Identification of lead compounds targeting the cathepsin B-like enzyme of Eimeria tenella

Antimicrobial Agents and Chemotherapy

Volumn 56, Issue 3, 2012, Pages 1190-1201

  Schaeffer, Marie ^a,d   Schroeder, Joerg ^b   Heckeroth, Anja R ^b   Noack, Sandra ^b   Gassel, Michael ^b   Mottram, Jeremy C ^a   Selzer, Paul M ^a,b   Coombs, Graham H ^a,c  

^a UNIVERSITY OF GLASGOW   (United Kingdom)

^b Intervet Innovation GmbH   (Germany)

^c UNIVERSITY OF STRATHCLYDE   (United Kingdom)

^d INSTITUT DE GÉNOMIQUE FONCTIONNELLE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

2 [(3 CHLORO 5 METHYL 1 PHENYL 1H PYRAZOL 4 YL)METHYLENE]HYDRAZONECARBOTHIOAMIDE; 4 [(3 CYANOPHENYL)AMINO] 6 (1 PIPERIDINYL) 1,3,4 TRIAZINE 2 CARBONITRILE; 4 [(4 METHOXYPHENYL)METHYLENE] 2 (4 PRPYLCYCLOHEXYL) 4(4H) OXAZOLONE; CP 673854; CP 725576; CP 989759; EIMERIA TENELLA CATHEPSIN B LIKE PROTEIN; GLYCOSYLATED PROTEIN; LEAD; NITRILE; OXAZOLONE; PROTEINASE INHIBITOR; PROTOZOAL PROTEIN; RECOMBINANT ENZYME; THIOSEMICARBAZONE; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; DEGLYCOSYLATION; EIMERIA TENELLA; ENZYME INHIBITION; ESCHERICHIA COLI; IC 50; IN VITRO STUDY; MOLECULAR DOCKING; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; ANIMALS; CATHEPSIN B; CHICKENS; CLONING, MOLECULAR; COCCIDIOSTATS; CYSTEINE PROTEINASE INHIBITORS; EIMERIA TENELLA; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NITRILES; OXAZOLONE; PICHIA; PROTOZOAN PROTEINS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT; SEQUENCE ANALYSIS, DNA; SMALL MOLECULE LIBRARIES; SUBSTRATE SPECIFICITY; THIOSEMICARBAZONES;

EID: 84857173873     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.05528-11     Document Type: Article

References (46)

1. Alves LC, et al. 2001. Analysis of the S(2) subsite specificities of the recombinant cysteine proteinases CPB of Leishmania mexicana, and cruzain of Trypanosoma cruzi, using fluorescent substrates containing nonnatural basic amino acids. Mol. Biochem. Parasitol. 117:137-143. (Pubitemid 32972274)
2. Atkinson HJ, Babbitt PC, Sajid M. 2009. The global cysteine peptidase landscape in parasites. Trends Parasitol. 25:573-581.
3. Baudys M, Meloun B, Gan-Erdene T, Pohl J, Kostka V. 1990. Disulfide bridges of bovine spleen cathepsin B. Biol. Chem. Hoppe-Seyler 371:485-491. (Pubitemid 20246560)
4. Bechet DM, et al. 1991. Expression of lysosomal cathepsin B during calf myoblast-myotube differentiation. Characterization of a cDNA encoding bovine cathepsin B. J. Biol. Chem. 266:14104-14112. (Pubitemid 21907466)
5. Belli SI, Smith NC, Ferguson DJ. 2006. The coccidian oocyst: a tough nut to crack! Trends Parasitol. 22:416-423. (Pubitemid 44176413)
6. Brickmann J, Exner TE, Keil M, Marhöfer RJ. 2000. Molecular graphics: trends and perspectives. J. Mol. Mod. 6:328-340.
7. Burden FR. 1989. Molecular identification number for substructure searches. J. Chem. Infect. Comput. Sci. 29:225-227.
8. Caffrey CR, et al. 2002. SmCB2, a novel tegumental cathepsin B from adult Schistosoma mansoni. Mol. Biochem. Parasitol. 121:49-61. (Pubitemid 34457833)
9. Carruthers VB, Sherman GD, Sibley LD. 2000. The Toxoplasma adhesive protein MIC2 is proteolytically processed at multiple sites by two parasite-derived proteases. J. Biol. Chem. 275:14346-14353. (Pubitemid 30339717)
10. Cavasotto CN, Phatak SS. 2009. Homology modeling in drug discovery: current trends and applications. Drug Discov. Today 14:676-683.
11. Chan SJ, San Segundo BS, McCormick MB, Steiner DF. 1986. Nucleotide and predicted amino acid sequences of cloned human and mouse preprocathepsin B cDNAs. Proc. Natl. Acad. Sci. U. S. A. 83:7721-7725. (Pubitemid 17183919)
12. Chatterjee S, et al. 1997. Synthesis and biological activity of a series of potent fluoromethyl ketone inhibitors of recombinant human calpain I. J. Med. Chem. 40:3820-3828. (Pubitemid 27481727)
13. Dong AS, et al. 1995. Avian cathepsin B cDNA: sequence and demonstration that mRNAs of two sizes are produced in cell types producing large quantities of the enzyme. Biochim. Biophys. Acta 1251:69-73.
14. Dou Z, Carruthers VB. 2011. Cathepsin proteases in Toxoplasma gondii. Adv. Exp. Med. Biol. 712:49-61.
15. Du X, et al. 2002. Synthesis and structure-activity relationship study of potent trypanocidal thiosemicarbazone inhibitors of the trypanosomal cysteine protease cruzain. J. Med. Chem. 45:2695-2707. (Pubitemid 34627642)
16. Dubremetz JF. 1998. Host cell invasion by Toxoplasma gondii. Trends Microbiol. 6:27-30. (Pubitemid 28068883)
17. Dutton CJ, Banks BJ, Cooper CB. 1995. Polyether ionophores. Nat. Prod. Rep. 12:165-181.
18. Fuller AL, McDougald LR. 1990. Reduction in cell entry of Eimeria tenella (Coccidia) sporozoites by protease inhibitors, and partial characterization of proteolytic activity associated with intact sporozoites and merozoites. J. Parasitol. 76:464-467. (Pubitemid 20299294)
19. Hasnain S, Hirama T, Huber CP, Mason P, Mort JS. 1993. Characterization of cathepsin B specificity by site-directed mutagenesis. Importance of Glu245 in the S2-P2 specificity for arginine and its role in transition state stabilization. J. Biol. Chem. 268:235-240. (Pubitemid 23021311)
20. Ihlenfeldt WD, Voigt JH, Bienfait B, Oellien F, Nicklaus MC. 2002. Enhanced CACTVS browser of the Open NCI Database. J. Chem. Infect. Comput. Sci. 42:46-57. (Pubitemid 35355324)
21. Illy C, et al. 1997. Role of the occluding loop in cathepsin B activity. J. Biol. Chem. 272:1197-1202. (Pubitemid 27034617)
22. Invitrogen. 2010. Pichia expression kit user manual. Invitrogen, Carlsbad, CA. http://tools.invitrogen.com/content/sfs/manuals/pich-man.pdf.
23. Kim K. 2004. Role of proteases in host cell invasion by Toxoplasma gondii and other apicomplexa. Acta Trop. 91:69-81. (Pubitemid 38670386)
24. Kozak M. 1999. Initiation of translation in prokaryotes and eukaryotes. Gene 234:187-208. (Pubitemid 29298181)
25. Meloun B, Baudys M, Pohl J, Pavlík M, Kostka V. 1988. Amino acid sequence of bovine spleen cathepsin B. J. Biol. Chem. 263:9087-9093.
26. Musil D, et al. 1991. The refined 2.15 Å X-ray crystal structure of human liver cathepsin B: the structural basis for its specificity. EMBO J. 10:2321-2330. (Pubitemid 121000005)
27. Nielsen H, Engelbrecht J, Brunak SS, von Heijne G. 1997. A neural network method for identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Int. J. Neural. Syst. 8:581-599.
28. Nissink JWM, et al. 2002. A new test set for validating predictions of protein-ligand interaction. Proteins Struct. Funct. Genet. 49:457-471. (Pubitemid 35388132)
29. Pandey KC, Sijwali PS, Singh A, Na BK, Rosenthal PJ. 2004. Independent intramolecular mediators of folding, activity, and inhibition for the Plasmodium falciparum cysteine protease falcipain-2. J. Biol. Chem. 279:3484-3491. (Pubitemid 38140587)
30. Pearlman RS, Smith KM. 1998. Novel software tools for chemical diversity. Perspect. Drug Discov. Design 9:339-353. (Pubitemid 128491931)
31. Pearlman RS, Smith KM. 1999. Metric validation and the receptor relevant subspace concept. J. Chem. Infect. Comput. Sci. 39:28-35. (Pubitemid 129676554)
32. Que X, et al. 2002. The cathepsin B of Toxoplasma gondii, toxopain-1, is critical for parasite invasion and rhoptry protein processing. J. Biol. Chem. 277:25791-25797. (Pubitemid 34951900)
33. Rankovic Z, Cai J, Cumming I. February 2005. Preparation of 2-cyano-1,3,5-triazine-4,6-diamine derivatives for the treatment of osteoporosis and atherosclerosis. International patent WO 2005011703 A1.
34. Rankovic Z, et al. 2010. Design and optimization of a series of novel 2-cyano-pyrimidines as cathepsin K inhibitors. Bioorg. Med. Chem. Lett. 20:1524-1527.
35. Ritonja A, Popovic T, Turk V, Wiedenmann K, Machleidt W. 1985. Amino acid sequence of human liver cathepsin B. FEBS Lett. 181:169-172. (Pubitemid 15127995)
36. Rosenthal PJ. 2011. Falcipains and other cysteine proteases of malaria parasites. Adv. Exp. Med. Biol. 712:30-48.
37. Sakanari JA, et al. 1997. Leishmania major: comparison of the cathepsin L- and B-like cysteine protease genes with those of other trypanosomatids. Exp. Parasitol. 85:63-76. (Pubitemid 27236715)
38. Sanderson SJ, et al. 2000. Expression and characterization of a recombinant cysteine proteinase of Leishmania mexicana. Biochem. J. 347:383-388. (Pubitemid 30229385)
39. Selzer PM, et al. 1999. Cysteine protease inhibitors as chemotherapy: lessons from a parasite target. Proc. Natl. Acad. Sci. U. S. A. 96:11015-11022. (Pubitemid 29487320)
40. Takio K, Towatari T, Katunuma N, Teller DC, Titani K. 1983. Homology of amino acid sequence of rat liver cathepsin B and H with that of papain. Proc. Natl. Acad. Sci. U. S. A. 80:3666-3670.
41. Teixeira C, Gomes JR, Gomes P. 2011. Falcipains, Plasmodium falciparum cysteine proteases as key drug targets against malaria. Curr. Med. Chem. 18:1555-1572.
42. Verdonk ML, Cole JC, Hartshorn MJ, Murray CW, Taylor RD. 2003. Improved protein-ligand docking using GOLD. Proteins 52:609-623. (Pubitemid 37034158)
43. Wang SX, et al. 2006. Structural basis for unique mechanisms of folding and hemoglobin binding by a malarial protease. Proc. Natl. Acad. Sci. U. S. A. 103:11503-11508. (Pubitemid 44182481)
44. Whitmire WM, Kyle JE, Speer CA, Burgess DE. 1988. Inhibition of penetration of cultured cells by Eimeria bovis sporozoites by monoclonal immunoglobulin G antibodies against the parasite surface protein P20. Infect. Immun. 56:2538-2543.
45. Yamamoto A, et al. 2000. Molecular dynamics simulations of bovine cathepsin B and its complex with CA074. Chem. Pharm. Bull. 48:480-485. (Pubitemid 30246302)
46. Yamamoto A, et al. 2000. Substrate specificity of bovine cathepsin B and its inhibition by CA074, based on crystal structure refinement of the complex. J. Biochem. 127:635-643. (Pubitemid 30238357)