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Volumn 13, Issue 1, 2014, Pages

The naturally competent strain Streptococcus thermophilus LMD-9 as a new tool to anchor heterologous proteins on the cell surface

Author keywords

Cell envelope proteinase (CEP); Cell wall anchored protein; Heterologous expression; Lactobacillus helveticus CNRZ32 CIRM BIA 103; PrtH; PrtS; Secretion; Streptococcus thermophilus LMD 9

Indexed keywords

BACTERIAL PROTEIN; CELL ENVELOPE PROTEINASE; PROTEINASE; UNCLASSIFIED DRUG;

EID: 84903585789     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-13-82     Document Type: Article
Times cited : (20)

References (49)
  • 3
    • 8844278305 scopus 로고    scopus 로고
    • Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism
    • Westers L, Westers H, Quax WJ. Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism. Biochim Biophys Acta-Mol Cell Res 2004, 1694:299-310.
    • (2004) Biochim Biophys Acta-Mol Cell Res , vol.1694 , pp. 299-310
    • Westers, L.1    Westers, H.2    Quax, W.J.3
  • 5
    • 78549296762 scopus 로고    scopus 로고
    • LAB-Secretome: a genome-scale comparative analysis of the predicted extracellular and surface-associated proteins of Lactic Acid Bacteria
    • Zhou MM, Theunissen D, Wels M, Siezen RJ. LAB-Secretome: a genome-scale comparative analysis of the predicted extracellular and surface-associated proteins of Lactic Acid Bacteria. BMC Genomics 2010, 11:651.
    • (2010) BMC Genomics , vol.11 , pp. 651
    • Zhou, M.M.1    Theunissen, D.2    Wels, M.3    Siezen, R.J.4
  • 6
    • 33645009654 scopus 로고    scopus 로고
    • Conservation of key elements of natural competence in Lactococcus lactis ssp
    • Wydau S, Dervyn R, Anba J, Ehrlich SD, Maguin E. Conservation of key elements of natural competence in Lactococcus lactis ssp. FEMS Microbiol Lett 2006, 257:32-42.
    • (2006) FEMS Microbiol Lett , vol.257 , pp. 32-42
    • Wydau, S.1    Dervyn, R.2    Anba, J.3    Ehrlich, S.D.4    Maguin, E.5
  • 7
    • 36849090593 scopus 로고    scopus 로고
    • Natural genetic transformation: prevalence, mechanisms and function
    • Johnsborg O, Eldholm V, Havarstein LS. Natural genetic transformation: prevalence, mechanisms and function. Res Microbiol 2007, 158:767-778.
    • (2007) Res Microbiol , vol.158 , pp. 767-778
    • Johnsborg, O.1    Eldholm, V.2    Havarstein, L.S.3
  • 9
    • 23944492123 scopus 로고    scopus 로고
    • Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus survive gastrointestinal transit of healthy volunteers consuming yogurt
    • Mater DDG, Bretigny L, Firmesse O, Flores MJ, Mogenet A, Bresson JL, Corthier G. Streptococcus thermophilus and Lactobacillus delbrueckii subsp. bulgaricus survive gastrointestinal transit of healthy volunteers consuming yogurt. FEMS Microbiol Lett 2005, 250:185-187.
    • (2005) FEMS Microbiol Lett , vol.250 , pp. 185-187
    • Mater, D.D.G.1    Bretigny, L.2    Firmesse, O.3    Flores, M.J.4    Mogenet, A.5    Bresson, J.L.6    Corthier, G.7
  • 11
    • 0031449016 scopus 로고    scopus 로고
    • Construction of a green-fluorescent protein-based, insertion-inactivation shuttle vector for lactic acid bacteria and Escherichia coli
    • Solaiman DKY, Somkuti GA. Construction of a green-fluorescent protein-based, insertion-inactivation shuttle vector for lactic acid bacteria and Escherichia coli. Biotechnol Lett 1997, 19:1175-1179.
    • (1997) Biotechnol Lett , vol.19 , pp. 1175-1179
    • Solaiman, D.K.Y.1    Somkuti, G.A.2
  • 12
    • 0026146554 scopus 로고
    • Transfer and expression of A streptomyces cholesterol oxidase gene in Streptococcus thermophilus
    • Somkuti GA, Solaiman DKY, Johnson TL, Steinberg DH. Transfer and expression of A streptomyces cholesterol oxidase gene in Streptococcus thermophilus. Biotechnol Appl Biochem 1991, 13:238-245.
    • (1991) Biotechnol Appl Biochem , vol.13 , pp. 238-245
    • Somkuti, G.A.1    Solaiman, D.K.Y.2    Johnson, T.L.3    Steinberg, D.H.4
  • 13
    • 84856514476 scopus 로고    scopus 로고
    • Vector-mediated chromosomal integration of the glutamate decarboxylase gene in Streptococcus thermophilus
    • Renye JA, Somkuti GA. Vector-mediated chromosomal integration of the glutamate decarboxylase gene in Streptococcus thermophilus. Biotechnol Lett 2012, 34:549-555.
    • (2012) Biotechnol Lett , vol.34 , pp. 549-555
    • Renye, J.A.1    Somkuti, G.A.2
  • 14
    • 33750052593 scopus 로고    scopus 로고
    • Natural genetic transformation: a novel tool for efficient genetic engineering of the dairy bacterium Streptococcus thermophilus
    • Blomqvist T, Steinmoen H, Havarstein LS. Natural genetic transformation: a novel tool for efficient genetic engineering of the dairy bacterium Streptococcus thermophilus. Appl Environ Microbiol 2006, 72:6751-6756.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 6751-6756
    • Blomqvist, T.1    Steinmoen, H.2    Havarstein, L.S.3
  • 15
    • 78650378430 scopus 로고    scopus 로고
    • Development of a versatile procedure based on natural transformation for marker-free targeted genetic modification in Streptococcus thermophilus
    • Fontaine L, Dandoy D, Boutry C, Delplace B, De Frahan MH, Fremaux C, Horvath P, Boyaval P, Hols P. Development of a versatile procedure based on natural transformation for marker-free targeted genetic modification in Streptococcus thermophilus. Appl Environ Microbiol 2010, 76:7870-7877.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 7870-7877
    • Fontaine, L.1    Dandoy, D.2    Boutry, C.3    Delplace, B.4    De Frahan, M.H.5    Fremaux, C.6    Horvath, P.7    Boyaval, P.8    Hols, P.9
  • 17
    • 77749279743 scopus 로고    scopus 로고
    • A novel pheromone quorum-sensing system controls the development of natural competence in Streptococcus thermophilus and Streptococcus salivarius
    • Fontaine L, Boutry C, De Frahan MH, Delplace B, Fremaux C, Horvath P, Boyaval P, Hols P. A novel pheromone quorum-sensing system controls the development of natural competence in Streptococcus thermophilus and Streptococcus salivarius. J Bacteriol 2010, 192:1444-1454.
    • (2010) J Bacteriol , vol.192 , pp. 1444-1454
    • Fontaine, L.1    Boutry, C.2    De Frahan, M.H.3    Delplace, B.4    Fremaux, C.5    Horvath, P.6    Boyaval, P.7    Hols, P.8
  • 18
    • 67650293862 scopus 로고    scopus 로고
    • The oligopeptide transport system is essential for the development of natural competence in Streptococcus thermophilus Strain LMD-9
    • Gardan R, Besset C, Guillot A, Gitton C, Monnet V. The oligopeptide transport system is essential for the development of natural competence in Streptococcus thermophilus Strain LMD-9. J Bacteriol 2009, 191:4647-4655.
    • (2009) J Bacteriol , vol.191 , pp. 4647-4655
    • Gardan, R.1    Besset, C.2    Guillot, A.3    Gitton, C.4    Monnet, V.5
  • 19
    • 80052190507 scopus 로고    scopus 로고
    • Specialized adaptation of a lactic acid bacterium to the milk environment: the comparative genomics of Streptococcus thermophilus LMD-9
    • Goh YJ, Goin C, O'Flaherty S, Altermann E, Hutkins R. Specialized adaptation of a lactic acid bacterium to the milk environment: the comparative genomics of Streptococcus thermophilus LMD-9. Microb Cell Fact 2011, 10(Suppl 1):S22.
    • (2011) Microb Cell Fact , vol.10 , Issue.SUPPL. 1
    • Goh, Y.J.1    Goin, C.2    O'Flaherty, S.3    Altermann, E.4    Hutkins, R.5
  • 21
    • 80052217785 scopus 로고    scopus 로고
    • The fast milk acidifying phenotype of Streptococcus thermophilus can be acquired by natural transformation of the genomic island encoding the cell-envelope proteinase PrtS
    • Dandoy D, Fremaux C, De Frahan MH, Horvath P, Boyaval P, Hols P, Fontaine L. The fast milk acidifying phenotype of Streptococcus thermophilus can be acquired by natural transformation of the genomic island encoding the cell-envelope proteinase PrtS. Microb Cell Fact 2011, 10(Suppl 1):S21.
    • (2011) Microb Cell Fact , vol.10 , Issue.SUPPL. 1
    • Dandoy, D.1    Fremaux, C.2    De Frahan, M.H.3    Horvath, P.4    Boyaval, P.5    Hols, P.6    Fontaine, L.7
  • 22
    • 79953062295 scopus 로고    scopus 로고
    • Original features of cell-envelope proteinases of Lactobacillus helveticus. A review
    • Sadat-Mekmene L, Genay M, Atlan D, Lortal S, Gagnaire V. Original features of cell-envelope proteinases of Lactobacillus helveticus. A review. Int J Food Microbiol 2011, 146:1-13.
    • (2011) Int J Food Microbiol , vol.146 , pp. 1-13
    • Sadat-Mekmene, L.1    Genay, M.2    Atlan, D.3    Lortal, S.4    Gagnaire, V.5
  • 24
    • 66249097755 scopus 로고    scopus 로고
    • PrtH2, not prtH, is the ubiquitous cell-wall proteinase gene in Lactobacillus helveticus
    • Genay M, Sadat L, Gagnaire V, Lortal S. prtH2, not prtH, is the ubiquitous cell-wall proteinase gene in Lactobacillus helveticus. Appl Environ Microbiol 2009, 75:3238-3249.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 3238-3249
    • Genay, M.1    Sadat, L.2    Gagnaire, V.3    Lortal, S.4
  • 25
    • 0033759602 scopus 로고    scopus 로고
    • Streptococcus thermophilus cell wall-anchored proteinase: release, purification and biochemical and genetic characterization
    • Fernandez-Espla MD, Garault P, Monnet V, Rul F. Streptococcus thermophilus cell wall-anchored proteinase: release, purification and biochemical and genetic characterization. Appl Environ Microbiol 2000, 66:4772-4778.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 4772-4778
    • Fernandez-Espla, M.D.1    Garault, P.2    Monnet, V.3    Rul, F.4
  • 26
    • 0032871626 scopus 로고    scopus 로고
    • Multi-domain, cell-envelope proteinases of lactic acid bacteria
    • Siezen RJ. Multi-domain, cell-envelope proteinases of lactic acid bacteria. Antonie Van Leeuwenhoek 1999, 76:139-155.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 139-155
    • Siezen, R.J.1
  • 27
    • 78149257874 scopus 로고    scopus 로고
    • Combined prediction of Tat and Sec signal peptides with hidden Markov models
    • Bagos PG, Nikolaou EP, Liakopoulos TD, Tsirigos KD. Combined prediction of Tat and Sec signal peptides with hidden Markov models. Bioinformatics 2010, 26:2811-2817.
    • (2010) Bioinformatics , vol.26 , pp. 2811-2817
    • Bagos, P.G.1    Nikolaou, E.P.2    Liakopoulos, T.D.3    Tsirigos, K.D.4
  • 28
    • 0032783298 scopus 로고    scopus 로고
    • Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32
    • Pederson JA, Mileski GJ, Weimer BC, Steele JL. Genetic characterization of a cell envelope-associated proteinase from Lactobacillus helveticus CNRZ32. J Bacteriol 1999, 181:4592-4597.
    • (1999) J Bacteriol , vol.181 , pp. 4592-4597
    • Pederson, J.A.1    Mileski, G.J.2    Weimer, B.C.3    Steele, J.L.4
  • 29
    • 0027514727 scopus 로고
    • Characterization of a cell envelope-associated proteinase activity from Streptococcus thermophilus H-strains
    • Shahbal S, Hemme D, Renault P. Characterization of a cell envelope-associated proteinase activity from Streptococcus thermophilus H-strains. Appl Environ Microbiol 1993, 59:177-182.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 177-182
    • Shahbal, S.1    Hemme, D.2    Renault, P.3
  • 30
  • 31
    • 26844559000 scopus 로고    scopus 로고
    • Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein
    • Ishihama Y, Oda Y, Tabata T, Sato T, Nagasu T, Rappsilber J, Mann M. Exponentially modified protein abundance index (emPAI) for estimation of absolute protein amount in proteomics by the number of sequenced peptides per protein. Mol Cell Proteomics 2005, 4:1265-1272.
    • (2005) Mol Cell Proteomics , vol.4 , pp. 1265-1272
    • Ishihama, Y.1    Oda, Y.2    Tabata, T.3    Sato, T.4    Nagasu, T.5    Rappsilber, J.6    Mann, M.7
  • 32
    • 0036674269 scopus 로고    scopus 로고
    • Large-scale proteomic analysis of the human splicesome
    • Rappsilber J, Ryder U, Lamond AI, Mann M. Large-scale proteomic analysis of the human splicesome. Genome Res 2002, 12:1231-1245.
    • (2002) Genome Res , vol.12 , pp. 1231-1245
    • Rappsilber, J.1    Ryder, U.2    Lamond, A.I.3    Mann, M.4
  • 34
    • 0015462556 scopus 로고
    • Peptidoglycan types of bacterial cell walls and their taxonomic implications
    • Schleifer KH, Kandler O. Peptidoglycan types of bacterial cell walls and their taxonomic implications. Bacteriol Rev 1972, 36:407-477.
    • (1972) Bacteriol Rev , vol.36 , pp. 407-477
    • Schleifer, K.H.1    Kandler, O.2
  • 36
    • 77952372626 scopus 로고    scopus 로고
    • Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control
    • Solis N, Larsen MR, Cordwell SJ. Improved accuracy of cell surface shaving proteomics in Staphylococcus aureus using a false-positive control. Proteomics 2010, 10:2037-2049.
    • (2010) Proteomics , vol.10 , pp. 2037-2049
    • Solis, N.1    Larsen, M.R.2    Cordwell, S.J.3
  • 37
    • 84862238853 scopus 로고    scopus 로고
    • Another turn of the screw in shaving Gram-positive bacteria: Optimization of proteomics surface protein identification in Streptococcus pneumoniae
    • Olaya-Abril A, Gomez-Gascon L, Jimenez-Munguia I, Obando I, Rodriguez-Ortega MJ. Another turn of the screw in shaving Gram-positive bacteria: Optimization of proteomics surface protein identification in Streptococcus pneumoniae. J Proteomics 2012, 75:3733-3746.
    • (2012) J Proteomics , vol.75 , pp. 3733-3746
    • Olaya-Abril, A.1    Gomez-Gascon, L.2    Jimenez-Munguia, I.3    Obando, I.4    Rodriguez-Ortega, M.J.5
  • 38
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • Henderson B, Martin A. Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect Immun 2011, 79:3476-3491.
    • (2011) Infect Immun , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 39
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria
    • Marraffini LA, Dedent AC, Schneewind O. Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria. Microbiol Mol Biol Rev 2006, 70:192-221.
    • (2006) Microbiol Mol Biol Rev , vol.70 , pp. 192-221
    • Marraffini, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 40
    • 80054970863 scopus 로고    scopus 로고
    • Heterologous protein display on the cell surface of lactic acid bacteria mediated by the s-layer protein
    • Hu SM, Kong J, Sun ZL, Han LL, Kong WT, Yang P. Heterologous protein display on the cell surface of lactic acid bacteria mediated by the s-layer protein. Microb Cell Fact 2011, 10:86.
    • (2011) Microb Cell Fact , vol.10 , pp. 86
    • Hu, S.M.1    Kong, J.2    Sun, Z.L.3    Han, L.L.4    Kong, W.T.5    Yang, P.6
  • 42
    • 56449116275 scopus 로고    scopus 로고
    • Variability and molecular typing of Streptococcus thermophilus strains displaying different proteolytic and acidifying properties
    • Galia W, Perrin C, Genay M, Dary A. Variability and molecular typing of Streptococcus thermophilus strains displaying different proteolytic and acidifying properties. Int Dairy J 2009, 19:89-95.
    • (2009) Int Dairy J , vol.19 , pp. 89-95
    • Galia, W.1    Perrin, C.2    Genay, M.3    Dary, A.4
  • 44
    • 0016686551 scopus 로고
    • Improved medium for lactic Streptococci and their bacteriophages
    • Terzaghi BE, Sandine WE. Improved medium for lactic Streptococci and their bacteriophages. Appl Microbiol 1975, 29:807-813.
    • (1975) Appl Microbiol , vol.29 , pp. 807-813
    • Terzaghi, B.E.1    Sandine, W.E.2
  • 45
    • 0035213445 scopus 로고    scopus 로고
    • Development of a minimal chemically-defined medium for the exponential growth of Streptococcus thermophilus
    • Letort C, Juillard V. Development of a minimal chemically-defined medium for the exponential growth of Streptococcus thermophilus. J Appl Microbiol 2001, 91:1023-1029.
    • (2001) J Appl Microbiol , vol.91 , pp. 1023-1029
    • Letort, C.1    Juillard, V.2
  • 48
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other gram-positive bacteria
    • Maguin E, Prevost H, Ehrlich SD, Gruss A. Efficient insertional mutagenesis in lactococci and other gram-positive bacteria. J Bacteriol 1996, 178:931-935.
    • (1996) J Bacteriol , vol.178 , pp. 931-935
    • Maguin, E.1    Prevost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 49
    • 0037719353 scopus 로고    scopus 로고
    • Qualitative aspect of proteolytic activity of thermophilic lactobacilli using in Swiss cheeses
    • Chopard MA, Schmitt M, Perrerad E, Chamba JF. Qualitative aspect of proteolytic activity of thermophilic lactobacilli using in Swiss cheeses. Lait 2001, 81:183-194.
    • (2001) Lait , vol.81 , pp. 183-194
    • Chopard, M.A.1    Schmitt, M.2    Perrerad, E.3    Chamba, J.F.4


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