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Volumn 76, Issue 21, 2010, Pages 7332-7337

Functionality of sortase a in Lactococcus lactis

Author keywords

[No Author keywords available]

Indexed keywords

CELL WALLS; LACTOCOCCUS LACTIS; LACTOCOCCUS LACTIS IL1403; SORTASE;

EID: 78149426311     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00928-10     Document Type: Article
Times cited : (37)

References (48)
  • 1
    • 0036207211 scopus 로고    scopus 로고
    • Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs
    • Barnett, T. C., and J. R. Scott. 2002. Differential recognition of surface proteins in Streptococcus pyogenes by two sortase gene homologs. J. Bacteriol. 184:2181-2191.
    • (2002) J. Bacteriol. , vol.184 , pp. 2181-2191
    • Barnett, T.C.1    Scott, J.R.2
  • 3
    • 2342560473 scopus 로고    scopus 로고
    • An inducible surface presentation system improves cellular immunity against human papillomavirus type 16 E7 antigen in mice after nasal administration with recombinant lactococci
    • Bermudez-Humaran, L. G., N. G. Cortes-Perez, Y. Le Loir, J. M. Alcocer- Gonzalez, R. S. Tamez-Guerra, R. M. de Oca-Luna, and P. Langella. 2004. An inducible surface presentation system improves cellular immunity against human papillomavirus type 16 E7 antigen in mice after nasal administration with recombinant lactococci. J. Med. Microbiol. 53:427-433.
    • (2004) J. Med. Microbiol. , vol.53 , pp. 427-433
    • Bermudez-Humaran, L.G.1    Cortes-Perez, N.G.2    Le Loir, Y.3    Alcocer-Gonzalez, J.M.4    Tamez-Guerra, R.S.5    De Oca-Luna, R.M.6    Langella, P.7
  • 5
    • 0018800089 scopus 로고
    • A rapid alkaline extraction procedure for screening recombinant plasmid DNA
    • Birnboim, H. C., and J. Doly. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513-1523.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 1513-1523
    • Birnboim, H.C.1    Doly, J.2
  • 6
    • 0027151798 scopus 로고
    • High-efficiency gene inactivation and replacement system for gram-positive bacteria
    • Biswas, I., A. Gruss, S. D. Ehrlich, and E. Maguin. 1993. High-efficiency gene inactivation and replacement system for gram-positive bacteria. J. Bacteriol. 175:3628-3635.
    • (1993) J. Bacteriol. , vol.175 , pp. 3628-3635
    • Biswas, I.1    Gruss, A.2    Ehrlich, S.D.3    Maguin, E.4
  • 7
    • 21844433171 scopus 로고    scopus 로고
    • Genome-wide detection and analysis of cell wall-bound proteins with LPxTG-like sorting motifs
    • Boekhorst, J., M. W. H. J. de Been, M. Kleerebezem, and R. J. Siezen. 2005. Genome-wide detection and analysis of cell wall-bound proteins with LPxTG-like sorting motifs. J. Bacteriol. 187:4928-4934.
    • (2005) J. Bacteriol. , vol.187 , pp. 4928-4934
    • Boekhorst, J.1    De Been, M.W.H.J.2    Kleerebezem, M.3    Siezen, R.J.4
  • 9
    • 33749630786 scopus 로고    scopus 로고
    • Different subcellular locations of secretome components of Gram-positive bacteria
    • Buist, G., A. N. Ridder, J. Kok, and O. P. Kuipers. 2006. Different subcellular locations of secretome components of Gram-positive bacteria. Microbiology 152:2867-2874.
    • (2006) Microbiology , vol.152 , pp. 2867-2874
    • Buist, G.1    Ridder, A.N.2    Kok, J.3    Kuipers, O.P.4
  • 11
    • 2142808787 scopus 로고    scopus 로고
    • A comparative genome analysis identifies distinct sorting pathways in Gram-positive bacteria
    • Comfort, D., and R. T. Clubb. 2004. A comparative genome analysis identifies distinct sorting pathways in Gram-positive bacteria. Infect. Immun. 72:2710-2722.
    • (2004) Infect. Immun. , vol.72 , pp. 2710-2722
    • Comfort, D.1    Clubb, R.T.2
  • 12
    • 0029757175 scopus 로고    scopus 로고
    • Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin
    • de Ruyter, P. G., O. P. Kuipers, and W. M. de Vos. 1996. Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin. Appl. Environ. Microbiol. 62:3662-3667.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3662-3667
    • De Ruyter, P.G.1    Kuipers, O.P.2    De Vos, W.M.3
  • 13
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure
    • Desvaux, M., E. Dumas, I. Chafsey, and M. Hebraud. 2006. Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure. FEMS Microbiol. Lett. 256:1-15.
    • (2006) FEMS Microbiol. Lett. , vol.256 , pp. 1-15
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Hebraud, M.4
  • 14
    • 2142805217 scopus 로고    scopus 로고
    • Ability of Lactococcus lactis to export viral capsid antigens: A crucial step for development of live vaccines
    • Dieye, Y., A. J. W. Hoekman, F. Clier, V. Juillard, H. J. Boot, and J.-C. Piard. 2003. Ability of Lactococcus lactis to export viral capsid antigens: A crucial step for development of live vaccines. Appl. Environ. Microbiol. 69:7281-7288.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 7281-7288
    • Dieye, Y.1    Hoekman, A.J.W.2    Clier, F.3    Juillard, V.4    Boot, H.J.5    Piard, J.-C.6
  • 15
    • 0034971985 scopus 로고    scopus 로고
    • Design of a protein-targeting system for lactic acid bacteria
    • Dieye, Y., S. Usai, F. Clier, A. Gruss, and J. C. Piard. 2001. Design of a protein-targeting system for lactic acid bacteria. J. Bacteriol. 183:4157-4166.
    • (2001) J. Bacteriol. , vol.183 , pp. 4157-4166
    • Dieye, Y.1    Usai, S.2    Clier, F.3    Gruss, A.4    Piard, J.C.5
  • 16
    • 16844372650 scopus 로고    scopus 로고
    • Sorting sortases: A nomenclature proposal for the various sortases of Gram-positive bacteria
    • Dramsi, S., P. Trieu-Cuot, and H. Bierne. 2005. Sorting sortases: A nomenclature proposal for the various sortases of Gram-positive bacteria. Res. Microbiol. 156:289-297.
    • (2005) Res. Microbiol. , vol.156 , pp. 289-297
    • Dramsi, S.1    Trieu-Cuot, P.2    Bierne, H.3
  • 18
    • 0028291165 scopus 로고
    • The Lactococcus lactis sex-factor aggregation gene cluA
    • Godon, J. J., K. Jury, C. A. Shearman, and M. J. Gasson. 1994. The Lactococcus lactis sex-factor aggregation gene cluA. Mol. Microbiol. 12:655-663.
    • (1994) Mol. Microbiol. , vol.12 , pp. 655-663
    • Godon, J.J.1    Jury, K.2    Shearman, C.A.3    Gasson, M.J.4
  • 19
    • 0036668061 scopus 로고    scopus 로고
    • Proteome analysis of human stomach tissue: Separation of soluble proteins by two-dimensional polyacrylamide gel electrophoresis and identification by mass spectrometry
    • Ha, G. H., S. U. Lee, D. G. Kang, N. Y. Ha, S. H. Kim, J. Kim, J. M. Bae, J. W. Kim, and C. W. Lee. 2002. Proteome analysis of human stomach tissue: Separation of soluble proteins by two-dimensional polyacrylamide gel electrophoresis and identification by mass spectrometry. Electrophoresis 23: 2513-2524.
    • (2002) Electrophoresis , vol.23 , pp. 2513-2524
    • Ha, G.H.1    Lee, S.U.2    Kang, D.G.3    Ha, N.Y.4    Kim, S.H.5    Kim, J.6    Bae, J.M.7    Kim, J.W.8    Lee, C.W.9
  • 20
    • 0032603342 scopus 로고    scopus 로고
    • Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels
    • Jensen, O. N., M. Wilm, A. Shevchenko, and M. Mann. 1999. Sample preparation methods for mass spectrometric peptide mapping directly from 2-DE gels. Methods Mol. Biol. 112:513-530.
    • (1999) Methods Mol. Biol. , vol.112 , pp. 513-530
    • Jensen, O.N.1    Wilm, M.2    Shevchenko, A.3    M.Mann, A.4
  • 24
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., B. Larsson, G. von Heijne, and E. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 25
    • 0027260596 scopus 로고
    • Efficient plasmid mobilization by pIP501 in Lactococcus lactis subsp. lactis
    • Langella, P., Y. Le Loir, S. D. Ehrlich, and A. Gruss. 1993. Efficient plasmid mobilization by pIP501 in Lactococcus lactis subsp. lactis. J. Bacteriol. 175: 5806-5813.
    • (1993) J. Bacteriol. , vol.175 , pp. 5806-5813
    • Langella, P.1    Le Loir, Y.2    Ehrlich, S.D.3    Gruss, A.4
  • 26
    • 41149094533 scopus 로고    scopus 로고
    • Ability of Lactobacillus fermentum to overcome host alpha-galactosidase deficiency, as evidenced by reduction of hydrogen excretion in rats consuming soya alphagalacto- oligosaccharides
    • LeBlanc, J. G., F. Ledue-Clier, M. Bensaada, G. S. de Giori, T. Guerekobaya, F. Sesma, V. Juillard, S. Rabot, and J. C. Piard. 2008. Ability of Lactobacillus fermentum to overcome host alpha-galactosidase deficiency, as evidenced by reduction of hydrogen excretion in rats consuming soya alphagalacto- oligosaccharides. BMC Microbiol. 8:22.
    • (2008) BMC Microbiol. , vol.8 , pp. 22
    • LeBlanc, J.G.1    Ledue-Clier, F.2    Bensaada, M.3    De Giori, G.S.4    Guerekobaya, T.5    Sesma, F.6    Juillard, V.7    S.Rabot, S.8    Piard, J.C.9
  • 27
    • 0030027865 scopus 로고    scopus 로고
    • Efficient insertional mutagenesis in lactococci and other gram-positive bacteria
    • Maguin, E., H. Prevost, S. D. Ehrlich, and A. Gruss. 1996. Efficient insertional mutagenesis in lactococci and other gram-positive bacteria. J. Bacteriol. 178:931-935.
    • (1996) J. Bacteriol. , vol.178 , pp. 931-935
    • Maguin, E.1    Prevost, H.2    Ehrlich, S.D.3    Gruss, A.4
  • 28
    • 37749043209 scopus 로고    scopus 로고
    • Pili in Grampositive bacteria: Assembly, involvement in colonization and biofilm development
    • Mandlik, A., A. Swierczynski, A. Das, and H. Ton-That. 2008. Pili in Grampositive bacteria: Assembly, involvement in colonization and biofilm development. Trends Microbiol. 16:33-40.
    • (2008) Trends Microbiol. , vol.16 , pp. 33-40
    • Mandlik, A.1    Swierczynski, A.2    Das, A.3    H.Ton-That, G.4
  • 29
    • 0033618622 scopus 로고    scopus 로고
    • Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall
    • Mazmanian, S. K., G. Liu, H. Ton-That, and O. Schneewind. 1999. Staphylococcus aureus sortase, an enzyme that anchors surface proteins to the cell wall. Science 285:760-763.
    • (1999) Science , vol.285 , pp. 760-763
    • Mazmanian, S.K.1    Liu, G.2    Ton-That, H.3    Schneewind, O.4
  • 30
    • 0023393604 scopus 로고
    • Secretion and processing of staphylococcal nuclease by Bacillus subtilis
    • Miller, J. R., S. Kovacevic, and L. E. Veal. 1987. Secretion and processing of staphylococcal nuclease by Bacillus subtilis. J. Bacteriol. 169:3508-3514.
    • (1987) J. Bacteriol. , vol.169 , pp. 3508-3514
    • Miller, J.R.1    Kovacevic, S.2    Veal, L.E.3
  • 31
    • 0036154791 scopus 로고    scopus 로고
    • Characterization of Streptococcus suis genes encoding proteins homologous to sortase of gram-positive bacteria
    • Osaki, M., D. Takamatsu, Y. Shimoji, and T. Sekizaki. 2002. Characterization of Streptococcus suis genes encoding proteins homologous to sortase of gram-positive bacteria. J. Bacteriol. 184:971-982.
    • (2002) J. Bacteriol. , vol.184 , pp. 971-982
    • Osaki, M.1    Takamatsu, D.2    Shimoji, Y.3    Sekizaki, T.4
  • 32
    • 0842281609 scopus 로고    scopus 로고
    • The biology of Gram-positive sortase enzymes
    • Paterson, G. K., and T. J. Mitchell. 2004. The biology of Gram-positive sortase enzymes. Trends Microbiol. 12:89-95.
    • (2004) Trends Microbiol. , vol.12 , pp. 89-95
    • Paterson, G.K.1    Mitchell, T.J.2
  • 33
    • 0022337107 scopus 로고
    • Efficient utilization of Escherichia coli transcriptional signals in Bacillus subtilis
    • Peschke, U., V. Beuck, H. Bujard, R. Gentz, and S. Le Grice. 1985. Efficient utilization of Escherichia coli transcriptional signals in Bacillus subtilis. J. Mol. Biol. 186:547-555.
    • (1985) J. Mol. Biol. , vol.186 , pp. 547-555
    • Peschke, U.1    Beuck, V.2    Bujard, H.3    Gentz, R.4    Le Grice, S.5
  • 34
    • 0030956641 scopus 로고    scopus 로고
    • Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria
    • Piard, J. C., I. Hautefort, V. A. Fischetti, S. D. Ehrlich, M. Fons, and A. Gruss. 1997. Cell wall anchoring of the Streptococcus pyogenes M6 protein in various lactic acid bacteria. J. Bacteriol. 179:3068-3072.
    • (1997) J. Bacteriol. , vol.179 , pp. 3068-3072
    • Piard, J.C.1    Hautefort, I.2    Fischetti, V.A.3    Ehrlich, S.D.4    Fons, M.5    Gruss, A.6
  • 35
    • 33646153514 scopus 로고    scopus 로고
    • Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations
    • Ramasamy, R., S. Yasawardena, A. Zomer, G. Venema, J. Kok, and K. Leenhouts. 2006. Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations. Vaccine 24:3900-3908.
    • (2006) Vaccine , vol.24 , pp. 3900-3908
    • Ramasamy, R.1    Yasawardena, S.2    Zomer, A.3    Venema, G.4    Kok, J.5    Leenhouts, K.6
  • 36
    • 57449114045 scopus 로고    scopus 로고
    • Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane
    • Raz, A., and V. A. Fischetti. 2008. Sortase A localizes to distinct foci on the Streptococcus pyogenes membrane. Proc. Natl. Acad. Sci. U. S. A. 105: 18549-18554.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 18549-18554
    • Raz, A.1    Fischetti, V.A.2
  • 37
    • 0031686041 scopus 로고    scopus 로고
    • Biochemistry and genetics of von Willebrand factor
    • Sadler, J. E. 1998. Biochemistry and genetics of von Willebrand factor. Annu. Rev. Biochem. 67:395-424.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 395-424
    • Sadler, J.E.1
  • 39
    • 0032871626 scopus 로고    scopus 로고
    • Multi-domain, cell-envelope proteinases of lactic acid bacteria
    • Siezen, R. J. 1999. Multi-domain, cell-envelope proteinases of lactic acid bacteria. Antonie Van Leeuwenhoek 76:139-155.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 139-155
    • Siezen, R.J.1
  • 40
    • 0023992075 scopus 로고
    • Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis
    • Simon, D., and A. Chopin. 1988. Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis. Biochimie 70: 559-566.
    • (1988) Biochimie , vol.70 , pp. 559-566
    • Simon, D.1    Chopin, A.2
  • 42
    • 0031975345 scopus 로고    scopus 로고
    • Functional display of a heterologous protein on the surface of Lactococcus lactis by means of the cell wall anchor of Staphylococcus aureus protein A
    • Steidler, L., J. Viaene, W. Fiers, and E. Remaut. 1998. Functional display of a heterologous protein on the surface of Lactococcus lactis by means of the cell wall anchor of Staphylococcus aureus protein A. Appl. Environ. Microbiol. 64:342-345.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 342-345
    • Steidler, L.1    Viaene, J.2    Fiers, W.3    Remaut, E.4
  • 44
    • 0025252546 scopus 로고
    • Cloning of usp45, a gene encoding a secreted protein from Lactococcus lactis subsp. lactis MG1363
    • van Asseldonk, M., G. Rutten, M. Oteman, R. J. Siezen, W. M. de Vos, and G. Simons. 1990. Cloning of usp45, a gene encoding a secreted protein from Lactococcus lactis subsp. lactis MG1363. Gene 95:155-160.
    • (1990) Gene , vol.95 , pp. 155-160
    • Van Asseldonk, M.1    Rutten, G.2    Oteman, M.3    Siezen, R.J.4    De Vos, W.M.5    Simons, G.6
  • 45
    • 0027309021 scopus 로고
    • Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis
    • van der Meer, J. R., J. Polman, M. M. Beerthuyzen, R. J. Siezen, O. P. Kuipers, and W. M. De Vos. 1993. Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis. J. Bacteriol. 175:2578-2588.
    • (1993) J. Bacteriol. , vol.175 , pp. 2578-2588
    • Van Der Meer, J.R.1    Polman, J.2    Beerthuyzen, M.M.3    Siezen, R.J.4    Kuipers, O.P.5    De Vos, W.M.6
  • 46
    • 0023429232 scopus 로고
    • Isolation and characterization of Streptococcus cremoris Wg2-specific promoters
    • van der Vossen, J. M., D. van der Lelie, and G. Venema. 1987. Isolation and characterization of Streptococcus cremoris Wg2-specific promoters. Appl. Environ. Microbiol. 53:2452-2457.
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 2452-2457
    • Van Der Vossen, J.M.1    Van Der Lelie, D.2    Venema, G.3
  • 48
    • 0024312215 scopus 로고
    • Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase
    • Vos, P., G. Simons, R. J. Siezen, and W. M. de Vos. 1989. Primary structure and organization of the gene for a procaryotic, cell envelope-located serine proteinase. J. Biol. Chem. 264:13579-13585.
    • (1989) J. Biol. Chem. , vol.264 , pp. 13579-13585
    • Vos, P.1    Simons, G.2    Siezen, R.J.3    De Vos, W.M.4


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