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Volumn 160, Issue 2, 2008, Pages 129-137

Identification and characterization of a cathepsin L-like cysteine protease from Gnathostoma spinigerum

Author keywords

Cathepsin L; Cysteine protease; Gnathostoma spinigerum; Gnathostomiasis; Pichia pastoris expression; Recombinant protein

Indexed keywords

CATHEPSIN L; CYSTEINE PROTEINASE; PROTEINASE;

EID: 50049131642     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2008.05.001     Document Type: Article
Times cited : (15)

References (47)
  • 1
    • 0027514602 scopus 로고
    • Clinical gnathostomiasis: case report and review of the English-language literature
    • Rusnak J.M., and Lucey D.R. Clinical gnathostomiasis: case report and review of the English-language literature. Clin Infect Dis 16 (1993) 33-50
    • (1993) Clin Infect Dis , vol.16 , pp. 33-50
    • Rusnak, J.M.1    Lucey, D.R.2
  • 2
    • 0031928623 scopus 로고    scopus 로고
    • The course of anaemia after the treatment of acute, falciparum malaria
    • Camacho L.H., Gordeuk V.R., Wilairatana P., et al. The course of anaemia after the treatment of acute, falciparum malaria. Ann Trop Med Parasitol 92 (1998) 525-537
    • (1998) Ann Trop Med Parasitol , vol.92 , pp. 525-537
    • Camacho, L.H.1    Gordeuk, V.R.2    Wilairatana, P.3
  • 3
    • 0031923047 scopus 로고    scopus 로고
    • Short report: gnathostomiasis in Mexico
    • Ogata K., Nawa Y., Akahane H., et al. Short report: gnathostomiasis in Mexico. Am J Trop Med Hyg 58 (1998) 316-318
    • (1998) Am J Trop Med Hyg , vol.58 , pp. 316-318
    • Ogata, K.1    Nawa, Y.2    Akahane, H.3
  • 5
    • 0014128418 scopus 로고
    • Fatal eosinophilic encephalomyelitis caused by the nematode Gnathostoma spinigerum
    • Chitanondh H., and Rosen L. Fatal eosinophilic encephalomyelitis caused by the nematode Gnathostoma spinigerum. Am J Trop Med Hyg 16 (1967) 638-645
    • (1967) Am J Trop Med Hyg , vol.16 , pp. 638-645
    • Chitanondh, H.1    Rosen, L.2
  • 6
    • 0020511516 scopus 로고
    • Eosinophilic meningoradiculomyelitis caused by Gnathostoma spinigerum. A case report
    • Kawamura J., Kohri Y., and Oka N. Eosinophilic meningoradiculomyelitis caused by Gnathostoma spinigerum. A case report. Arch Neurol 40 (1983) 583-585
    • (1983) Arch Neurol , vol.40 , pp. 583-585
    • Kawamura, J.1    Kohri, Y.2    Oka, N.3
  • 7
    • 0014393804 scopus 로고
    • Two fatal cases of eosinophilic myeloencephalitis a newly recognized disease caused by Gnathostoma spinigerum
    • Punyagupta S., Juttijudata P., Bunnag T., et al. Two fatal cases of eosinophilic myeloencephalitis a newly recognized disease caused by Gnathostoma spinigerum. Trans R Soc Trop Med Hyg 62 (1968) 801-809
    • (1968) Trans R Soc Trop Med Hyg , vol.62 , pp. 801-809
    • Punyagupta, S.1    Juttijudata, P.2    Bunnag, T.3
  • 8
    • 0030900627 scopus 로고    scopus 로고
    • Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components
    • Berasain P., Goni F., McGonigle S., et al. Proteinases secreted by Fasciola hepatica degrade extracellular matrix and basement membrane components. J Parasitol 83 (1997) 1-5
    • (1997) J Parasitol , vol.83 , pp. 1-5
    • Berasain, P.1    Goni, F.2    McGonigle, S.3
  • 9
    • 0025607058 scopus 로고
    • Metalloproteases of infective Ancylostoma hookworm larvae and their possible functions in tissue invasion and ecdysis
    • Hotez P., Haggerty J., Hawdon J., et al. Metalloproteases of infective Ancylostoma hookworm larvae and their possible functions in tissue invasion and ecdysis. Infect Immun 58 (1990) 3883-3892
    • (1990) Infect Immun , vol.58 , pp. 3883-3892
    • Hotez, P.1    Haggerty, J.2    Hawdon, J.3
  • 11
    • 0022536606 scopus 로고
    • Schistosoma mansoni: proteinase activity of "hemoglobinase" from the digestive tract of adult worms
    • Chappell C.L., and Dresden M.H. Schistosoma mansoni: proteinase activity of "hemoglobinase" from the digestive tract of adult worms. Exp Parasitol 61 (1986) 160-167
    • (1986) Exp Parasitol , vol.61 , pp. 160-167
    • Chappell, C.L.1    Dresden, M.H.2
  • 12
    • 0035951780 scopus 로고    scopus 로고
    • Cathepsin B-like cysteine proteases confer intestinal cysteine protease activity in Haemonchus contortus
    • Shompole S., and Jasmer D.P. Cathepsin B-like cysteine proteases confer intestinal cysteine protease activity in Haemonchus contortus. J Biol Chem 276 (2001) 2928-2934
    • (2001) J Biol Chem , vol.276 , pp. 2928-2934
    • Shompole, S.1    Jasmer, D.P.2
  • 13
    • 0033995763 scopus 로고    scopus 로고
    • Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced
    • Berasain P., Carmona C., Frangione B., et al. Fasciola hepatica: parasite-secreted proteinases degrade all human IgG subclasses: determination of the specific cleavage sites and identification of the immunoglobulin fragments produced. Exp Parasitol 94 (2000) 99-110
    • (2000) Exp Parasitol , vol.94 , pp. 99-110
    • Berasain, P.1    Carmona, C.2    Frangione, B.3
  • 14
    • 0027375061 scopus 로고
    • Cathepsin L proteinase secreted by Fasciola hepatica in vitro prevents antibody-mediated eosinophil attachment to newly excysted juveniles
    • Carmona C., Dowd A.J., Smith A.M., et al. Cathepsin L proteinase secreted by Fasciola hepatica in vitro prevents antibody-mediated eosinophil attachment to newly excysted juveniles. Mol Biochem Parasitol 62 (1993) 9-17
    • (1993) Mol Biochem Parasitol , vol.62 , pp. 9-17
    • Carmona, C.1    Dowd, A.J.2    Smith, A.M.3
  • 15
    • 0020368625 scopus 로고
    • Proteolytic cleavage of immunoglobulin by enzymes released by Fasciola hepatica
    • Chapman C.B., and Mitchell G.F. Proteolytic cleavage of immunoglobulin by enzymes released by Fasciola hepatica. Vet Parasitol 11 (1982) 165-178
    • (1982) Vet Parasitol , vol.11 , pp. 165-178
    • Chapman, C.B.1    Mitchell, G.F.2
  • 16
    • 0027943101 scopus 로고
    • Cleavage of immunoglobulin G by excretory-secretory cathepsin S-like protease of Spirometra mansoni plerocercoid
    • Kong Y., Chung Y.B., Cho S.Y., et al. Cleavage of immunoglobulin G by excretory-secretory cathepsin S-like protease of Spirometra mansoni plerocercoid. Parasitology 109 Pt 5 (1994) 611-621
    • (1994) Parasitology , vol.109 , Issue.PART 5 , pp. 611-621
    • Kong, Y.1    Chung, Y.B.2    Cho, S.Y.3
  • 17
    • 2942538289 scopus 로고    scopus 로고
    • A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling
    • Guiliano D.B., Hong X., McKerrow J.H., et al. A gene family of cathepsin L-like proteases of filarial nematodes are associated with larval molting and cuticle and eggshell remodeling. Mol Biochem Parasitol 136 (2004) 227-242
    • (2004) Mol Biochem Parasitol , vol.136 , pp. 227-242
    • Guiliano, D.B.1    Hong, X.2    McKerrow, J.H.3
  • 18
    • 0029973555 scopus 로고    scopus 로고
    • Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae
    • Lustigman S., McKerrow J.H., Shah K., et al. Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae. J Biol Chem 271 (1996) 30181-30189
    • (1996) J Biol Chem , vol.271 , pp. 30181-30189
    • Lustigman, S.1    McKerrow, J.H.2    Shah, K.3
  • 19
    • 0033004539 scopus 로고    scopus 로고
    • Proteinases and associated genes of parasitic helminths
    • Tort J., Brindley P.J., Knox D., et al. Proteinases and associated genes of parasitic helminths. Adv Parasitol 43 (1999) 161-266
    • (1999) Adv Parasitol , vol.43 , pp. 161-266
    • Tort, J.1    Brindley, P.J.2    Knox, D.3
  • 20
    • 0034896063 scopus 로고    scopus 로고
    • Molecular cloning of a gene encoding matrix metalloproteinase-like protein from Gnathostoma spinigerum
    • Uparanukraw P., Morakote N., Harnnoi T., et al. Molecular cloning of a gene encoding matrix metalloproteinase-like protein from Gnathostoma spinigerum. Parasitol Res 87 (2001) 751-757
    • (2001) Parasitol Res , vol.87 , pp. 751-757
    • Uparanukraw, P.1    Morakote, N.2    Harnnoi, T.3
  • 21
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine proteases of parasitic organisms
    • Sajid M., and McKerrow J.H. Cysteine proteases of parasitic organisms. Mol Biochem Parasitol 120 (2002) 1-21
    • (2002) Mol Biochem Parasitol , vol.120 , pp. 1-21
    • Sajid, M.1    McKerrow, J.H.2
  • 22
    • 0028825753 scopus 로고
    • Gnathostoma spinigerum: growth and development of third-stage larvae in vitro
    • Maleewong W., Intapan P.M., Khempila J., et al. Gnathostoma spinigerum: growth and development of third-stage larvae in vitro. J Parasitol 81 (1995) 800-803
    • (1995) J Parasitol , vol.81 , pp. 800-803
    • Maleewong, W.1    Intapan, P.M.2    Khempila, J.3
  • 24
    • 0040922445 scopus 로고
    • Serine proteases from nematode and protozoan parasites: isolation of sequence homologs using generic molecular probes
    • Sakanari J.A., Staunton C.E., Eakin A.E., et al. Serine proteases from nematode and protozoan parasites: isolation of sequence homologs using generic molecular probes. Proc Natl Acad Sci USA 86 (1989) 4863-4867
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4863-4867
    • Sakanari, J.A.1    Staunton, C.E.2    Eakin, A.E.3
  • 25
    • 0030801002 scopus 로고    scopus 로고
    • Gapped BLAST and PSI-BLAST: a new generation of protein database search programs
    • Altschul S.F., Madden T.L., Schaffer A.A., et al. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucl Acids Res 25 (1997) 3389-3402
    • (1997) Nucl Acids Res , vol.25 , pp. 3389-3402
    • Altschul, S.F.1    Madden, T.L.2    Schaffer, A.A.3
  • 26
    • 3042521098 scopus 로고    scopus 로고
    • Improved prediction of signal peptides: SignalP 3.0
    • Bendtsen J.D., Nielsen H., von H.G., et al. Improved prediction of signal peptides: SignalP 3.0. J Mol Biol 340 (2004) 783-795
    • (2004) J Mol Biol , vol.340 , pp. 783-795
    • Bendtsen, J.D.1    Nielsen, H.2    von, H.G.3
  • 27
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22 (1994) 4673-4680
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 28
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., et al. MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24 (2007) 1596-1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3
  • 29
    • 0027521381 scopus 로고
    • The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences
    • Bjellqvist B., Hughes G.J., Pasquali C., et al. The focusing positions of polypeptides in immobilized pH gradients can be predicted from their amino acid sequences. Electrophoresis 14 (1993) 1023-1031
    • (1993) Electrophoresis , vol.14 , pp. 1023-1031
    • Bjellqvist, B.1    Hughes, G.J.2    Pasquali, C.3
  • 30
    • 33744961634 scopus 로고    scopus 로고
    • Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities
    • Choe Y., Leonetti F., Greenbaum D.C., et al. Substrate profiling of cysteine proteases using a combinatorial peptide library identifies functionally unique specificities. J Biol Chem 281 (2006) 12824-12832
    • (2006) J Biol Chem , vol.281 , pp. 12824-12832
    • Choe, Y.1    Leonetti, F.2    Greenbaum, D.C.3
  • 31
    • 0034608931 scopus 로고    scopus 로고
    • Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries
    • Harris J.L., Backes B.J., Leonetti F., et al. Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries. Proc Natl Acad Sci USA 97 (2000) 7754-7759
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 7754-7759
    • Harris, J.L.1    Backes, B.J.2    Leonetti, F.3
  • 32
    • 0027052982 scopus 로고
    • pGSTag-a versatile bacterial expression plasmid for enzymatic labeling of recombinant proteins
    • Ron D., and Dressler H. pGSTag-a versatile bacterial expression plasmid for enzymatic labeling of recombinant proteins. Biotechniques 13 (1992) 866-869
    • (1992) Biotechniques , vol.13 , pp. 866-869
    • Ron, D.1    Dressler, H.2
  • 33
    • 0024675021 scopus 로고
    • Anatomical localization of Gnathostoma spinigerum larval antigens by an indirect fluorescent antibody test
    • Morakote N., Nateewatana N., Maleewong W., et al. Anatomical localization of Gnathostoma spinigerum larval antigens by an indirect fluorescent antibody test. Southeast Asian J Trop Med Public Health 20 (1989) 291-295
    • (1989) Southeast Asian J Trop Med Public Health , vol.20 , pp. 291-295
    • Morakote, N.1    Nateewatana, N.2    Maleewong, W.3
  • 34
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Peiffer S.L., and DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc Natl Acad Sci USA 90 (1993) 3063-3067
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 35
    • 0028905069 scopus 로고
    • Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing
    • Vernet T., Berti P.J., de M.C., et al. Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. J Biol Chem 270 (1995) 10838-10846
    • (1995) J Biol Chem , vol.270 , pp. 10838-10846
    • Vernet, T.1    Berti, P.J.2    de, M.C.3
  • 36
    • 0036072851 scopus 로고    scopus 로고
    • A cathepsin L protease essential for Caenorhabditis elegans embryogenesis is functionally conserved in parasitic nematodes
    • Britton C., and Murray L. A cathepsin L protease essential for Caenorhabditis elegans embryogenesis is functionally conserved in parasitic nematodes. Mol Biochem Parasitol 122 (2002) 21-33
    • (2002) Mol Biochem Parasitol , vol.122 , pp. 21-33
    • Britton, C.1    Murray, L.2
  • 37
    • 0021782839 scopus 로고
    • Cathepsin L-a lysosomal cysteine proteinase
    • Kirschke H., and Barrett A.J. Cathepsin L-a lysosomal cysteine proteinase. Prog Clin Biol Res 180 (1985) 61-69
    • (1985) Prog Clin Biol Res , vol.180 , pp. 61-69
    • Kirschke, H.1    Barrett, A.J.2
  • 38
    • 0028309017 scopus 로고
    • The proregion of cathepsin L is required for proper folding, stability, and ER exit
    • Tao K., Stearns N.A., Dong J., et al. The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch Biochem Biophys 311 (1994) 19-27
    • (1994) Arch Biochem Biophys , vol.311 , pp. 19-27
    • Tao, K.1    Stearns, N.A.2    Dong, J.3
  • 39
    • 0028944193 scopus 로고
    • Recombinant pro-regions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes
    • Taylor M.A., Baker K.C., Briggs G.S., et al. Recombinant pro-regions from papain and papaya proteinase IV are selective high affinity inhibitors of the mature papaya enzymes. Protein Eng 8 (1995) 59-62
    • (1995) Protein Eng , vol.8 , pp. 59-62
    • Taylor, M.A.1    Baker, K.C.2    Briggs, G.S.3
  • 40
    • 0035996748 scopus 로고    scopus 로고
    • Recombinant expression and purification of an enzymatically active cysteine proteinase of the protozoan parasite Entamoeba histolytica
    • Hellberg A., Nowak N., Leippe M., et al. Recombinant expression and purification of an enzymatically active cysteine proteinase of the protozoan parasite Entamoeba histolytica. Protein Expr Purif 24 (2002) 131-137
    • (2002) Protein Expr Purif , vol.24 , pp. 131-137
    • Hellberg, A.1    Nowak, N.2    Leippe, M.3
  • 42
    • 0024331466 scopus 로고
    • Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli
    • Smith S.M., and Gottesman M.M. Activity and deletion analysis of recombinant human cathepsin L expressed in Escherichia coli. J Biol Chem 264 (1989) 20487-20495
    • (1989) J Biol Chem , vol.264 , pp. 20487-20495
    • Smith, S.M.1    Gottesman, M.M.2
  • 43
    • 0036072703 scopus 로고    scopus 로고
    • Characterisation and expression of the Fasciola gigantica cathepsin L gene
    • Yamasaki H., Mineki R., Murayama K., et al. Characterisation and expression of the Fasciola gigantica cathepsin L gene. Int J Parasitol 32 (2002) 1031-1042
    • (2002) Int J Parasitol , vol.32 , pp. 1031-1042
    • Yamasaki, H.1    Mineki, R.2    Murayama, K.3
  • 44
    • 0037197769 scopus 로고    scopus 로고
    • Substrate specificity of schistosome versus human legumain determined by P1-P3 peptide libraries
    • Mathieu M.A., Bogyo M., Caffrey C.R., et al. Substrate specificity of schistosome versus human legumain determined by P1-P3 peptide libraries. Mol Biochem Parasitol 121 (2002) 99-105
    • (2002) Mol Biochem Parasitol , vol.121 , pp. 99-105
    • Mathieu, M.A.1    Bogyo, M.2    Caffrey, C.R.3
  • 45
    • 0036479227 scopus 로고    scopus 로고
    • Cathepsin L is essential for embryogenesis and development of Caenorhabditis elegans
    • Hashmi S., Britton C., Liu J., et al. Cathepsin L is essential for embryogenesis and development of Caenorhabditis elegans. J Biol Chem 277 (2002) 3477-3486
    • (2002) J Biol Chem , vol.277 , pp. 3477-3486
    • Hashmi, S.1    Britton, C.2    Liu, J.3
  • 46
    • 0032945715 scopus 로고    scopus 로고
    • Recombinant expression and localization of Schistosoma mansoni cathepsin L1 support its role in the degradation of host hemoglobin
    • Brady C.P., Dowd A.J., Brindley P.J., et al. Recombinant expression and localization of Schistosoma mansoni cathepsin L1 support its role in the degradation of host hemoglobin. Infect Immun 67 (1999) 368-374
    • (1999) Infect Immun , vol.67 , pp. 368-374
    • Brady, C.P.1    Dowd, A.J.2    Brindley, P.J.3
  • 47
    • 12344273618 scopus 로고    scopus 로고
    • Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum
    • Dahl E.L., and Rosenthal P.J. Biosynthesis, localization, and processing of falcipain cysteine proteases of Plasmodium falciparum. Mol Biochem Parasitol 139 (2005) 205-212
    • (2005) Mol Biochem Parasitol , vol.139 , pp. 205-212
    • Dahl, E.L.1    Rosenthal, P.J.2


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