffer RL. Escherichia coli mutant defective in dipeptidyl carboxypeptidase. Proc Natl Acad Sci USA 1978;75:5998-6001
   PubMed Web of Science ®Google Scholar
• Junot C, Gonzales MF, Ezan E, et al. RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatorypeptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis. J Pharmacol Exp Ther 2001;297:606-11
   PubMed Web of Science ®Google Scholar
• Nchinda AT, Chibale K, Redelinghuys P, et al. Synthesis of novel keto-ACE analogues as domainselective angiotensin-I converting enzyme inhibitors. Bioorg Med Chem Lett 2006;16:4612-15
   PubMed Web of Science ®Google Scholar
• Watermeyer JM, Kröger WL, O'Neill HG, et al. Probing the basis of domain-dependent inhibition using novel ketone inhibitors of angiotensinconverting enzyme. Biochemistry 2008;47:5942-50
   PubMed Web of Science ®Google Scholar
• Nchinda AT, Chibale K, Redelinghuys P, et al. Synthesis and molecular modeling of a lisinopriltryptophan analogue inhibitor of angiotensin I-converting enzyme. Bioorg Med Chem Lett 2006;16:4616-19
   PubMed Web of Science ®Google Scholar
• Turner AJ, Hooper NM. The angiotensin converting enzyme gene family: genomics and pharmacology. Trends Pharmacol Sci 2002;23:177-83
   PubMed Web of Science ®Google Scholar
• Baig MS, Gangwar S, Goyal N. Biochemical characterization of dipeptidylcarboxypeptidase of Leishmania donovani. Cell Mol Biol 2011;57(1):56-61
   PubMed Web of Science ®Google Scholar
• Comellas-Bigler M, Lang R, Bode W, Maskos K. Crystal structure of E. coli dipeptidylcarboxypeptidaseDCP:future indication of a ligand dependent hinge movement mechanism. J Mol Biol 2005;349:99
   PubMed Web of Science ®Google Scholar
• Donoghue M, Hsieh F, Baronas E, et al. A novel angiotensin-converting enzymerelated carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1–9. Circ Res 2000;87:E1-9
   Google Scholar
• Tipnis SR, Hooper NM, Hyde R. A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril- insensitive carboxypeptidase. J Biol Chem 2000;275:33238-43
   PubMed Web of Science ®Google Scholar
• Anthony CS, Masuyer G, Sturrock ED, et al. Structure based drug design of angiotensin-I converting enzyme inhibitors. Curr Med Chem 2012;19:845-55
   PubMed Web of Science ®Google Scholar
• Gangwar S, Baig MS, Shah P, et al. Identification of novel inhibitors of dipeptidylcarboxypeptidase of Leishmania donovani via ligand-based virtual screening and biological evaluation. Chem Biol Drug Des 2012;79:149-56
   PubMed Web of Science ®Google Scholar