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Volumn 76, Issue 8, 2010, Pages 2410-2418

Characterization of a novel LysM domain from lactobacillus fermentam bacteriophage endolysin and its use as an anchor to display heterologous proteins on the surfaces of lactic acid bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL CELLS; BINDING CAPACITIES; BINDING LIGANDS; C TERMINUS; CELL WALLS; CONCENTRATION OF; FLUORESCENCE INTENSITIES; FUSION PROTEINS; GALACTOSIDASES; GRAM-NEGATIVE BACTERIA; GREEN FLUORESCENT PROTEIN; HETEROLOGOUS PROTEINS; IN-VITRO; LACTIC ACID BACTERIA; LACTOBACILLUS CASEI; LACTOCOCCUS LACTIS; OPTIMAL CONDITIONS; PEPTIDOGLYCANS; SEQUENCE ANALYSIS; STREPTOCOCCUS THERMOPHILUS; SURFACE DISPLAY SYSTEM; SURFACE DISPLAYS;

EID: 77950567929     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01752-09     Document Type: Article
Times cited : (58)

References (33)
  • 5
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • Buist, G., A. Steen, J. Kok, and O. P. Kuipers. 2008. LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol. Microbiol. 68: 838-847.
    • (2008) Mol. Microbiol. , vol.68 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 6
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist, G., J. Kok, K. J. Leenhouts, M. Dabrowska, G. Venema, and A. J. Haandrikman. 1995. Molecular cloning and nucleotide sequence of the gene encoding the major peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation. J. Bacteriol. 177: 1554-1563.
    • (1995) J. Bacteriol. , vol.177 , pp. 1554-1563
    • Buist, G.1    Kok, J.2    Leenhouts, K.J.3    Dabrowska, M.4    Venema, G.5    Haandrikman, A.J.6
  • 7
    • 0344393481 scopus 로고    scopus 로고
    • Identification and characterization of a peptidoglycan hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation
    • Carroll, S. A., T. Hain, U. Technow, A. Darji, P. Pashalidis, S. W. Joseph, and T. Chakraborty. 2003. Identification and characterization of a peptidoglycan hydrolase, MurA, of Listeria monocytogenes, a muramidase needed for cell separation. J. Bacteriol. 185: 6801-6808.
    • (2003) J. Bacteriol. , vol.185 , pp. 6801-6808
    • Carroll, S.A.1    Hain, T.2    Technow, U.3    Darji, A.4    Pashalidis, P.5    Joseph, S.W.6    Chakraborty, T.7
  • 8
    • 0034971985 scopus 로고    scopus 로고
    • Design of a protein-targeting system for lactic acid bacteria
    • DOI 10.1128/JB.183.14.4157-4166.2001
    • 8. 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. (Pubitemid 32568066)
    • (2001) Journal of Bacteriology , vol.183 , Issue.14 , pp. 4157-4166
    • Dieye, Y.1    Usai, S.2    Clier, F.3    Gruss, A.4    Piard, J.-C.5
  • 9
    • 51349138721 scopus 로고    scopus 로고
    • Bacteriophage and peptidoglycan degrading enzymes with antimicrobial applications
    • Donovan, D. M. 2007. Bacteriophage and peptidoglycan degrading enzymes with antimicrobial applications. Recent Pat. Biotechnol. 1: 113-122.
    • (2007) Recent Pat. Biotechnol. , vol.1 , pp. 113-122
    • Donovan, D.M.1
  • 11
    • 0037212403 scopus 로고    scopus 로고
    • Microbial cell-surface display
    • Lee, S. Y., J. H. Choi, and Z. Xu. 2003. Microbial cell-surface display. Trends Biotechnol. 21: 45-52.
    • (2003) Trends Biotechnol. , vol.21 , pp. 45-52
    • Lee, S.Y.1    Choi, J.H.2    Xu, Z.3
  • 12
    • 49449101856 scopus 로고    scopus 로고
    • Engineering of a human vaginal Lactobacillus strain for surface expression of two-domain CD4 molecules
    • Liu, X., L. A. Lagenaur, P. P. Lee, and Q. Xu. 2008. Engineering of a human vaginal Lactobacillus strain for surface expression of two-domain CD4 molecules. Appl. Environ. Microbiol. 74: 4626-4635.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 4626-4635
    • Liu, X.1    Lagenaur, L.A.2    Lee, P.P.3    Xu, Q.4
  • 13
    • 0036231904 scopus 로고    scopus 로고
    • C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates
    • Loessner, M. J., K. Kramer, F. Ebel, and S. Scherer. 2002. C-terminal domains of Listeria monocytogenes bacteriophage murein hydrolases determine specific recognition and high-affinity binding to bacterial cell wall carbohydrates. Mol. Microbiol. 44: 335-349.
    • (2002) Mol. Microbiol. , vol.44 , pp. 335-349
    • Loessner, M.J.1    Kramer, K.2    Ebel, F.3    Scherer, S.4
  • 14
    • 77950588042 scopus 로고    scopus 로고
    • Cloning and expression of the beta-galactosidase gene of Paenibacillus sp. Kl in E. coli
    • Lu, W., W. Kong, Z. Sun, J. Kong, and M. Ji. 2008. Cloning and expression of the beta-galactosidase gene of Paenibacillus sp. Kl in E. coli. J. Shandong Univ. (Nat. Sci.) 43: 69-73.
    • (2008) J. Shandong Univ. (Nat. Sci.) , vol.43 , pp. 69-73
    • Lu, W.1    Kong, W.2    Sun, Z.3    Kong, J.4    Ji, M.5
  • 15
    • 33645137247 scopus 로고    scopus 로고
    • Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria
    • Marrafflni, L. A., A. C. Dedent, and O. Schneewind. 2006. Sortases and the art of anchoring proteins to the envelopes of gram-positive bacteria. Microbiol. Mol. Biol. Rev. 70: 192-221.
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 192-221
    • Marrafflni, L.A.1    Dedent, A.C.2    Schneewind, O.3
  • 16
    • 33644859125 scopus 로고    scopus 로고
    • Display of ∞-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch
    • Narita, J., K. Okano, T. Kitao, S. Ishida, T. Sewaki, M. H. Sung, H. Fukuda, and A. Kondo. 2006. Display of ∞-amylase on the surface of Lactobacillus casei cells by use of the PgsA anchor protein, and production of lactic acid from starch. Appl. Environ. Microbiol. 72: 269-275.
    • (2006) Appl. Environ. Microbiol. , vol.72 , pp. 269-275
    • Narita, J.1    Okano, K.2    Kitao, T.3    Ishida, S.4    Sewaki, T.5    Sung, M.H.6    Fukuda, H.7    Kondo, A.8
  • 17
    • 39649095621 scopus 로고    scopus 로고
    • System using tandem repeats of the cA peptidoglycan-binding domain from Lactococcus lactis for display of both N- And C-terminal fusions on cell surfaces of lactic acid bacteria
    • Okano, K., Q. Zhang, S. Kimura, J. Narita, T. Tanaka, H. Fukuda, and A. Kondo. 2008. System using tandem repeats of the cA peptidoglycan-binding domain from Lactococcus lactis for display of both N- and C-terminal fusions on cell surfaces of lactic acid bacteria. Appl. Environ. Microbiol. 74: 1117-1123.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1117-1123
    • Okano, K.1    Zhang, Q.2    Kimura, S.3    Narita, J.4    Tanaka, T.5    Fukuda, H.6    Kondo, A.7
  • 18
    • 23944501101 scopus 로고    scopus 로고
    • Cell surface display system for Lactococcus lactis: A novel development for oral vaccine
    • Rana, A. R., N. R. Varma, K. Yusoff, E. Ross, and H. L. Foo. 2005. Cell surface display system for Lactococcus lactis: a novel development for oral vaccine. Appl. Microbiol. Biotechnol. 68: 75-81.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 75-81
    • Rana, A.R.1    Varma, N.R.2    Yusoff, K.3    Ross, E.4    Foo, H.L.5
  • 19
    • 0036151762 scopus 로고    scopus 로고
    • Production and targeting of the Brucella abortus antigen L7/L12 in Lactococcus lactis: A first step towards food-grade live vaccines against brucellosis
    • Ribeiro, L. A., V. Azevedo, Y. Le Loir, S. C. Oliveira, Y. Dieye, J. C. Piard, A. Gruss, and P. Langella. 2002. Production and targeting of the Brucella abortus antigen L7/L12 in Lactococcus lactis: a first step towards food-grade live vaccines against brucellosis. Appl. Environ. Microbiol. 68: 910-916.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 910-916
    • Ribeiro, L.A.1    Azevedo, V.2    Le Loir, Y.3    Oliveira, S.C.4    Dieye, Y.5    Piard, J.C.6    Gruss, A.7    Langella, P.8
  • 20
    • 0027467007 scopus 로고
    • Cell-surface location of Ltoeria-specific protein p60-detection of Listeria cells by indirect immunofluorescence
    • Ruhland, G. J., M. Hellwig, G. Wanner, and F. Fiedler. 1993. Cell-surface location of Ltoeria-specific protein p60-detection of Listeria cells by indirect immunofluorescence. J. Gen. Microbiol. 139: 609-616.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 609-616
    • Ruhland, G.J.1    Hellwig, M.2    Wanner, G.3    Fiedler, F.4
  • 22
    • 20444471564 scopus 로고    scopus 로고
    • AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning
    • Steen, A., G. Buist, G. J. Horsburgh, G. Venema, O. P. Kuipers, S. J. Foster, and J. Kok. 2005. AcmA of Lactococcus lactis is an N- acetylglucosaminidase with an optimal number of LysM domains for proper functioning. FEBS J. 272: 2854-2868.
    • (2005) FEBS J. , vol.272 , pp. 2854-2868
    • Steen, A.1    Buist, G.2    Horsburgh, G.J.3    Venema, G.4    Kuipers, O.P.5    Foster, S.J.6    Kok, J.7
  • 24
    • 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
  • 25
    • 40749125219 scopus 로고    scopus 로고
    • Bidirectional cell-surface anchoring function of C-terminal repeat region of peptidoglycan hydrolase of Lactococcus lactis IL1403
    • Tarahomjoo, S., Y. Katakura, E. Satoh, and S. Shioya. 2008. Bidirectional cell-surface anchoring function of C-terminal repeat region of peptidoglycan hydrolase of Lactococcus lactis IL1403. J. Biosci. Bioeng. 105: 116-121.
    • (2008) J. Biosci. Bioeng. , vol.105 , pp. 116-121
    • Tarahomjoo, S.1    Katakura, Y.2    Satoh, E.3    Shioya, S.4
  • 26
    • 2942584912 scopus 로고    scopus 로고
    • Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus
    • Turner, M. S., L. M. Hafner, T. Walsh, and P. M. Giffard. 2004. Identification and characterization of the novel LysM domain-containing surface protein Sep from Lactobacillus fermentum BR11 and its use as a peptide fusion partner in Lactobacillus and Lactococcus. Appl. Environ. Microbiol. 70: 3673-3680.
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3673-3680
    • Turner, M.S.1    Hafner, L.M.2    Walsh, T.3    Giffard, P.M.4
  • 30
    • 56649097462 scopus 로고    scopus 로고
    • Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophage phiPYB5 of Lactobacillus fermentum
    • Wang, S., J. Kong, and X. Zhang. 2008. Identification and characterization of the two-component cell lysis cassette encoded by temperate bacteriophage phiPYB5 of Lactobacillus fermentum. J. Appl. Microbiol. 105: 1939-1944.
    • (2008) J. Appl. Microbiol. , vol.105 , pp. 1939-1944
    • Wang, S.1    Kong, J.2    Zhang, X.3
  • 31
    • 52649134462 scopus 로고    scopus 로고
    • The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis
    • Yamamoto, H., Y. Miyake, M. Hisaoka, S. Kurosawa, and J. Sekiguchi. 2008. The major and minor wall teichoic acids prevent the sidewall localization of vegetative DL-endopeptidase LytF in Bacillus subtilis. Mol. Microbiol. 70: 297-310.
    • (2008) Mol. Microbiol. , vol.70 , pp. 297-310
    • Yamamoto, H.1    Miyake, Y.2    Hisaoka, M.3    Kurosawa, S.4    Sekiguchi, J.5
  • 32
    • 33748680714 scopus 로고    scopus 로고
    • Isolation and characterization of a Lactobacillus fermentum temperate bacteriophage from Chinese yogurt
    • Zhang, X., J. Kong, and Y. Qu. 2006. Isolation and characterization of a Lactobacillus fermentum temperate bacteriophage from Chinese yogurt. J. Appl. Microbiol. 101: 857-863.
    • (2006) J. Appl. Microbiol. , vol.101 , pp. 857-863
    • Zhang, X.1    Kong, J.2    Qu, Y.3
  • 33
    • 22544440575 scopus 로고    scopus 로고
    • The holin protein of bacteriophage PRD1 forms a pore for small-molecule and endolysin translocation
    • DOI 10.1128/JB.187.15.5397-5405.2005
    • 33. Ziedaite, G., R. Daugelaviclus, J. K. Bamford, and D. H. Bamford. 2005. The holin protein of bacteriophage FRDl forms a pore for small-molecule and endolysin translocation. J. Bacteriol. 187: 5397-5405. (Pubitemid 41022959)
    • (2005) Journal of Bacteriology , vol.187 , Issue.15 , pp. 5397-5405
    • Ziedaite, G.1    Daugelavicius, R.2    Bamford, J.K.H.3    Bamford, D.H.4


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