메뉴 건너뛰기




Volumn 54, Issue 5, 2004, Pages 1224-1236

A potential role for ICP, a leishmanial inhibitor of cysteine peptidases, in the interaction between host and parasite

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE PROTEINASE; ENZYME PRECURSOR; INHIBITOR OF CYSTEINE PEPTIDASE; PROTOZOAL PROTEIN; UNCLASSIFIED DRUG;

EID: 9644257515     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2004.04355.x     Document Type: Article
Times cited : (56)

References (45)
  • 2
    • 0032534577 scopus 로고    scopus 로고
    • Leishmania mexicana cysteine proteinase-deficient mutants have attenuated virulence for mice and potentiate a T Helper 1 (TH1) response
    • Alexander, J., Coombs, G.H., and Mottram, J.C. (1998) Leishmania mexicana cysteine proteinase-deficient mutants have attenuated virulence for mice and potentiate a T Helper 1 (TH1) response. J Immunol 161: 6794-6801.
    • (1998) J Immunol , vol.161 , pp. 6794-6801
    • Alexander, J.1    Coombs, G.H.2    Mottram, J.C.3
  • 3
    • 0032883457 scopus 로고    scopus 로고
    • Leishmania species: Models of intracellular parasitism
    • Alexander, J., Satoskar, A.R., and Russell, D.G. (1999) Leishmania species: models of intracellular parasitism. J Cell Sci 112: 2993-3002.
    • (1999) J Cell Sci , vol.112 , pp. 2993-3002
    • Alexander, J.1    Satoskar, A.R.2    Russell, D.G.3
  • 4
    • 0028809686 scopus 로고
    • Isolation of lmcpc, a gene encoding a Leishmania mexicana cathepsin B-like cysteine proteinase
    • Bart, G., Coombs, G.H., and Mottram, J.C. (1995) Isolation of lmcpc, a gene encoding a Leishmania mexicana cathepsin B-like cysteine proteinase. Mol Biochem Parasitol 73: 271-274.
    • (1995) Mol Biochem Parasitol , vol.73 , pp. 271-274
    • Bart, G.1    Coombs, G.H.2    Mottram, J.C.3
  • 5
    • 0026674542 scopus 로고
    • Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms
    • Bates, P.A., Robertson, C.D., Tetley, L., and Coombs, G.H. (1992) Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms. Parasitology 105: 193-202.
    • (1992) Parasitology , vol.105 , pp. 193-202
    • Bates, P.A.1    Robertson, C.D.2    Tetley, L.3    Coombs, G.H.4
  • 6
    • 0034474592 scopus 로고    scopus 로고
    • Processing and trafficking of cysteine proteases in Leishmania mexicana
    • Brooks, D.R., Tetley, L., Coombs, G.H., and Mottram, J.C. (2000a) Processing and trafficking of cysteine proteases in Leishmania mexicana. J Cell Sci 113: 4035-4041.
    • (2000) J Cell Sci , vol.113 , pp. 4035-4041
    • Brooks, D.R.1    Tetley, L.2    Coombs, G.H.3    Mottram, J.C.4
  • 7
    • 0034607789 scopus 로고    scopus 로고
    • Stable transformation of trypanosomatids through targeted chromosomal integration of the selectable marker gene encoding basticidin S deaminase
    • Brooks, D.R., McCulloch, R., Coombs, G.H., and Mottram, J.C. (2000b) Stable transformation of trypanosomatids through targeted chromosomal integration of the selectable marker gene encoding basticidin S deaminase. FEMS Microbiol Lett 186: 287-291.
    • (2000) FEMS Microbiol Lett , vol.186 , pp. 287-291
    • Brooks, D.R.1    McCulloch, R.2    Coombs, G.H.3    Mottram, J.C.4
  • 8
    • 0035869563 scopus 로고    scopus 로고
    • Successful therapy of lethal murine visceral leishmaniasis with cystatin involves up-regulation of nitric oxide and a favorable T cell response
    • Das, L., Datta, N., Bandyopadhyay, S., and Das, P.K. (2001) Successful therapy of lethal murine visceral leishmaniasis with cystatin involves up-regulation of nitric oxide and a favorable T cell response. J Immunol 166: 4020-4028.
    • (2001) J Immunol , vol.166 , pp. 4020-4028
    • Das, L.1    Datta, N.2    Bandyopadhyay, S.3    Das, P.K.4
  • 10
    • 1942532958 scopus 로고    scopus 로고
    • Sphingolipid-free Leishmania are defective in membrane trafficking, differentiation and infectivity
    • Denny, P.W., Goulding, D., Ferguson, M.A.J., and Smith, D.F. (2004) Sphingolipid-free Leishmania are defective in membrane trafficking, differentiation and infectivity. Mol Microbiol 52: 313-327.
    • (2004) Mol Microbiol , vol.52 , pp. 313-327
    • Denny, P.W.1    Goulding, D.2    Ferguson, M.A.J.3    Smith, D.F.4
  • 11
    • 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., and Coombs, G.H. (2000) Analysis of the roles of cysteine proteinases of Leishmania mexicana in the host-parasite interaction. Parasitology 121: 367-377.
    • (2000) Parasitology , vol.121 , pp. 367-377
    • Frame, M.J.1    Mottram, J.C.2    Coombs, G.H.3
  • 12
    • 0035794186 scopus 로고    scopus 로고
    • The role of phosphomannose isomerase in Leishmania mexicana glycoconjugate synthesis and virulence
    • Garami, A., and Ilg, T. (2001) The role of phosphomannose isomerase in Leishmania mexicana glycoconjugate synthesis and virulence. J Biol Chem 276: 6566-6575.
    • (2001) J Biol Chem , vol.276 , pp. 6566-6575
    • Garami, A.1    Ilg, T.2
  • 13
    • 0035012676 scopus 로고    scopus 로고
    • Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan
    • Ghedin, E., Debrabant, A., Engel, J.C., and Dwyer, D.M. (2001) Secretory and endocytic pathways converge in a dynamic endosomal system in a primitive protozoan. Traffic 2: 175-188.
    • (2001) Traffic , vol.2 , pp. 175-188
    • Ghedin, E.1    Debrabant, A.2    Engel, J.C.3    Dwyer, D.M.4
  • 15
    • 0031826072 scopus 로고    scopus 로고
    • Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
    • Groves, M.R., Coulombe, R., Jenkins, J., and Cygler, M. (1998) Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Protein-Struct Fund Genet 32: 504-514.
    • (1998) Protein-Struct Fund Genet , vol.32 , pp. 504-514
    • Groves, M.R.1    Coulombe, R.2    Jenkins, J.3    Cygler, M.4
  • 16
    • 0035490884 scopus 로고    scopus 로고
    • The endocytic pathway: A mosaic of domains
    • Gruenberg, J. (2001) The endocytic pathway: a mosaic of domains. Nat Rev Mol Cell Biol 2: 721-730.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 721-730
    • Gruenberg, J.1
  • 18
    • 0033016717 scopus 로고    scopus 로고
    • Correlation between protein and mRNA abundance in yeast
    • Gygi, S.P., Rochon, Y., Franza, B.R., and Aebersold, R. (1999) Correlation between protein and mRNA abundance in yeast. Mol Cell Biol 19: 1720-1730.
    • (1999) Mol Cell Biol , vol.19 , pp. 1720-1730
    • Gygi, S.P.1    Rochon, Y.2    Franza, B.R.3    Aebersold, R.4
  • 19
    • 0343267840 scopus 로고    scopus 로고
    • Use of the green fluorescent protein as a marker in transfected Leishmania
    • Ha, D.S., Schwarz, J.K., Turco, S.J., and Beverley, S.M. (1996) Use of the green fluorescent protein as a marker in transfected Leishmania. Mol Biochem Parasitol 77: 57-64.
    • (1996) Mol Biochem Parasitol , vol.77 , pp. 57-64
    • Ha, D.S.1    Schwarz, J.K.2    Turco, S.J.3    Beverley, S.M.4
  • 20
    • 0039702904 scopus 로고    scopus 로고
    • Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif
    • Huete-Pérez, J.A., Engel, J.C., Brinen, L.S., Mottram, J.C., and McKerrow, J.H. (1999) Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif. J Biol Chem 274: 16249-16256.
    • (1999) J Biol Chem , vol.274 , pp. 16249-16256
    • Huete-Pérez, J.A.1    Engel, J.C.2    Brinen, L.S.3    Mottram, J.C.4    McKerrow, J.H.5
  • 21
    • 0027947483 scopus 로고
    • Distribution of parasite cysteine proteinases in lesions of mice infected with Leishmania mexicana amastigotes
    • Ilg, T., Fuchs, M., Gnau, V., Wolfram, M., Harbecke, D., and Overath, P. (1994) Distribution of parasite cysteine proteinases in lesions of mice infected with Leishmania mexicana amastigotes. Mol Biochem Parasitol 67: 193-203.
    • (1994) Mol Biochem Parasitol , vol.67 , pp. 193-203
    • Ilg, T.1    Fuchs, M.2    Gnau, V.3    Wolfram, M.4    Harbecke, D.5    Overath, P.6
  • 22
    • 0026915084 scopus 로고
    • Cystatin-like cysteine proteinase inhibitors of parasitic protozoa
    • Irvine, J.W., Coombs, G.H., and North, M.J. (1992) Cystatin-like cysteine proteinase inhibitors of parasitic protozoa. FEMS Microbiol Lett 96: 67-72.
    • (1992) FEMS Microbiol Lett , vol.96 , pp. 67-72
    • Irvine, J.W.1    Coombs, G.H.2    North, M.J.3
  • 26
    • 0242693036 scopus 로고    scopus 로고
    • Targeted integration into a rRNA locus results in uniform and high level expression of transgenes in Leish-mania amastigotes
    • Misslitz, A., Mottram, J.C., Overath, P., and Aebischer, T. (2000) Targeted integration into a rRNA locus results in uniform and high level expression of transgenes in Leish-mania amastigotes. Mol Biochem Parasitol 107: 251-261.
    • (2000) Mol Biochem Parasitol , vol.107 , pp. 251-261
    • Misslitz, A.1    Mottram, J.C.2    Overath, P.3    Aebischer, T.4
  • 27
    • 0035189728 scopus 로고    scopus 로고
    • Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi
    • Monteiro, A.C.S., Abrahamson, M., Lima, A.P.C.A., Vannier-Santos, M.A., and Scharfstein, J. (2001) Identification, characterization and localization of chagasin, a tight-binding cysteine protease inhibitor in Trypanosoma cruzi. J Cell Sci 114: 3933-3942.
    • (2001) J Cell Sci , vol.114 , pp. 3933-3942
    • Monteiro, A.C.S.1    Abrahamson, M.2    Lima, A.P.C.A.3    Vannier-Santos, M.A.4    Scharfstein, J.5
  • 28
    • 0036861169 scopus 로고    scopus 로고
    • The kinetoplastida endocytic apparatus. Part I: A dynamic system for nutrition and evasion of host defences
    • Morgan, G.W., Hall, B.S., Denny, P.W., Carrington, M., and Field, M.C. (2002a) The kinetoplastida endocytic apparatus. Part I: a dynamic system for nutrition and evasion of host defences. Trends Parasitol 18: 491-496.
    • (2002) Trends Parasitol , vol.18 , pp. 491-496
    • Morgan, G.W.1    Hall, B.S.2    Denny, P.W.3    Carrington, M.4    Field, M.C.5
  • 29
    • 0036898661 scopus 로고    scopus 로고
    • The endocytic apparatus of the kinetoplastida. Part II: Machinery and components of the system
    • Morgan, G.W., Hall, B.S., Denny, P.W., Field, M.C., and Carrington, M. (2002b) The endocytic apparatus of the kinetoplastida. Part II: machinery and components of the system. Trends Parasitol 18: 540-546.
    • (2002) Trends Parasitol , vol.18 , pp. 540-546
    • Morgan, G.W.1    Hall, B.S.2    Denny, P.W.3    Field, M.C.4    Carrington, M.5
  • 30
    • 0026708826 scopus 로고
    • A developmentally regulated cysteine proteinase gene of Leishmania mexicana
    • Mottram, U.C., Robertson, C.D., Coombs, G.H., and Barry, J.D. (1992) A developmentally regulated cysteine proteinase gene of Leishmania mexicana. Mol Microbiol 6: 1925-1932.
    • (1992) Mol Microbiol , vol.6 , pp. 1925-1932
    • Mottram, U.C.1    Robertson, C.D.2    Coombs, G.H.3    Barry, J.D.4
  • 31
    • 0029898541 scopus 로고    scopus 로고
    • Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors
    • Mottram, U.C., Souza, A.E., Hutchison, U.E., Carter, R., Frame, M.J., and Coombs, G.H. (1996) Evidence from disruption of the lmcpb gene array of Leishmania mexicana that cysteine proteinases are virulence factors. Proc Natl Acad Sci USA 93: 6008-6013.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 6008-6013
    • Mottram, U.C.1    Souza, A.E.2    Hutchison, U.E.3    Carter, R.4    Frame, M.J.5    Coombs, G.H.6
  • 32
    • 0030970429 scopus 로고    scopus 로고
    • The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes which differ in their stage-regulation and substrate preferences
    • Mottram, U.C., Frame, M.J., Brooks, D.R., Tetley, L., Hutchison, J.E., Souza, A.E., and Coombs, G.H. (1997) The multiple cpb cysteine proteinase genes of Leishmania mexicana encode isoenzymes which differ in their stage-regulation and substrate preferences. J Biol Chem 272: 14285-14293.
    • (1997) J Biol Chem , vol.272 , pp. 14285-14293
    • Mottram, U.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
  • 33
    • 4143091399 scopus 로고    scopus 로고
    • Cysteine peptidases as virulence factors of Leishmania
    • Mottram, J.C., Coombs, G.H., and Alexander, J. (2004) Cysteine peptidases as virulence factors of Leishmania. Curr Opin Microbiol 7: 375-381.
    • (2004) Curr Opin Microbiol , vol.7 , pp. 375-381
    • Mottram, J.C.1    Coombs, G.H.2    Alexander, J.3
  • 35
    • 0033592539 scopus 로고    scopus 로고
    • N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei
    • Nolan, D.P., Geuskens, M., and Pays, E. (1999) N-linked glycans containing linear poly-N-acetyllactosamine as sorting signals in endocytosis in Trypanosoma brucei. Curr Biol 9: 1169-1172.
    • (1999) Curr Biol , vol.9 , pp. 1169-1172
    • Nolan, D.P.1    Geuskens, M.2    Pays, E.3
  • 36
    • 0037088614 scopus 로고    scopus 로고
    • Differential endocytic functions of Trypanosoma brucei Rab5 isoforms reveal a glycosylphosphatidylinositol-specific endosomal pathway
    • Pal, A., Hall, B.S., Nesbeth, D.N., Field, H.I., and Field, M.C. (2002) Differential endocytic functions of Trypanosoma brucei Rab5 isoforms reveal a glycosylphosphatidylinositol-specific endosomal pathway. J Biol Chem 277: 9529-9539.
    • (2002) J Biol Chem , vol.277 , pp. 9529-9539
    • Pal, A.1    Hall, B.S.2    Nesbeth, D.N.3    Field, H.I.4    Field, M.C.5
  • 37
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D.N., Pappin, D.J.C., Creasy, D.M., and Cottrell, J.S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 38
    • 0022479593 scopus 로고
    • Leishmania mexicana: Amastigote hydrolases in unusual lysosomes
    • Pupkis, M.F., Tetley, L., and Coombs, G.H. (1986) Leishmania mexicana: amastigote hydrolases in unusual lysosomes. Exp Parasitol 62: 29-39.
    • (1986) Exp Parasitol , vol.62 , pp. 29-39
    • Pupkis, M.F.1    Tetley, L.2    Coombs, G.H.3
  • 39
    • 0036076146 scopus 로고    scopus 로고
    • Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors
    • Rigden, D.J., Mosolov, V.V., and Galperin, M.Y. (2002) Sequence conservation in the chagasin family suggests a common trend in cysteine proteinase binding by unrelated protein inhibitors. Protein Sci 11: 1971-1977.
    • (2002) Protein Sci , vol.11 , pp. 1971-1977
    • Rigden, D.J.1    Mosolov, V.V.2    Galperin, M.Y.3
  • 40
    • 0025113919 scopus 로고
    • Characterization of 3 groups of cysteine proteinases in the amastigotes of Leishmania mexicana mexicana
    • Robertson, C.D., and Coombs, G.H. (1990) Characterization of 3 groups of cysteine proteinases in the amastigotes of Leishmania mexicana mexicana. Mol Biochem Parasitol 42: 269-276.
    • (1990) Mol Biochem Parasitol , vol.42 , pp. 269-276
    • Robertson, C.D.1    Coombs, G.H.2
  • 41
    • 0035048929 scopus 로고    scopus 로고
    • Leishmania-sand fly interactions controlling species-specific vector competence
    • Sacks, D.L. (2001) Leishmania-sand fly interactions controlling species-specific vector competence. Cell Microbiol 3: 189-196.
    • (2001) Cell Microbiol , vol.3 , pp. 189-196
    • Sacks, D.L.1
  • 42
    • 0038025678 scopus 로고    scopus 로고
    • Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens
    • Sanderson, S.J., Westrop, G.D., Scharfstein, J., Mottram, J.C., and Coombs, G.H. (2003) Functional conservation of a natural cysteine peptidase inhibitor in protozoan and bacterial pathogens. FEBS Left 542: 12-16.
    • (2003) FEBS Left , vol.542 , pp. 12-16
    • Sanderson, S.J.1    Westrop, G.D.2    Scharfstein, J.3    Mottram, J.C.4    Coombs, G.H.5
  • 43
    • 13044256387 scopus 로고    scopus 로고
    • Cysteine protease inhibitors as chemotherapy: Lessons from a parasite target
    • Selzer, P.M., Pingel, S., Hsieh, I., Ugele, B., Chan, V.J., Engel, J.C., et al. (1999) Cysteine protease inhibitors as chemotherapy: lessons from a parasite target. Proc Natl Acad Sci USA 96: 11015-11022.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11015-11022
    • Selzer, P.M.1    Pingel, S.2    Hsieh, I.3    Ugele, B.4    Chan, V.J.5    Engel, J.C.6
  • 44
    • 0242389827 scopus 로고    scopus 로고
    • Rab5-mediated endosome-endosome fusion regulates hemoglobin endocytosis in Leishmania donovani
    • Singh, S.B., Tandon, R., Krishnamurthy, G., Vikram, R., Sharma, N., Basu, S.K., and Mukhopadhyay, A. (2003) Rab5-mediated endosome-endosome fusion regulates hemoglobin endocytosis in Leishmania donovani. EMBO J 22: 5712-5722.
    • (2003) EMBO J , vol.22 , pp. 5712-5722
    • Singh, S.B.1    Tandon, R.2    Krishnamurthy, G.3    Vikram, R.4    Sharma, N.5    Basu, S.K.6    Mukhopadhyay, A.7
  • 45
    • 0036829716 scopus 로고    scopus 로고
    • Developmental changes in lysosome morphology and function Leishmania parasites
    • Waller, R.F., and McConville, M.J. (2002) Developmental changes in lysosome morphology and function Leishmania parasites, Int J Parasitol 32: 1435-1445.
    • (2002) Int J Parasitol , vol.32 , pp. 1435-1445
    • Waller, R.F.1    McConville, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.