메뉴 건너뛰기




Volumn 156, Issue 2, 2007, Pages 191-198

Cloning, site-directed mutagenesis and expression of cathepsin L-like cysteine protease from Uronema marinum (Ciliophora: Scuticociliatida)

Author keywords

Cathepsin L; Ciliate; Cysteine protease; Scuticociliate; Site directed mutagenesis; Uronema marinum

Indexed keywords

CATHEPSIN L; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; LEUPEPTIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; POLYCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 35348932095     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2007.07.021     Document Type: Article
Times cited : (13)

References (35)
  • 1
    • 3042875205 scopus 로고
    • Isolation and in vitro cultivation of an unidentified ciliate causing scuticociliatosis in Japanese flounder (Paralichthys olivaceus)
    • Yoshinaga T., and Nakazoe J. Isolation and in vitro cultivation of an unidentified ciliate causing scuticociliatosis in Japanese flounder (Paralichthys olivaceus). Gyobyo Kenkyu 28 (1993) 131-134
    • (1993) Gyobyo Kenkyu , vol.28 , pp. 131-134
    • Yoshinaga, T.1    Nakazoe, J.2
  • 2
    • 0034127125 scopus 로고    scopus 로고
    • Systemic infection with Uronema-like ciliates in farmed turbot Scophtalmus maximus (L.)
    • Sterud E., Hansen M.K., and Mo T.A. Systemic infection with Uronema-like ciliates in farmed turbot Scophtalmus maximus (L.). J Fish Dis 23 (2000) 33-37
    • (2000) J Fish Dis , vol.23 , pp. 33-37
    • Sterud, E.1    Hansen, M.K.2    Mo, T.A.3
  • 3
    • 0035969109 scopus 로고    scopus 로고
    • Morphology and biology of parasite responsible for scuticociliatosis of cultured olive flounder Paralichthys olivaceus
    • Jee B.Y., Kim Y.C., and Park M.S. Morphology and biology of parasite responsible for scuticociliatosis of cultured olive flounder Paralichthys olivaceus. Dis Aquat Org 47 (2001) 49-55
    • (2001) Dis Aquat Org , vol.47 , pp. 49-55
    • Jee, B.Y.1    Kim, Y.C.2    Park, M.S.3
  • 4
    • 26844507495 scopus 로고    scopus 로고
    • Protease in cell lysate of Uronema marinum (Ciliata: Scuticociliatida), an opportunistic pathogen of cultured olive flounder (Paralichthys olivaceus)
    • Kwon S.R., Kim C.S., Ahn K.J., et al. Protease in cell lysate of Uronema marinum (Ciliata: Scuticociliatida), an opportunistic pathogen of cultured olive flounder (Paralichthys olivaceus). J Fish Sci Tech 5 (2002) 145-149
    • (2002) J Fish Sci Tech , vol.5 , pp. 145-149
    • Kwon, S.R.1    Kim, C.S.2    Ahn, K.J.3
  • 5
    • 0035936577 scopus 로고    scopus 로고
    • The molecular basis of nuclear genetic code change in ciliates
    • Lozupone C.A., Knight R.D., and Landweber L.F. The molecular basis of nuclear genetic code change in ciliates. Curr Biol 11 (2001) 65-74
    • (2001) Curr Biol , vol.11 , pp. 65-74
    • Lozupone, C.A.1    Knight, R.D.2    Landweber, L.F.3
  • 6
    • 0028231010 scopus 로고
    • The DNA of ciliated protozoa
    • Prescott D.M. The DNA of ciliated protozoa. Microbiol Rev 58 (1994) 233-267
    • (1994) Microbiol Rev , vol.58 , pp. 233-267
    • Prescott, D.M.1
  • 7
    • 0037123363 scopus 로고    scopus 로고
    • The use of synthetic genes for the expression of ciliate proteins in heterologous systems
    • Lin Y., Cheng G., Wang X., and Clark T.G. The use of synthetic genes for the expression of ciliate proteins in heterologous systems. Gene 288 (2002) 85-94
    • (2002) Gene , vol.288 , pp. 85-94
    • Lin, Y.1    Cheng, G.2    Wang, X.3    Clark, T.G.4
  • 8
    • 0024596636 scopus 로고
    • Parasite proteinases
    • McKerrow J.H. Parasite proteinases. Exp Parasitol 68 (1989) 111-115
    • (1989) Exp Parasitol , vol.68 , pp. 111-115
    • McKerrow, J.H.1
  • 9
    • 0036882393 scopus 로고    scopus 로고
    • Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design
    • Lecaille F., Kaleta J., and Bromme D. Human and parasitic papain-like cysteine proteases: their role in physiology and pathology and recent developments in inhibitor design. Chem Rev 102 (2002) 4459-4488
    • (2002) Chem Rev , vol.102 , pp. 4459-4488
    • Lecaille, F.1    Kaleta, J.2    Bromme, D.3
  • 10
    • 0036178381 scopus 로고    scopus 로고
    • Cysteine protease of parasitic organisms
    • Sajid M., and McKerrow J.H. Cysteine protease 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
  • 11
    • 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., and Dalton J.P. Cathepsin L proteinase secreted by Fasciola hepatica in vitro prevents antibody mediated eosinophil attachment to newly excysted juveniles. Mol Biochem Parasitol 62 (1993) 9-18
    • (1993) Mol Biochem Parasitol , vol.62 , pp. 9-18
    • Carmona, C.1    Dowd, A.J.2    Smith, A.M.3    Dalton, J.P.4
  • 12
    • 0027715975 scopus 로고
    • Fasciola hepatica: a secreted cathepsin L-like proteinase cleaves host immunoglobulin
    • Smith A.M., Dowd A.J., Heffernan M., Robertson C.D., and Dalton J.P. Fasciola hepatica: a secreted cathepsin L-like proteinase cleaves host immunoglobulin. Int J Parasitol 23 (1993) 977-983
    • (1993) Int J Parasitol , vol.23 , pp. 977-983
    • Smith, A.M.1    Dowd, A.J.2    Heffernan, M.3    Robertson, C.D.4    Dalton, J.P.5
  • 13
    • 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
  • 14
    • 2542426758 scopus 로고    scopus 로고
    • Cysteine protease activities in the fish pathogen Philasterides dicentrarchi (Ciliophora: Scuticociliatida)
    • Paramá A., Iglesias R., Álvarez M.F., Leiro J., Ubeira F.M., and Sanmartín M.L. Cysteine protease activities in the fish pathogen Philasterides dicentrarchi (Ciliophora: Scuticociliatida). Parasitology 128 (2004) 541-548
    • (2004) Parasitology , vol.128 , pp. 541-548
    • Paramá, A.1    Iglesias, R.2    Álvarez, M.F.3    Leiro, J.4    Ubeira, F.M.5    Sanmartín, M.L.6
  • 15
    • 0033034097 scopus 로고    scopus 로고
    • Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep
    • Piacenza L., Acosta D., Basmadjian I., Dalton J.P., and Carmoma C. Vaccination with cathepsin L proteinases and with leucine aminopeptidase induces high levels of protection against fascioliasis in sheep. Infect Immun 67 (1999) 1954-1961
    • (1999) Infect Immun , vol.67 , pp. 1954-1961
    • Piacenza, L.1    Acosta, D.2    Basmadjian, I.3    Dalton, J.P.4    Carmoma, C.5
  • 16
    • 0043282646 scopus 로고    scopus 로고
    • Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines
    • Dalton J.P., Neill S.O., Stack C., et al. Fasciola hepatica cathepsin L-like proteases: biology, function, and potential in the development of first generation liver fluke vaccines. Int J Parasitol 33 (2003) 1173-1181
    • (2003) Int J Parasitol , vol.33 , pp. 1173-1181
    • Dalton, J.P.1    Neill, S.O.2    Stack, C.3
  • 17
    • 12244294771 scopus 로고    scopus 로고
    • Pseudocohnilembus persalinus (Ciliophora: Scuticociitida) is an additional causing species of scuticociliatosis in olive flounder Paralichthys olivaceus
    • Kim S.M., Cho J.B., Lee E.H., et al. Pseudocohnilembus persalinus (Ciliophora: Scuticociitida) is an additional causing species of scuticociliatosis in olive flounder Paralichthys olivaceus. Dis Aquat Org 62 (2004) 239-244
    • (2004) Dis Aquat Org , vol.62 , pp. 239-244
    • Kim, S.M.1    Cho, J.B.2    Lee, E.H.3
  • 18
    • 15544389775 scopus 로고    scopus 로고
    • Uronema marinum: identification and biochemical characterization of phosphatidylcholine-hydrolyzing phospholipase C
    • Seo J.S., Kim M.S., Lee S.H., et al. Uronema marinum: identification and biochemical characterization of phosphatidylcholine-hydrolyzing phospholipase C. Exp Parasitol 110 (2005) 22-29
    • (2005) Exp Parasitol , vol.110 , pp. 22-29
    • Seo, J.S.1    Kim, M.S.2    Lee, S.H.3
  • 19
    • 26844545933 scopus 로고    scopus 로고
    • Molecular cloning and characterization of Cathepsin B from a scuticociliate Uronema marinum
    • Lim S.U., Seo J.S., Kim M.S., et al. Molecular cloning and characterization of Cathepsin B from a scuticociliate Uronema marinum. Comp Biochem Physiol B Biochem Mol Biol 142 (2005) 283-292
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.142 , pp. 283-292
    • Lim, S.U.1    Seo, J.S.2    Kim, M.S.3
  • 20
    • 0037098946 scopus 로고    scopus 로고
    • Site-directed mutagenesis by the megaprimer PCR method: variations on a theme for simultaneous introduction of multiple mutations
    • Angelaccio S., and Bonaccorsi di Patti M.C. Site-directed mutagenesis by the megaprimer PCR method: variations on a theme for simultaneous introduction of multiple mutations. Anal Biochem 306 (2002) 346-349
    • (2002) Anal Biochem , vol.306 , pp. 346-349
    • Angelaccio, S.1    Bonaccorsi di Patti, M.C.2
  • 21
    • 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
  • 22
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucleic Acids Symp 41 (1999) 95-98
    • (1999) Nucleic Acids Symp , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 23
    • 3242810318 scopus 로고    scopus 로고
    • MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment
    • Kumar S., Tamura K., and Nei M. MEGA3: integrated software for molecular evolutionary genetics analysis and sequence alignment. Brief Bioinform 5 (2004) 150-163
    • (2004) Brief Bioinform , vol.5 , pp. 150-163
    • Kumar, S.1    Tamura, K.2    Nei, M.3
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0019765848 scopus 로고
    • Cathepsin B, Cathepsin H, and cathepsin L
    • Barrett A.J., and Kirschke H. Cathepsin B, Cathepsin H, and cathepsin L. Methods Enzymol 80 (1981) 535-561
    • (1981) Methods Enzymol , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 26
    • 33846233481 scopus 로고    scopus 로고
    • Production and characterization of polyclonal antibody against recombinant ORF 049L of rock bream (Oplegnathus fasciatus) iridovirus
    • Kim Y.I., Ha Y.M., Ahn S.J., Nam Y.K., Kim K.H., and Kim S.K. Production and characterization of polyclonal antibody against recombinant ORF 049L of rock bream (Oplegnathus fasciatus) iridovirus. Process Biochem 42 (2007) 134-140
    • (2007) Process Biochem , vol.42 , pp. 134-140
    • Kim, Y.I.1    Ha, Y.M.2    Ahn, S.J.3    Nam, Y.K.4    Kim, K.H.5    Kim, S.K.6
  • 27
    • 0020770479 scopus 로고
    • Patterns of amino acids near signal-sequence cleavage sites
    • Von Heijne G. Patterns of amino acids near signal-sequence cleavage sites. Eur J Biochem 133 (1983) 17-21
    • (1983) Eur J Biochem , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 28
    • 0028673327 scopus 로고
    • Families of cysteine peptidases
    • Rawlings N.D., and Barret A.J. Families of cysteine peptidases. Methods Enzymol 244 (1994) 461-486
    • (1994) Methods Enzymol , vol.244 , pp. 461-486
    • Rawlings, N.D.1    Barret, A.J.2
  • 29
    • 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
  • 30
    • 0028905069 scopus 로고
    • Processing of the papain precursor
    • Vernet T., Berti P.J., Montigny C., et al. Processing of the papain precursor. J Biol Chem 270 (1995) 10838-10846
    • (1995) J Biol Chem , vol.270 , pp. 10838-10846
    • Vernet, T.1    Berti, P.J.2    Montigny, C.3
  • 31
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: more than scavengers
    • Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta 1477 (2000) 98-111
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 32
    • 0031574019 scopus 로고    scopus 로고
    • Approaches to DNA mutagenesis: an overview
    • Ling M.M., and Robinson B.H. Approaches to DNA mutagenesis: an overview. Anal Biochem 254 (1997) 157-178
    • (1997) Anal Biochem , vol.254 , pp. 157-178
    • Ling, M.M.1    Robinson, B.H.2
  • 33
    • 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., Tannich E., and Bruchhaus I. Recombinant expression and purification of an enzymatically active cysteine proteinase of the protozoan parasite Entamoeba histolytica. Protein Exp Purif 24 (2002) 131-137
    • (2002) Protein Exp Purif , vol.24 , pp. 131-137
    • Hellberg, A.1    Nowak, N.2    Leippe, M.3    Tannich, E.4    Bruchhaus, I.5
  • 34
    • 0033808652 scopus 로고    scopus 로고
    • Cloning and functional expression of a Boophilus microplus cathepsin L-like enzyme
    • Renard G., Garcia J.F., Cardoso F.C., et al. Cloning and functional expression of a Boophilus microplus cathepsin L-like enzyme. Insect Biochem Mol Biol 30 (2000) 1017-1026
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 1017-1026
    • Renard, G.1    Garcia, J.F.2    Cardoso, F.C.3
  • 35
    • 0036072703 scopus 로고    scopus 로고
    • Characterization and expression of the Fasciola gigantica cathepsin L gene
    • Yamasaki H., Mineki R., Murayama F., Ito A., and Aoki T. Characterization 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, F.3    Ito, A.4    Aoki, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.