메뉴 건너뛰기




Volumn 114, Issue 1, 2001, Pages 81-88

Identification of peptides inhibitory to recombinant cysteine proteinase, CPB, of Leishmania mexicana

Author keywords

Cathepsin L; Cruzain; Cysteine proteinase; Inhibitors; Leishmania; Thiol protease

Indexed keywords

ANTHRANILIC ACID; ANTIPARASITIC AGENT; CATHEPSIN L; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR;

EID: 0035946413     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(01)00239-0     Document Type: Article
Times cited : (24)

References (44)
  • 1
    • 0020004009 scopus 로고
    • Proteinases of Leishmania mexicana and other flagellate protozoa
    • Coombs G.H. Proteinases of Leishmania mexicana and other flagellate protozoa. Parasitology. 84:1982;149-155.
    • (1982) Parasitology , vol.84 , pp. 149-155
    • Coombs, G.H.1
  • 2
    • 0021137779 scopus 로고
    • Purification and characterization of proteolytic enzymes of Leishmania mexicana amastigotes and promastigotes
    • Pupkis M.F., Coombs G.H. Purification and characterization of proteolytic enzymes of Leishmania mexicana amastigotes and promastigotes. J. Gen. Microbiol. 130:1984;2375-2383.
    • (1984) J. Gen. Microbiol. , vol.130 , pp. 2375-2383
    • Pupkis, M.F.1    Coombs, G.H.2
  • 3
    • 0025113919 scopus 로고
    • Characterization of three groups of cysteine proteinases in the amastigotes of Leishmania mexicana
    • Robertson C.D., Coombs G.H. Characterization of three groups of cysteine proteinases in the amastigotes of Leishmania mexicana. Mol. Biochem. Parasitol. 42:1990;269-276.
    • (1990) Mol. Biochem. Parasitol. , vol.42 , pp. 269-276
    • Robertson, C.D.1    Coombs, G.H.2
  • 4
    • 0026890633 scopus 로고
    • Stage-specific proteinases of Leishmania mexicana promastigotes
    • Robertson C.D., Coombs G.H. Stage-specific proteinases of Leishmania mexicana promastigotes. FEMS Microbiol. Lett. 94:1992;127-132.
    • (1992) FEMS Microbiol. Lett. , vol.94 , pp. 127-132
    • Robertson, C.D.1    Coombs, G.H.2
  • 5
    • 0028425460 scopus 로고
    • Expression of cysteine proteinases by metacyclic promastigotes of Leishmania mexicana
    • Bates P.A., Robertson C.D., Coombs G.H. Expression of cysteine proteinases by metacyclic promastigotes of Leishmania mexicana. J. Euk. Microbiol. 41:1994;199-203.
    • (1994) J. Euk. Microbiol. , vol.41 , pp. 199-203
    • Bates, P.A.1    Robertson, C.D.2    Coombs, G.H.3
  • 6
    • 0030970429 scopus 로고    scopus 로고
    • The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences
    • Mottram J.C., Frame M.C., Brooks D.R., Tetley L., Hutchison J.E., Souza A.E., Coombs G.H. The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences. J. Biol. Chem. 272:1997;14285-14293.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14285-14293
    • Mottram, J.C.1    Frame, M.C.2    Brooks, D.R.3    Tetley, L.4    Hutchison, J.E.5    Souza, A.E.6    Coombs, G.H.7
  • 7
    • 0026783342 scopus 로고
    • Characterization of a multicopy gene for a major stage-specific cysteine proteinase of Leishmania mexicana
    • Souza A.E., Waugh S., Coombs G.H., Mottram J.C. Characterization of a multicopy gene for a major stage-specific cysteine proteinase of Leishmania mexicana. FEBS Lett. 311:1992;124-127.
    • (1992) FEBS Lett. , vol.311 , pp. 124-127
    • Souza, A.E.1    Waugh, S.2    Coombs, G.H.3    Mottram, J.C.4
  • 8
    • 0028202206 scopus 로고
    • Multiple high activity cysteine proteases of Leishmania mexicana are encoded by the lmcpb gene array
    • Robertson C.D., Coombs G.H. Multiple high activity cysteine proteases of Leishmania mexicana are encoded by the lmcpb gene array. Microbiology. 140:1994;417-424.
    • (1994) Microbiology , vol.140 , pp. 417-424
    • Robertson, C.D.1    Coombs, G.H.2
  • 9
    • 0029898541 scopus 로고    scopus 로고
    • Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors
    • Mottram J.C., Souza A.E., Hutchison J.E., Carter R., Frame M.J., Coombs G.H. Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors. Proc. Natl. Acad. Sci. USA. 93:1996;6008-6013.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6008-6013
    • Mottram, J.C.1    Souza, A.E.2    Hutchison, J.E.3    Carter, R.4    Frame, M.J.5    Coombs, G.H.6
  • 11
    • 0027476019 scopus 로고
    • Identification of two distinct cysteine proteinase genes of Leishmania pifanoi axenic amastigotes using the polymerase chain reaction
    • Traub-Cseko Y.M., Duboise M., Boukai L.K., McMahon-Pratt D. Identification of two distinct cysteine proteinase genes of Leishmania pifanoi axenic amastigotes using the polymerase chain reaction. Mol. Biochem. Parasitol. 57:1993;101-116.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 101-116
    • Traub-Cseko, Y.M.1    Duboise, M.2    Boukai, L.K.3    McMahon-Pratt, D.4
  • 12
    • 0030981096 scopus 로고    scopus 로고
    • Leishmania major: Comparison of the cathepsin L- And B-like cysteine protease genes with those of other trypanosomatids
    • Sakanari J.A., Nadler S.A., Chan V.J., Engel J.C., Leptak C., Bouvier J. Leishmania major: comparison of the cathepsin L- and B-like cysteine protease genes with those of other trypanosomatids. Exp. Parasitol. 85:1997;63-76.
    • (1997) Exp. Parasitol. , vol.85 , pp. 63-76
    • Sakanari, J.A.1    Nadler, S.A.2    Chan, V.J.3    Engel, J.C.4    Leptak, C.5    Bouvier, J.6
  • 13
    • 0026570815 scopus 로고
    • The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes
    • Campetella O., Henriksson J., Åslund L., Frasch A.C.C., Pettersson U., Cazzulo J.J. The major cysteine proteinase (cruzipain) from Trypanosoma cruzi is encoded by multiple polymorphic tandemly organized genes located on different chromosomes. Mol. Biochem. Parasitol. 50:1992;225-234.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 225-234
    • Campetella, O.1    Henriksson, J.2    Åslund, L.3    Frasch, A.C.C.4    Pettersson, U.5    Cazzulo, J.J.6
  • 15
    • 0024329436 scopus 로고
    • A cysteine proteinase cDNA from Trypanosoma brucei predicts an enzyme with an unusual C-terminal extension
    • Mottram J.C., North M.J., Barry J.D., Coombs G.H. A cysteine proteinase cDNA from Trypanosoma brucei predicts an enzyme with an unusual C-terminal extension. FEBS Lett. 258:1989;211-215.
    • (1989) FEBS Lett. , vol.258 , pp. 211-215
    • Mottram, J.C.1    North, M.J.2    Barry, J.D.3    Coombs, G.H.4
  • 16
    • 0030981772 scopus 로고    scopus 로고
    • Parasite proteinases and amino acid metabolism: Possibilities for chemotherapeutic exploitation
    • Coombs G.H., Mottram J.C. Parasite proteinases and amino acid metabolism: possibilities for chemotherapeutic exploitation. Parasitology. 114:1997;S61-S80.
    • (1997) Parasitology , vol.114 , pp. 61-S80
    • Coombs, G.H.1    Mottram, J.C.2
  • 18
    • 0026606269 scopus 로고
    • Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi in vitro
    • Meirelles M.N.L., Juliano L., Carmona E., Silva S.G., Costa E.M., Murta A.C., Scharfstein J. Inhibitors of the major cysteinyl proteinase (GP57/51) impair host cell invasion and arrest the intracellular development of Trypanosoma cruzi in vitro. Mol. Biochem. Parasitol. 52:1992;175-184.
    • (1992) Mol. Biochem. Parasitol. , vol.52 , pp. 175-184
    • Meirelles, M.N.L.1    Juliano, L.2    Carmona, E.3    Silva, S.G.4    Costa, E.M.5    Murta, A.C.6    Scharfstein, J.7
  • 19
    • 0032541311 scopus 로고    scopus 로고
    • Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection
    • Engel J.C., Doyle P.S., Hsieh I., McKerrow J.H. Cysteine protease inhibitors cure an experimental Trypanosoma cruzi infection. J. Exp. Med. 188:1998;725-734.
    • (1998) J. Exp. Med. , vol.188 , pp. 725-734
    • Engel, J.C.1    Doyle, P.S.2    Hsieh, I.3    McKerrow, J.H.4
  • 21
    • 0033820138 scopus 로고    scopus 로고
    • Analysis of the roles of cysteine proteinases of Leishmania mexicana in the host-parasite interaction
    • Frame M.J., Mottram J.C., Coombs G.H. Analysis of the roles of cysteine proteinases of Leishmania mexicana in the host-parasite interaction. Parasitology. 121:2000;367-377.
    • (2000) Parasitology , vol.121 , pp. 367-377
    • Frame, M.J.1    Mottram, J.C.2    Coombs, G.H.3
  • 22
    • 0032781317 scopus 로고    scopus 로고
    • Development of cysteine protease inhibitors as chemotherapy for parasitic diseases: Insights on safety, target validation, and mechanism of action
    • McKerrow J.H. Development of cysteine protease inhibitors as chemotherapy for parasitic diseases: insights on safety, target validation, and mechanism of action. Int. J. Parasitol. 29:1999;833-837.
    • (1999) Int. J. Parasitol. , vol.29 , pp. 833-837
    • McKerrow, J.H.1
  • 23
    • 0032129794 scopus 로고    scopus 로고
    • Roles of cysteine proteinases of trypanosomes and Leishmania in host-parasite interactions
    • Mottram J.C., Brooks D.R., Coombs G.H. Roles of cysteine proteinases of trypanosomes and Leishmania in host-parasite interactions. Curr. Opin. Microbiol. 1:1998;455-460.
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 455-460
    • Mottram, J.C.1    Brooks, D.R.2    Coombs, G.H.3
  • 24
    • 0033083293 scopus 로고    scopus 로고
    • Recent advances in identifying and validating drug targets in trypanosomes and leishmanias
    • Barrett M.P., Mottram J.C., Coombs G.H. Recent advances in identifying and validating drug targets in trypanosomes and leishmanias. Trends Microbiol. 7:1999;82-88.
    • (1999) Trends Microbiol. , vol.7 , pp. 82-88
    • Barrett, M.P.1    Mottram, J.C.2    Coombs, G.H.3
  • 26
    • 0034683233 scopus 로고    scopus 로고
    • The substrate specificity of a recombinant cysteine protease from Leishmania mexicana: Application of a combinatorial peptide library approach
    • Hilaire P.M.S., Alves L.C., Sanderson S.J., Mottram J.C., Juliano M.A., Juliano L., Coombs G.H., Meldal M. The substrate specificity of a recombinant cysteine protease from Leishmania mexicana: Application of a combinatorial peptide library approach. Chembiochem. 1:2000;115-122.
    • (2000) Chembiochem , vol.1 , pp. 115-122
    • Hilaire, P.M.S.1    Alves, L.C.2    Sanderson, S.J.3    Mottram, J.C.4    Juliano, M.A.5    Juliano, L.6    Coombs, G.H.7    Meldal, M.8
  • 27
    • 0029902382 scopus 로고    scopus 로고
    • Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment
    • Coulombe R., Grochulski P., Sivaraman J., Menard R., Mort J.S., Cygler M. Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment. EMBO J. 15:1996;5492-5503.
    • (1996) EMBO J. , vol.15 , pp. 5492-5503
    • Coulombe, R.1    Grochulski, P.2    Sivaraman, J.3    Menard, R.4    Mort, J.S.5    Cygler, M.6
  • 28
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • Carmona E., Dufour É., Plouffe C., Takebe S., Manson P., Mort S.M., Ménard R. Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry. 35:1996;8149-8157.
    • (1996) Biochemistry , vol.35 , pp. 8149-8157
    • Carmona, E.1    Dufour, É.2    Plouffe, C.3    Takebe, S.4    Manson, P.5    Mort, S.M.6    Ménard, R.7
  • 29
    • 0027068057 scopus 로고
    • Potent slow-binding inhibition of cathepsin B by its propeptide
    • Fox T., de Miguel E., Mort J.S., Storer A.C. Potent slow-binding inhibition of cathepsin B by its propeptide. Biochemistry. 31:1992;12571-12576.
    • (1992) Biochemistry , vol.31 , pp. 12571-12576
    • Fox, T.1    De Miguel, E.2    Mort, J.S.3    Storer, A.C.4
  • 30
    • 0029976244 scopus 로고    scopus 로고
    • Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide
    • Turk D., Podobnik M., Kuhelj R., Dolinar M., Turk V. Crystal structures of human procathepsin B at 3.2 and 3.3 Angstroms resolution reveal an interaction motif between a papain-like cysteine protease and its propeptide. FEBS Lett. 384:1996;211-214.
    • (1996) FEBS Lett. , vol.384 , pp. 211-214
    • Turk, D.1    Podobnik, M.2    Kuhelj, R.3    Dolinar, M.4    Turk, V.5
  • 31
    • 0030584678 scopus 로고    scopus 로고
    • Structure of rat procathepsin B: Model for inhibition of cysteine protease activity by the proregion
    • Cygler M., Sivaraman J., Grochulski P., Coulombe R., Storer A.C., Mort J.S. Structure of rat procathepsin B: model for inhibition of cysteine protease activity by the proregion. Structure. 4:1996;405-416.
    • (1996) Structure , vol.4 , pp. 405-416
    • Cygler, M.1    Sivaraman, J.2    Grochulski, P.3    Coulombe, R.4    Storer, A.C.5    Mort, J.S.6
  • 32
    • 0030565487 scopus 로고    scopus 로고
    • Inhibition of cathepsin B by its propeptide: Use of overlapping peptides to identify a critical segment
    • Chagas J.R., Ferrer-Di Martino M., Gauthier F., Lalmanach G. Inhibition of cathepsin B by its propeptide: use of overlapping peptides to identify a critical segment. FEBS Lett. 392:1996;233-236.
    • (1996) FEBS Lett. , vol.392 , pp. 233-236
    • Chagas, J.R.1    Ferrer-Di Martino, M.2    Gauthier, F.3    Lalmanach, G.4
  • 34
    • 0032980694 scopus 로고    scopus 로고
    • The propeptide of Fasciola hepatica cathepsin L is a potent and selective inhibitor of the mature enzyme
    • Roche L., Tort J., Dalton J.P. The propeptide of Fasciola hepatica cathepsin L is a potent and selective inhibitor of the mature enzyme. Mol. Biochem. Parasitol. 98:1999;271-277.
    • (1999) Mol. Biochem. Parasitol. , vol.98 , pp. 271-277
    • Roche, L.1    Tort, J.2    Dalton, J.P.3
  • 35
    • 0030891637 scopus 로고    scopus 로고
    • Characterization of the substrate specificity of the major cysteine proteinase (cruzipain) from Trypanosona cruzi using a portion-mixing combinatorial library and fluorogenic peptides
    • Del Nery E., Scharfstein J., Meldal M., Svendsen I., Walmsley A., Juliano M.A., Juliano L. Characterization of the substrate specificity of the major cysteine proteinase (cruzipain) from Trypanosona cruzi using a portion-mixing combinatorial library and fluorogenic peptides. Biochem. J. 323:1997;427-433.
    • (1997) Biochem. J. , vol.323 , pp. 427-433
    • Del Nery, E.1    Scharfstein, J.2    Meldal, M.3    Svendsen, I.4    Walmsley, A.5    Juliano, M.A.6    Juliano, L.7
  • 36
    • 0025967144 scopus 로고
    • Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins
    • Chagas J.R., Juliano L., Prado E.S. Intramolecularly quenched fluorogenic tetrapeptide substrates for tissue and plasma kallikreins. Anal. Biochem. 192:1990;419-425.
    • (1990) Anal. Biochem. , vol.192 , pp. 419-425
    • Chagas, J.R.1    Juliano, L.2    Prado, E.S.3
  • 38
    • 34249758919 scopus 로고
    • Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs
    • Hirata Y., Cezari M.H.S., Nakaie C.R., Boschcov P., Ito A.S., Juliano M.A., Juliano L. Internally quenched fluorogenic protease substrates: Solid-phase synthesis and fluorescence spectroscopy of peptides containing ortho-aminobenzoyl/dinitrophenyl groups as donor-acceptor pairs. Lett. Peptide Sci. 1:1994;299-308.
    • (1994) Lett. Peptide Sci. , vol.1 , pp. 299-308
    • Hirata, Y.1    Cezari, M.H.S.2    Nakaie, C.R.3    Boschcov, P.4    Ito, A.S.5    Juliano, M.A.6    Juliano, L.7
  • 39
    • 0026620531 scopus 로고
    • Temperature-dependent substrate inhibition of the cysteine proteinase (GP57/51) from Trypanosoma cruzi
    • Lima A.P.C.A., Scharfstein J., Storer A.C., Menard R. Temperature-dependent substrate inhibition of the cysteine proteinase (GP57/51) from Trypanosoma cruzi. Mol. Biochem. Parasitol. 56:1992;335-338.
    • (1992) Mol. Biochem. Parasitol. , vol.56 , pp. 335-338
    • Lima, A.P.C.A.1    Scharfstein, J.2    Storer, A.C.3    Menard, R.4
  • 40
    • 0005499841 scopus 로고
    • Statistical estimations in enzyme kinetics
    • Wilkinson G.N. Statistical estimations in enzyme kinetics. Biochem. J. 80:1961;324-332.
    • (1961) Biochem. J. , vol.80 , pp. 324-332
    • Wilkinson, G.N.1
  • 41
    • 0021676681 scopus 로고
    • Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin
    • Nicklin M.J., Barrett A.J. Inhibition of cysteine proteinases and dipeptidyl peptidase I by egg-white cystatin. Biochem. J. 223:1984;245-253.
    • (1984) Biochem. J. , vol.223 , pp. 245-253
    • Nicklin, M.J.1    Barrett, A.J.2
  • 42
    • 0030970429 scopus 로고    scopus 로고
    • The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences
    • Mottram J.C., Frame M.J., Brooks D.R., Tetley L., Hutchison J.E., Souza A.E., Coombs G.H. The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes that differ in their stage regulation and substrate preferences. J. Biol. Chem. 272:1997;14285-14293.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14285-14293
    • Mottram, J.C.1    Frame, M.J.2    Brooks, D.R.3    Tetley, L.4    Hutchison, J.E.5    Souza, A.E.6    Coombs, G.H.7
  • 43
    • 0031468018 scopus 로고    scopus 로고
    • Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity
    • Cygler M., Mort J.S. Proregion structure of members of the papain superfamily. Mode of inhibition of enzymatic activity. Biochimie. 79:1997;645-652.
    • (1997) Biochimie , vol.79 , pp. 645-652
    • Cygler, M.1    Mort, J.S.2
  • 44
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft
    • Groves M.R., Taylor M.A.J., Scott M., Cummings N.J., Pikersgill R.W., Jenkins J.A. The prosequence of procaricain forms an α-helical domain that prevents access to the substrate-binding cleft. Structure. 4:1996;1193-1203.
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.J.2    Scott, M.3    Cummings, N.J.4    Pikersgill, R.W.5    Jenkins, J.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.