메뉴 건너뛰기




Volumn 98, Issue 10, 2014, Pages 4331-4345

Exploiting the peptidoglycan-binding motif, LysM, for medical and industrial applications

Author keywords

Cell immobilization; LysM; Microbe detection; Noncovalent peptidoglycan binding; Protein display; Vaccine

Indexed keywords

CELL IMMOBILIZATION; CELL MEMBRANES; ENZYME IMMOBILIZATION; INDUSTRIAL APPLICATIONS; SURFACE ANALYSIS; VACCINES;

EID: 84900825895     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5633-7     Document Type: Short Survey
Times cited : (59)

References (90)
  • 2
    • 55749106255 scopus 로고    scopus 로고
    • Detection and localization of single LysM-peptidoglycan interactions
    • Andre G, Leenhouts K, Hols P, Dufrêne YF (2008) Detection and localization of single LysM-peptidoglycan interactions. J Bacteriol 190:7079-7086
    • (2008) J Bacteriol , vol.190 , pp. 7079-7086
    • Andre, G.1    Leenhouts, K.2    Hols, P.3    Dufrêne, Y.F.4
  • 5
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • Bateman A, Bycroft M (2000) The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 299:1113-1119
    • (2000) J Mol Biol , vol.299 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 7
    • 33846926952 scopus 로고    scopus 로고
    • C-terminal WxL domain mediates cell wall binding in Enterococcus faecalis and other gram-positive bacteria
    • DOI 10.1128/JB.00773-06
    • Brinster S, Furlan S, Serror P (2007) C-terminal WxL domain mediates cell wall binding in Enterococcus faecalis and other gram-positive bacteria. J Bacteriol 189:1244-1253 (Pubitemid 46239746)
    • (2007) Journal of Bacteriology , vol.189 , Issue.4 , pp. 1244-1253
    • Brinster, S.1    Furlan, S.2    Serror, P.3
  • 8
    • 0028907622 scopus 로고
    • Molecular cloning and nucleotide sequence of the gene encoding themajor peptidoglycan hydrolase of Lactococcus lactis, a muramidase needed for cell separation
    • Buist G, Kok J, Leenhouts KJ, Dabrowska M, Venema G, Haandrikman AJ (1995) Molecular cloning and nucleotide sequence of the gene encoding themajor 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
  • 9
    • 33749630786 scopus 로고    scopus 로고
    • Different subcellular locations of secretome components of Gram-positive bacteria
    • Read, Engl
    • Buist G, Ridder A, Kok J, Kuipers OP (2006) Different subcellular locations of secretome components of Gram-positive bacteria. Microbiol (Read, Engl) 152:2867-2874
    • (2006) Microbiol , vol.152 , pp. 2867-2874
    • Buist, G.1    Ridder, A.2    Kok, J.3    Kuipers, O.P.4
  • 10
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • DOI 10.1111/j.1365-2958.2008.06211.x
    • Buist G, Steen A, Kok J, Kuipers OP (2008) LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 68:838-847 (Pubitemid 351581067)
    • (2008) Molecular Microbiology , vol.68 , Issue.4 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 11
    • 84885461739 scopus 로고    scopus 로고
    • Staphylococcus aureus mutants lacking the LytR-CpsA-Psr family of enzymes release cell wall teichoic acids into the extracellular medium
    • Chan YGY, Frankel MB, Dengler V, Schneewind O, Missiakas D (2013) Staphylococcus aureus mutants lacking the LytR-CpsA-Psr family of enzymes release cell wall teichoic acids into the extracellular medium. J Bacteriol 195:4650-4659
    • (2013) J Bacteriol , vol.195 , pp. 4650-4659
    • Chan, Y.G.Y.1    Frankel, M.B.2    Dengler, V.3    Schneewind, O.4    Missiakas, D.5
  • 13
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure
    • Desvaux M, Dumas E, Chafsey I, Hébraud M (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    Hébraud, M.4
  • 14
    • 84862587725 scopus 로고    scopus 로고
    • Bacterium-like particles supplemented with inactivated influenza antigen induce cross-protective influenza-specific antibody responses through intranasal administration
    • De Haan A, Haijema BJ, Voorn P, Meijerhof T, van Roosmalen ML, Leenhouts K (2012) Bacterium-like particles supplemented with inactivated influenza antigen induce cross-protective influenza-specific antibody responses through intranasal administration. Vaccine 30:4884-4891
    • (2012) Vaccine , vol.30 , pp. 4884-4891
    • De Haan, A.1    Haijema, B.J.2    Voorn, P.3    Meijerhof, T.4    Van Roosmalen, M.L.5    Leenhouts, K.6
  • 15
    • 63349108180 scopus 로고    scopus 로고
    • Fungal LysM effectors: Extinguishers of host immunity?
    • De Jonge R, Thomma BPHJ (2009) Fungal LysM effectors: extinguishers of host immunity? Trends Microbiol 17:151-157
    • (2009) Trends Microbiol , vol.17 , pp. 151-157
    • De Jonge, R.1    Thomma, B.P.H.J.2
  • 17
    • 0037016664 scopus 로고    scopus 로고
    • The elastin-binding protein of Staphylococcus aureus (EbpS) is expressed at the cell surface as an integral membrane protein and not as a cell wall-associated protein
    • DOI 10.1074/jbc.M107621200
    • Downer R, Roche F, Park PW, Mecham RP, Foster TJ (2002) The elastin-binding protein of Staphylococcus aureus (EbpS) is expressed at the cell surface as an integral membrane protein and not as a cell wall-associated protein. J Biol Chem 277:243-250 (Pubitemid 34952051)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 243-250
    • Downer, R.1    Roche, F.2    Park, P.W.3    Mecham, R.P.4    Foster, T.J.5
  • 18
    • 79960425958 scopus 로고    scopus 로고
    • The cell surface proteome of Staphylococcus aureus
    • Dreisbach A, van Dijl JM, Buist G (2011) The cell surface proteome of Staphylococcus aureus. Proteomics 11:3154-3168
    • (2011) Proteomics , vol.11 , pp. 3154-3168
    • Dreisbach, A.1    Van Dijl, J.M.2    Buist, G.3
  • 19
    • 84858975440 scopus 로고    scopus 로고
    • Determinants of murein hydrolase targeting to cross-wall of Staphylococcus aureus peptidoglycan
    • Frankel MB, Schneewind O (2012) Determinants of murein hydrolase targeting to cross-wall of Staphylococcus aureus peptidoglycan. J Biol Chem 287:10460-10471
    • (2012) J Biol Chem , vol.287 , pp. 10460-10471
    • Frankel, M.B.1    Schneewind, O.2
  • 21
    • 0023055384 scopus 로고
    • Nucleotide sequence of Bacillus phage phi 29 genes 14 and 15: Homology of gene 15 with other phage lysozymes
    • Garvey KJ, Saedi MS, Ito J (1986) Nucleotide sequence of Bacillus phage phi 29 genes 14 and 15: homology of gene 15 with other phage lysozymes. Nucleic Acids Res 14:10001-10008
    • (1986) Nucleic Acids Res , vol.14 , pp. 10001-10008
    • Garvey, K.J.1    Saedi, M.S.2    Ito, J.3
  • 22
    • 0028326013 scopus 로고
    • Binding site-shaped repeated sequences of bacterial wall peptidoglycan hydrolases
    • Ghuysen JM, Lamotte-Brasseur J, Joris B, Shockman GD (1994) Binding site-shaped repeated sequences of bacterial wall peptidoglycan hydrolases. FEBS Lett 342:23-28
    • (1994) FEBS Lett , vol.342 , pp. 23-28
    • Ghuysen, J.M.1    Lamotte-Brasseur, J.2    Joris, B.3    Shockman, G.D.4
  • 23
    • 54349127109 scopus 로고    scopus 로고
    • Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: Application to the villin headpiece subdomain and the LysM domain
    • Glasscock JM, Zhu Y, Chowdhury P, Tang J, Gai F (2008) Using an amino acid fluorescence resonance energy transfer pair to probe protein unfolding: application to the villin headpiece subdomain and the LysM domain. Biochemistry 47:11070-11076
    • (2008) Biochemistry , vol.47 , pp. 11070-11076
    • Glasscock, J.M.1    Zhu, Y.2    Chowdhury, P.3    Tang, J.4    Gai, F.5
  • 24
    • 33645237316 scopus 로고    scopus 로고
    • Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus
    • Gründling A, Schneewind O (2006) Cross-linked peptidoglycan mediates lysostaphin binding to the cell wall envelope of Staphylococcus aureus. J Bacteriol 188:2463-2472
    • (2006) J Bacteriol , vol.188 , pp. 2463-2472
    • Gründling, A.1    Schneewind, O.2
  • 26
    • 84863114164 scopus 로고    scopus 로고
    • Characterization of the modular design of the autolysin/adhesin Aaa from Staphylococcus aureus
    • Hirschhausen N, Schlesier T, Peters G, Heilmann C (2012) Characterization of the modular design of the autolysin/adhesin Aaa from Staphylococcus aureus. PLoS ONE 7:e40353
    • (2012) PLoS ONE , vol.7
    • Hirschhausen, N.1    Schlesier, T.2    Peters, G.3    Heilmann, C.4
  • 27
    • 77950567929 scopus 로고    scopus 로고
    • Characterization of a novel LysM domain from Lactobacillus fermentum bacteriophage endolysin and its use as an anchor to display heterologous proteins on the surfaces of lactic acid bacteria
    • Hu S, Kong J, Kong W, Guo T, Ji M (2010) Characterization of a novel LysM domain from Lactobacillus fermentum bacteriophage endolysin and its use as an anchor to display heterologous proteins on the surfaces of lactic acid bacteria. Appl Environ Microbiol 76:2410-2418
    • (2010) Appl Environ Microbiol , vol.76 , pp. 2410-2418
    • Hu, S.1    Kong, J.2    Kong, W.3    Guo, T.4    Ji, M.5
  • 28
    • 77956931038 scopus 로고    scopus 로고
    • Immobilization of Lactococcus lactis to cellulosic material by cellulose-binding domain of Cellvibrio japonicus
    • Kylä-Nikkilä K, Alakuijala U, Saris PEJ (2010) Immobilization of Lactococcus lactis to cellulosic material by cellulose-binding domain of Cellvibrio japonicus. J Appl Microbiol 109:1274-1283
    • (2010) J Appl Microbiol , vol.109 , pp. 1274-1283
    • Kylä-Nikkilä, K.1    Alakuijala, U.2    Saris, P.E.J.3
  • 29
    • 84860512983 scopus 로고    scopus 로고
    • In vitro and in vivo analyses of the Bacillus anthracis spore cortex lytic protein SleL
    • Read, Engl
    • Lambert EA, Sherry N, Popham DL (2012) In vitro and in vivo analyses of the Bacillus anthracis spore cortex lytic protein SleL. Microbiol (Read, Engl) 158:1359-1368
    • (2012) Microbiol , vol.158 , pp. 1359-1368
    • Lambert, E.A.1    Sherry, N.2    Popham, D.L.3
  • 33
    • 78650165803 scopus 로고    scopus 로고
    • Assembly of the type II secretion system: Identification of ExeA residues critical for peptidoglycan binding and secretin multimerization
    • Li G, Miller A, Bull H, Howard SP (2011) Assembly of the type II secretion system: identification of ExeA residues critical for peptidoglycan binding and secretin multimerization. J Bacteriol 193: 197-204
    • (2011) J Bacteriol , vol.193 , pp. 197-204
    • Li, G.1    Miller, A.2    Bull, H.3    Howard, S.P.4
  • 34
    • 75349094573 scopus 로고    scopus 로고
    • Functional cell surface display of endo-beta-1, 3-1, 4-glucanase in Lactococcus lactis using N-acetylmuraminidase as the anchoring motif
    • Li X, Huang X, Shao X, Li L (2009) Functional cell surface display of endo-beta-1, 3-1, 4-glucanase in Lactococcus lactis using N-acetylmuraminidase as the anchoring motif. Sheng Wu Gong Cheng Xue Bao 25:89-94
    • (2009) Sheng Wu Gong Cheng Xue Bao , vol.25 , pp. 89-94
    • Li, X.1    Huang, X.2    Shao, X.3    Li, L.4
  • 35
    • 11144296012 scopus 로고    scopus 로고
    • Receptor Binding Domain of Escherichia coli F18 Fimbrial Adhesin FedF Can Be both Efficiently Secreted and Surface Displayed in a Functional Form in Lactococcus lactis
    • DOI 10.1128/AEM.70.4.2061-2071.2004
    • Lindholm A, Smeds A, Palva A (2004) Receptor binding domain of Escherichia coli F18 fimbrial adhesin FedF can be both efficiently secreted and surface displayed in a functional form in Lactococcus lactis. Appl Environ Microbiol 70:2061-2071 (Pubitemid 38500504)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.4 , pp. 2061-2071
    • Lindholm, A.1    Smeds, A.2    Palva, A.3
  • 37
    • 0028131141 scopus 로고
    • Lytic enzymes associated with defective prophages of Bacillus subtilis: Sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX
    • Read Engl
    • Longchamp PF, Mauël C, Karamata D (1994) Lytic enzymes associated with defective prophages of Bacillus subtilis: sequencing and characterization of the region comprising the N-acetylmuramoyl-L-alanine amidase gene of prophage PBSX. Microbiol (Read Engl) 140(Pt 8):1855-1867
    • (1994) Microbiol , vol.140 , Issue.PART 8 , pp. 1855-1867
    • Longchamp, P.F.1    Mauël, C.2    Karamata, D.3
  • 38
    • 80053201228 scopus 로고    scopus 로고
    • Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins
    • Low LY, Yang C, Perego M, Osterman A, Liddington R (2011) Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity, and host range of phage lysins. J Biol Chem 286:34391-34403
    • (2011) J Biol Chem , vol.286 , pp. 34391-34403
    • Low, L.Y.1    Yang, C.2    Perego, M.3    Osterman, A.4    Liddington, R.5
  • 39
    • 33644852491 scopus 로고    scopus 로고
    • Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges
    • DOI 10.1074/jbc.M509691200
    • Lu JZ, Fujiwara T, Komatsuzawa H, Sugai M, Sakon J (2006) Cell wall-targeting domain of glycylglycine endopeptidase distinguishes among peptidoglycan cross-bridges. J Biol Chem 281:549-558 (Pubitemid 43671218)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 549-558
    • Lu, J.Z.1    Fujiwara, T.2    Komatsuzawa, H.3    Sugai, M.4    Sakon, J.5
  • 41
    • 35449004023 scopus 로고    scopus 로고
    • Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis
    • DOI 10.1099/mic.0.2007/005835-0
    • Meyrand M, Boughammoura A, Courtin P, Mézange C, Guillot A, Chapot-Chartier M-P (2007) Peptidoglycan N-acetylglucosamine deacetylation decreases autolysis in Lactococcus lactis. Microbiol (Read Engl) 153:3275-3285 (Pubitemid 47629533)
    • (2007) Microbiology , vol.153 , Issue.10 , pp. 3275-3285
    • Meyrand, M.1    Boughammoura, A.2    Courtin, P.3    Mezange, C.4    Guillot, A.5    Chapot-Chartier, M.-P.6
  • 42
    • 79954724947 scopus 로고    scopus 로고
    • Lactobacillus acidophilus as a live vehicle for oral immunization against chicken anemia virus
    • Moeini H, Rahim RA, Omar AR, Shafee N, Yusoff K (2011) Lactobacillus acidophilus as a live vehicle for oral immunization against chicken anemia virus. Appl Microbiol Biotechnol 90:77-88
    • (2011) Appl Microbiol Biotechnol , vol.90 , pp. 77-88
    • Moeini, H.1    Rahim, R.A.2    Omar, A.R.3    Shafee, N.4    Yusoff, K.5
  • 43
    • 84857126472 scopus 로고    scopus 로고
    • Bacterium-like particles as multi-epitope delivery platform for Plasmodium berghei circumsporozoite protein induce complete protection against malaria in mice
    • Nganou-Makamdop K, van Roosmalen ML, Audouy SAL, van Gemert G-J, Leenhouts K, Hermsen CC, Sauerwein RW(2012) Bacterium-like particles as multi-epitope delivery platform for Plasmodium berghei circumsporozoite protein induce complete protection against malaria in mice. Malar J 11:50
    • (2012) Malar J , vol.11 , pp. 50
    • Nganou-Makamdop, K.1    Van Roosmalen, M.L.2    Audouy, S.A.L.3    Van Gemert, G.-J.4    Leenhouts, K.5    Hermsen, C.C.6    Sauerwein, R.W.7
  • 44
    • 41949097138 scopus 로고    scopus 로고
    • LysM domains from Pteris ryukyuensis chitinase-A: A stability study and characterization of the chitin-binding site
    • Ohnuma T, Onaga S, Murata K, Taira T, Katoh E (2008) LysM domains from Pteris ryukyuensis chitinase-A: a stability study and characterization of the chitin-binding site. J Biol Chem 283:5178-5187
    • (2008) J Biol Chem , vol.283 , pp. 5178-5187
    • Ohnuma, T.1    Onaga, S.2    Murata, K.3    Taira, T.4    Katoh, E.5
  • 45
    • 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
    • DOI 10.1128/AEM.02012-07
    • Okano K, Zhang Q, Kimura S, Narita J, Tanaka T, Fukuda H, Kondo A (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 (Pubitemid 351287083)
    • (2008) Applied and Environmental Microbiology , vol.74 , Issue.4 , pp. 1117-1123
    • Okano, K.1    Zhang, Q.2    Kimura, S.3    Narita, J.4    Tanaka, T.5    Fukuda, H.6    Kondo, A.7
  • 47
    • 24644437812 scopus 로고    scopus 로고
    • The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as a protein module in eukaryotes
    • DOI 10.1002/prot.20543
    • Percudani R, Montanini B, Ottonello S (2005) The anti-HIV cyanovirin-N domain is evolutionarily conserved and occurs as a protein module in eukaryotes. Proteins 60:670-678 (Pubitemid 41266424)
    • (2005) Proteins: Structure, Function and Genetics , vol.60 , Issue.4 , pp. 670-678
    • Percudani, R.1    Montanini, B.2    Ottonello, S.3
  • 48
    • 84864413727 scopus 로고    scopus 로고
    • Monitoring lysin motif-ligand interactions via tryptophan analog fluorescence spectroscopy
    • Petrović DM, Leenhouts K, van Roosmalen ML, Kleinjan F, Broos J (2012) Monitoring lysin motif-ligand interactions via tryptophan analog fluorescence spectroscopy. Anal Biochem 428:111-118
    • (2012) Anal Biochem , vol.428 , pp. 111-118
    • Petrović, D.M.1    Leenhouts, K.2    Van Roosmalen, M.L.3    Kleinjan, F.4    Broos, J.5
  • 49
    • 0034108191 scopus 로고    scopus 로고
    • HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing
    • DOI 10.1046/j.1365-2958.2000.01757.x
    • Poquet I, Saint V, Seznec E, Simoes N, Bolotin A, Gruss A (2000) HtrA is the unique surface housekeeping protease in Lactococcus lactis and is required for natural protein processing. Mol Microbiol 35:1042-1051 (Pubitemid 30137774)
    • (2000) Molecular Microbiology , vol.35 , Issue.5 , pp. 1042-1051
    • Poquet, I.1    Saint, V.2    Seznec, E.3    Simoes, N.4    Bolotin, A.5    Gruss, A.6
  • 50
    • 69349099057 scopus 로고    scopus 로고
    • Sortase-mediated protein ligation: An emerging biotechnology tool for protein modification and immobilisation
    • Proft T (2010) Sortase-mediated protein ligation: an emerging biotechnology tool for protein modification and immobilisation. Biotechnol Lett 32:1-10
    • (2010) Biotechnol Lett , vol.32 , pp. 1-10
    • Proft, T.1
  • 51
    • 23944501101 scopus 로고    scopus 로고
    • Cell surface display system for Lactococcus lactis: A novel development for oral vaccine
    • DOI 10.1007/s00253-004-1851-8
    • Raha AR, Varma NRS, Yusoff K, Ross E, Foo HL (2005) Cell surface display system for Lactococcus lactis: a novel development for oral vaccine. Appl Microbiol Biotechnol 68:75-81 (Pubitemid 41202117)
    • (2005) Applied Microbiology and Biotechnology , vol.68 , Issue.1 , pp. 75-81
    • Raha, A.R.1    Varma, N.R.S.2    Yusoff, K.3    Ross, E.4    Foo, H.L.5
  • 52
    • 33646153514 scopus 로고    scopus 로고
    • Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations
    • Ramasamy R, Yasawardena S, Zomer A, Venema G, Kok J, Leenhouts K (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
  • 53
    • 77249086689 scopus 로고    scopus 로고
    • Neonatal mucosal immunization with a non-living, non-genetically modified Lactococcus lactis vaccine carrier induces systemic and local Th1-type immunity and protects against lethal bacterial infection
    • Ramirez K, Ditamo Y, Rodriguez L, Picking WL, van Roosmalen ML, Leenhouts K, Pasetti MF (2010) Neonatal mucosal immunization with a non-living, non-genetically modified Lactococcus lactis vaccine carrier induces systemic and local Th1-type immunity and protects against lethal bacterial infection. Mucosal Immunol 3: 159-171
    • (2010) Mucosal Immunol , vol.3 , pp. 159-171
    • Ramirez, K.1    Ditamo, Y.2    Rodriguez, L.3    Picking, W.L.4    Van Roosmalen, M.L.5    Leenhouts, K.6    Pasetti, M.F.7
  • 54
    • 77958608927 scopus 로고    scopus 로고
    • Engineered lactic acid bacterium Lactococcus lactis capable of binding antibodies and tumor necrosis factor alpha
    • Ravnikar M, Strukelj B, Obermajer N, Lunder M, Berlec A (2010) Engineered lactic acid bacterium Lactococcus lactis capable of binding antibodies and tumor necrosis factor alpha. Appl Environ Microbiol 76:6928-6932
    • (2010) Appl Environ Microbiol , vol.76 , pp. 6928-6932
    • Ravnikar, M.1    Strukelj, B.2    Obermajer, N.3    Lunder, M.4    Berlec, A.5
  • 55
    • 84880070064 scopus 로고    scopus 로고
    • A novel type of peptidoglycan-binding domain highly specific for amidated D-Asp cross-bridge, identified in Lactobacillus casei bacteriophage endolysins
    • Regulski K, Courtin P, Kulakauskas S, Chapot-Chartier M-P (2013) A novel type of peptidoglycan-binding domain highly specific for amidated D-Asp cross-bridge, identified in Lactobacillus casei bacteriophage endolysins. J Biol Chem 288:20416-20426
    • (2013) J Biol Chem , vol.288 , pp. 20416-20426
    • Regulski, K.1    Courtin, P.2    Kulakauskas, S.3    Chapot-Chartier, M.-P.4
  • 60
    • 81755177747 scopus 로고    scopus 로고
    • A LysM and SH3-domain containing region of the Listeria monocytogenes p60 protein stimulates accessory cells to promote activation of host NK cells
    • Schmidt RL, Filak HC, Lemon JD, Potter TA, Lenz LL (2011) A LysM and SH3-domain containing region of the Listeria monocytogenes p60 protein stimulates accessory cells to promote activation of host NK cells. PLoS Pathog 7:e1002368
    • (2011) PLoS Pathog , vol.7
    • Schmidt, R.L.1    Filak, H.C.2    Lemon, J.D.3    Potter, T.A.4    Lenz, L.L.5
  • 61
    • 84858222518 scopus 로고    scopus 로고
    • Protein secretion and surface display in Gram-positive bacteria
    • Schneewind O, Missiakas DM (2012) Protein secretion and surface display in Gram-positive bacteria. Philos Trans R Soc Lond B Biol Sci 367:1123-1139
    • (2012) Philos Trans R Soc Lond B Biol Sci , vol.367 , pp. 1123-1139
    • Schneewind, O.1    Missiakas, D.M.2
  • 62
    • 84856365560 scopus 로고    scopus 로고
    • An improved system for the surface immobilisation of proteins on Bacillus thuringiensis vegetative cells and spores through a new spore cortex-lytic enzyme anchor
    • Shao X, Ni H, Lu T, Jiang M, Li H, Huang X, Li L (2012) An improved system for the surface immobilisation of proteins on Bacillus thuringiensis vegetative cells and spores through a new spore cortex-lytic enzyme anchor. New Biotechnol 29:302-310
    • (2012) New Biotechnol , vol.29 , pp. 302-310
    • Shao, X.1    Ni, H.2    Lu, T.3    Jiang, M.4    Li, H.5    Huang, X.6    Li, L.7
  • 63
    • 84877826648 scopus 로고    scopus 로고
    • A Lysin motif (LysM)-containing protein functions in antibacterial responses of red swamp crayfish, Procambarus clarkii
    • Shi X-Z, Zhou J, Lan J-F, Jia Y-P, Zhao X-F, Wang J-X (2013) A Lysin motif (LysM)-containing protein functions in antibacterial responses of red swamp crayfish, Procambarus clarkii. Dev Comp Immunol 40:311-319
    • (2013) Dev Comp Immunol , vol.40 , pp. 311-319
    • Shi, X.-Z.1    Zhou, J.2    Lan, J.-F.3    Jia, Y.-P.4    Zhao, X.-F.5    Wang, J.-X.6
  • 65
    • 84877738556 scopus 로고    scopus 로고
    • Immobilization of nisin producer Lactococcus lactis strains to chitin with surface-displayed chitin-binding domain
    • Şimşek Ö, Sabanoǧlu S, Çon AH, Karasu N, Akçelik M, Saris PEJ (2013) Immobilization of nisin producer Lactococcus lactis strains to chitin with surface-displayed chitin-binding domain. Appl Microbiol Biotechnol 97:4577-4587
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 4577-4587
    • Şimşek, Ö.1    Sabanoǧlu, S.2    Çon, A.H.3    Karasu, N.4    Akçelik, M.5    Saris, P.E.J.6
  • 66
    • 20444471564 scopus 로고    scopus 로고
    • AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning
    • DOI 10.1111/j.1742-4658.2005.04706.x
    • Steen A, Buist G, Horsburgh GJ, Venema G, Kuipers OP, Foster SJ, Kok J (2005a) AcmA of Lactococcus lactis is an N-acetylglucosaminidase with an optimal number of LysM domains for proper functioning. FEBS J 272:2854-2868 (Pubitemid 40825430)
    • (2005) FEBS Journal , vol.272 , Issue.11 , 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
  • 70
    • 40749125219 scopus 로고    scopus 로고
    • Bidirectional Cell-Surface Anchoring Function of C-Terminal Repeat Region of Peptidoglycan Hydrolase of Lactococcus lactis IL1403
    • DOI 10.1263/jbb.105.116, PII S1389172308700379
    • Tarahomjoo S, Katakura Y, Satoh E, Shioya S (2008a) Bidirectional cell-surface anchoring function of C-terminal repeat region of peptidoglycan hydrolase of Lactococcus lactis IL1403. J Biosci Bioeng 105:116-121 (Pubitemid 351380992)
    • (2008) Journal of Bioscience and Bioengineering , vol.105 , Issue.2 , pp. 116-121
    • Tarahomjoo, S.1    Katakura, Y.2    Satoh, E.3    Shioya, S.4
  • 71
    • 40749093994 scopus 로고    scopus 로고
    • Expression of C-terminal Repeat Region of Peptidoglycan Hydrolase of Lactococcus lactis IL1403 in Methylotrophic Yeast Pichia pastoris
    • DOI 10.1263/jbb.105.134, PII S1389172308700409
    • Tarahomjoo S, Katakura Y, Shioya S (2008b) Expression of C-terminal repeat region of peptidoglycan hydrolase of Lactococcus lactis IL1403 in methylotrophic yeast Pichia pastoris. J Biosci Bioeng 105:134-139 (Pubitemid 351380994)
    • (2008) Journal of Bioscience and Bioengineering , vol.105 , Issue.2 , pp. 134-139
    • Tarahomjoo, S.1    Katakura, Y.2    Shioya, S.3
  • 72
    • 44949191449 scopus 로고    scopus 로고
    • New strategy for enhancement of microbial viability in simulated gastric conditions based on display of starch-binding domain on cell surface
    • DOI 10.1263/jbb.105.503, PII S1389172308701014
    • Tarahomjoo S, Katakura Y, Shioya S (2008c) New strategy for enhancement of microbial viability in simulated gastric conditions based on display of starch-binding domain on cell surface. J Biosci Bioeng 105:503-507 (Pubitemid 351815031)
    • (2008) Journal of Bioscience and Bioengineering , vol.105 , Issue.5 , pp. 503-507
    • Tarahomjoo, S.1    Katakura, Y.2    Shioya, S.3
  • 73
    • 84870502596 scopus 로고    scopus 로고
    • A bacteriophage endolysin-based electrochemical impedance biosensor for the rapid detection of Listeria cells
    • Tolba M, Ahmed MU, Tlili C, Eichenseher F, Loessner MJ, Zourob M (2012) A bacteriophage endolysin-based electrochemical impedance biosensor for the rapid detection of Listeria cells. Analyst 137:5749-5756
    • (2012) Analyst , vol.137 , pp. 5749-5756
    • Tolba, M.1    Ahmed, M.U.2    Tlili, C.3    Eichenseher, F.4    Loessner, M.J.5    Zourob, M.6
  • 75
    • 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
    • DOI 10.1128/AEM.70.6.3673-3680.2004
    • Turner MS, Hafner LM, Walsh T, Giffard PM (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 (Pubitemid 38745917)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.6 , pp. 3673-3680
    • Turner, M.S.1    Hafner, L.M.2    Walsh, T.3    Giffard, P.M.4
  • 76
    • 84886053974 scopus 로고    scopus 로고
    • Bacterium-like particles for efficient immune stimulation of existing vaccines and new subunit vaccines in mucosal applications
    • doi:10.3389/fimmu.2013.00282
    • Van Braeckel-Budimir N, Haijema BJ, Leenhouts K (2013) Bacterium-like particles for efficient immune stimulation of existing vaccines and new subunit vaccines in mucosal applications. Front Immunol 4:282. doi:10.3389/fimmu.2013. 00282
    • (2013) Front Immunol , vol.4 , pp. 282
    • Van Braeckel-Budimir, N.1    Haijema, B.J.2    Leenhouts, K.3
  • 81
    • 84876672120 scopus 로고    scopus 로고
    • The acid tolerant and cold-active β-galactosidase from Lactococcus lactis strain is an attractive biocatalyst for lactose hydrolysis
    • Vincent V, Aghajari N, Pollet N, Boisson A, Boudebbouze S, Haser R, Maguin E, Rhimi M (2013) The acid tolerant and cold-active β-galactosidase from Lactococcus lactis strain is an attractive biocatalyst for lactose hydrolysis. Antonie Van Leeuwenhoek 103:701-712
    • (2013) Antonie Van Leeuwenhoek , vol.103 , pp. 701-712
    • Vincent, V.1    Aghajari, N.2    Pollet, N.3    Boisson, A.4    Boudebbouze, S.5    Haser, R.6    Maguin, E.7    Rhimi, M.8
  • 82
    • 84867581104 scopus 로고    scopus 로고
    • A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material
    • Visweswaran GRR, Dijkstra BW, Kok J (2012) A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall material. Appl Microbiol Biotechnol 96:729-737
    • (2012) Appl Microbiol Biotechnol , vol.96 , pp. 729-737
    • Visweswaran, G.R.R.1    Dijkstra, B.W.2    Kok, J.3
  • 84
    • 39149110299 scopus 로고    scopus 로고
    • Peptidoglycan structure and architecture
    • DOI 10.1111/j.1574-6976.2007.00094.x
    • Vollmer W, Blanot D, de Pedro MA (2008a) Peptidoglycan structure and architecture. FEMS Microbiol Rev 32:149-167 (Pubitemid 351257814)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 149-167
    • Vollmer, W.1    Blanot, D.2    De Pedro, M.A.3
  • 85
    • 39149144016 scopus 로고    scopus 로고
    • Bacterial peptidoglycan (murein) hydrolases
    • DOI 10.1111/j.1574-6976.2007.00099.x
    • Vollmer W, Joris B, Charlier P, Foster S (2008b) Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiol Rev 32:259-286 (Pubitemid 351257818)
    • (2008) FEMS Microbiology Reviews , vol.32 , Issue.2 , pp. 259-286
    • Vollmer, W.1    Joris, B.2    Charlier, P.3    Foster, S.4
  • 86
    • 84865837379 scopus 로고    scopus 로고
    • LYK4, a lysin motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis
    • Wan J, Tanaka K, Zhang X-C, Son GH, Brechenmacher L, Nguyen THN, Stacey G (2012) LYK4, a lysin motif receptor-like kinase, is important for chitin signaling and plant innate immunity in Arabidopsis. Plant Physiol 160:396-406
    • (2012) Plant Physiol , vol.160 , pp. 396-406
    • Wan, J.1    Tanaka, K.2    Zhang, X.-C.3    Son, G.H.4    Brechenmacher, L.5    Nguyen, T.H.N.6    Stacey, G.7
  • 87
    • 84880897338 scopus 로고    scopus 로고
    • Novel methods for expression of foreign antigens in live vector vaccines
    • Wang JY, Harley RH, Galen JE (2013) Novel methods for expression of foreign antigens in live vector vaccines. Hum Vaccin Immunother 9:1558-1564
    • (2013) Hum Vaccin Immunother , vol.9 , pp. 1558-1564
    • Wang, J.Y.1    Harley, R.H.2    Galen, J.E.3
  • 88
    • 79960016255 scopus 로고    scopus 로고
    • Mucosal vaccination and therapy with genetically modified lactic acid bacteria
    • Wells J (2011) Mucosal vaccination and therapy with genetically modified lactic acid bacteria. Annu Rev Food Sci Technol 2:423-445
    • (2011) Annu Rev Food Sci Technol , vol.2 , pp. 423-445
    • Wells, J.1
  • 89
    • 81255154486 scopus 로고    scopus 로고
    • Novel surface display system for heterogonous proteins on Lactobacillus plantarum
    • Xu W, Huang M, Zhang Y, Yi X, Dong W, Gao X, Jia C (2011) Novel surface display system for heterogonous proteins on Lactobacillus plantarum. Lett Appl Microbiol 53:641-648
    • (2011) Lett Appl Microbiol , vol.53 , pp. 641-648
    • Xu, W.1    Huang, M.2    Zhang, Y.3    Yi, X.4    Dong, W.5    Gao, X.6    Jia, C.7
  • 90
    • 63049116700 scopus 로고    scopus 로고
    • NSOM- and AFM-based nanotechnology elucidates nano-structural and atomic-force features of a Y. pestis V immunogen-containing particle vaccine capable of eliciting robust response
    • Zeng G, Chen J, Zhong L, Wang R, Jiang L, Cai J, Yan L, Huang D, Chen CY, Chen ZW (2009) NSOM- and AFM-based nanotechnology elucidates nano-structural and atomic-force features of a Y. pestis V immunogen-containing particle vaccine capable of eliciting robust response. Proteomics 9:1538-1547
    • (2009) Proteomics , vol.9 , pp. 1538-1547
    • Zeng, G.1    Chen, J.2    Zhong, L.3    Wang, R.4    Jiang, L.5    Cai, J.6    Yan, L.7    Huang, D.8    Chen, C.Y.9    Chen, Z.W.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.