메뉴 건너뛰기




Volumn 8, Issue , 2009, Pages 48-

Surface display of heterologous proteins in Bacillus thuringiensis using a peptidoglycan hydrolase anchor

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; HYDROLASE; LYSINE; N ACETYL BETA GLUCOSAMINIDASE; OXIDOREDUCTASE; PEPTIDOGLYCAN HYDROLASE; PROTEIN CRY3AA; UNCLASSIFIED DRUG;

EID: 70449359790     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-8-48     Document Type: Article
Times cited : (22)

References (39)
  • 1
    • 0037178208 scopus 로고    scopus 로고
    • Display of proteins on bacteria
    • 10.1016/S0168-1656(02)00043-3, 12039531
    • Samuelson P, Gunneriusson E, Nygren PA, Stahl S. Display of proteins on bacteria. J Biotechnol 2002, 96(2):129-154. 10.1016/S0168-1656(02)00043-3, 12039531.
    • (2002) J Biotechnol , vol.96 , Issue.2 , pp. 129-154
    • Samuelson, P.1    Gunneriusson, E.2    Nygren, P.A.3    Stahl, S.4
  • 2
    • 0028820391 scopus 로고
    • How does Bacillus thuringiensis produce so much insecticidal crystal protein?
    • 177438, 7592363
    • Agaisse H, Lereclus D. How does Bacillus thuringiensis produce so much insecticidal crystal protein?. J Bacteriol 1995, 177(21):6027-6032. 177438, 7592363.
    • (1995) J Bacteriol , vol.177 , Issue.21 , pp. 6027-6032
    • Agaisse, H.1    Lereclus, D.2
  • 3
    • 22444443023 scopus 로고    scopus 로고
    • Insecticidal bacteria: an overwhelming success for invertebrate pathology
    • 10.1016/j.jip.2005.06.007, 16039303
    • Federici BA. Insecticidal bacteria: an overwhelming success for invertebrate pathology. J Invertebr Pathol 2005, 89(1):30-38. 10.1016/j.jip.2005.06.007, 16039303.
    • (2005) J Invertebr Pathol , vol.89 , Issue.1 , pp. 30-38
    • Federici, B.A.1
  • 4
    • 23044500836 scopus 로고    scopus 로고
    • Development and characterization of membrane surface display system using molecular chaperon, prsA, of Bacillus subtilis
    • 10.1016/j.bbrc.2005.07.024, 16051192
    • Kim JH, Park IS, Kim BG. Development and characterization of membrane surface display system using molecular chaperon, prsA, of Bacillus subtilis. Biochem Biophys Res Commun 2005, 334(4):1248-1253. 10.1016/j.bbrc.2005.07.024, 16051192.
    • (2005) Biochem Biophys Res Commun , vol.334 , Issue.4 , pp. 1248-1253
    • Kim, J.H.1    Park, I.S.2    Kim, B.G.3
  • 5
    • 0036192017 scopus 로고    scopus 로고
    • Simultaneous display of bacterial and fungal lipases on the cell surface of Bacillus subtilis
    • Kobayashi G, Fujii K, Serizawa M, Yamamoto H, Sekiguchi J. Simultaneous display of bacterial and fungal lipases on the cell surface of Bacillus subtilis. J Biosci Bioeng 2002, 93(1):15-19.
    • (2002) J Biosci Bioeng , vol.93 , Issue.1 , pp. 15-19
    • Kobayashi, G.1    Fujii, K.2    Serizawa, M.3    Yamamoto, H.4    Sekiguchi, J.5
  • 6
    • 0032774774 scopus 로고    scopus 로고
    • Cell surface-exposed tetanus toxin fragment C produced by recombinant Bacillus anthracis protects against tetanus toxin
    • 96818, 10456940
    • Mesnage S, Weber-Levy M, Haustant M, Mock M, Fouet A. Cell surface-exposed tetanus toxin fragment C produced by recombinant Bacillus anthracis protects against tetanus toxin. Infect Immun 1999, 67(9):4847-4850. 96818, 10456940.
    • (1999) Infect Immun , vol.67 , Issue.9 , pp. 4847-4850
    • Mesnage, S.1    Weber-Levy, M.2    Haustant, M.3    Mock, M.4    Fouet, A.5
  • 7
    • 46549085982 scopus 로고    scopus 로고
    • Displaying the protein of Mycoplasma gallisepticum agglutinin on the cell surface of Bacillus thuringiensis with the S-layer protein
    • 10.1016/j.vetmic.2007.12.007, 18243589
    • Liu M, Guo S, Hu S, Xiao Y, Xu Q, Li Z, Bi D, Sun M. Displaying the protein of Mycoplasma gallisepticum agglutinin on the cell surface of Bacillus thuringiensis with the S-layer protein. Vet Microbiol 2008, 130(1-2):99-106. 10.1016/j.vetmic.2007.12.007, 18243589.
    • (2008) Vet Microbiol , vol.130 , Issue.1-2 , pp. 99-106
    • Liu, M.1    Guo, S.2    Hu, S.3    Xiao, Y.4    Xu, Q.5    Li, Z.6    Bi, D.7    Sun, M.8
  • 8
    • 40549120122 scopus 로고    scopus 로고
    • Display of avian influenza virus nucleoprotein on Bacillus thuringiensis cell surface using CTC as a fusion partner
    • 10.1007/s00253-008-1345-1, 18236038
    • Liu M, Li S, Hu S, Zhao C, Bi D, Sun M. Display of avian influenza virus nucleoprotein on Bacillus thuringiensis cell surface using CTC as a fusion partner. Appl Microbiol Biotechnol 2008, 78(4):669-676. 10.1007/s00253-008-1345-1, 18236038.
    • (2008) Appl Microbiol Biotechnol , vol.78 , Issue.4 , pp. 669-676
    • Liu, M.1    Li, S.2    Hu, S.3    Zhao, C.4    Bi, D.5    Sun, M.6
  • 9
    • 20444396112 scopus 로고    scopus 로고
    • Surface display of recombinant proteins on Bacillus thuringiensis spores
    • 10.1128/AEM.71.6.3337-3341.2005, 1151829, 15933037
    • Du C, Chan WC, McKeithan TW, Nickerson KW. Surface display of recombinant proteins on Bacillus thuringiensis spores. Appl Environ Microbiol 2005, 71(6):3337-3341. 10.1128/AEM.71.6.3337-3341.2005, 1151829, 15933037.
    • (2005) Appl Environ Microbiol , vol.71 , Issue.6 , pp. 3337-3341
    • Du, C.1    Chan, W.C.2    McKeithan, T.W.3    Nickerson, K.W.4
  • 10
    • 27444433821 scopus 로고    scopus 로고
    • The autolytic phenotype of the Bacillus cereus group
    • 10.1111/j.1365-2672.2005.02713.x, 16238737
    • Raddadi N, Cherif A, Mora D, Brusetti L, Borin S, Boudabous A, Daffonchio D. The autolytic phenotype of the Bacillus cereus group. J Appl Microbiol 2005, 99(5):1070-1081. 10.1111/j.1365-2672.2005.02713.x, 16238737.
    • (2005) J Appl Microbiol , vol.99 , Issue.5 , pp. 1070-1081
    • Raddadi, N.1    Cherif, A.2    Mora, D.3    Brusetti, L.4    Borin, S.5    Boudabous, A.6    Daffonchio, D.7
  • 12
    • 0037930133 scopus 로고    scopus 로고
    • Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents
    • 10.1074/jbc.M211055200, 12684515
    • Steen A, Buist G, Leenhouts KJ, El Khattabi M, Grijpstra F, Zomer AL, Venema G, Kuipers OP, Kok J. Cell wall attachment of a widely distributed peptidoglycan binding domain is hindered by cell wall constituents. J Biol Chem 2003, 278(26):23874-23881. 10.1074/jbc.M211055200, 12684515.
    • (2003) J Biol Chem , vol.278 , Issue.26 , pp. 23874-23881
    • Steen, A.1    Buist, G.2    Leenhouts, K.J.3    El Khattabi, M.4    Grijpstra, F.5    Zomer, A.L.6    Venema, G.7    Kuipers, O.P.8    Kok, J.9
  • 14
    • 42549103340 scopus 로고    scopus 로고
    • LysM, a widely distributed protein motif for binding to (peptido)glycans
    • 10.1111/j.1365-2958.2008.06211.x, 18430080
    • Buist G, Steen A, Kok J, Kuipers OP. LysM, a widely distributed protein motif for binding to (peptido)glycans. Mol Microbiol 2008, 68(4):838-847. 10.1111/j.1365-2958.2008.06211.x, 18430080.
    • (2008) Mol Microbiol , vol.68 , Issue.4 , pp. 838-847
    • Buist, G.1    Steen, A.2    Kok, J.3    Kuipers, O.P.4
  • 15
    • 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
    • 10.1128/AEM.02012-07, 2258587, 18156338
    • Okano K, Zhang Q, Kimura S, Narita J, Tanaka T, Fukuda H, Kondo A. 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 2008, 74(4):1117-1123. 10.1128/AEM.02012-07, 2258587, 18156338.
    • (2008) Appl Environ Microbiol , 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
  • 16
    • 33646153514 scopus 로고    scopus 로고
    • Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations
    • 10.1016/j.vaccine.2006.02.040, 16545511
    • Ramasamy R, Yasawardena S, Zomer A, Venema G, Kok J, Leenhouts K. Immunogenicity of a malaria parasite antigen displayed by Lactococcus lactis in oral immunisations. Vaccine 2006, 24(18):3900-3908. 10.1016/j.vaccine.2006.02.040, 16545511.
    • (2006) Vaccine , vol.24 , Issue.18 , pp. 3900-3908
    • Ramasamy, R.1    Yasawardena, S.2    Zomer, A.3    Venema, G.4    Kok, J.5    Leenhouts, K.6
  • 17
    • 61849085824 scopus 로고    scopus 로고
    • Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A
    • 10.1371/journal.pone.0004658, 2646837, 19252736
    • Yin J, Li L, Shaw N, Li Y, Song JK, Zhang W, Xia C, Zhang R, Joachimiak A, Zhang HC. Structural basis and catalytic mechanism for the dual functional endo-beta-N-acetylglucosaminidase A. PLoS One 2009, 4(3):e4658. 10.1371/journal.pone.0004658, 2646837, 19252736.
    • (2009) PLoS One , vol.4 , Issue.3
    • Yin, J.1    Li, L.2    Shaw, N.3    Li, Y.4    Song, J.K.5    Zhang, W.6    Xia, C.7    Zhang, R.8    Joachimiak, A.9    Zhang, H.C.10
  • 18
    • 39149144016 scopus 로고    scopus 로고
    • Bacterial peptidoglycan (murein) hydrolases
    • 10.1111/j.1574-6976.2007.00099.x, 18266855
    • Vollmer W, Joris B, Charlier P, Foster S. Bacterial peptidoglycan (murein) hydrolases. FEMS Microbiol Rev 2008, 32(2):259-286. 10.1111/j.1574-6976.2007.00099.x, 18266855.
    • (2008) FEMS Microbiol Rev , vol.32 , Issue.2 , pp. 259-286
    • Vollmer, W.1    Joris, B.2    Charlier, P.3    Foster, S.4
  • 19
    • 0033950951 scopus 로고    scopus 로고
    • Autolysins of Bacillus subtilis : multiple enzymes with multiple functions
    • Smith TJ, Blackman SA, Foster SJ. Autolysins of Bacillus subtilis : multiple enzymes with multiple functions. Microbiology 2000, 146(Pt 2):249-262.
    • (2000) Microbiology , vol.146 , Issue.PART 2 , pp. 249-262
    • Smith, T.J.1    Blackman, S.A.2    Foster, S.J.3
  • 20
    • 61349134731 scopus 로고    scopus 로고
    • Deletion and site-directed mutagenesis of laccase from Shigella dysenteriae results in enhanced enzymatic activity and thermostability
    • Shao X, Gao Y, Jiang M, Li L. Deletion and site-directed mutagenesis of laccase from Shigella dysenteriae results in enhanced enzymatic activity and thermostability. Enzyme Microb Technol 2009, 44:274-280.
    • (2009) Enzyme Microb Technol , vol.44 , pp. 274-280
    • Shao, X.1    Gao, Y.2    Jiang, M.3    Li, L.4
  • 21
    • 70449355685 scopus 로고    scopus 로고
    • Softberry
    • Softberry. , http://linux1.softberry.com/berry.phtml
  • 22
    • 70449332344 scopus 로고    scopus 로고
    • PSORTb
    • PSORTb. , http://www.psort.org/psortb/
  • 23
    • 70449343307 scopus 로고    scopus 로고
    • SignalP
    • SignalP. , http://www.cbs.dtu.dk/services/SignalP/
  • 24
    • 0034674162 scopus 로고    scopus 로고
    • The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD)
    • 10.1006/jmbi.2000.3778, 10843862
    • Bateman A, Bycroft M. The structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD). J Mol Biol 2000, 299(4):1113-1119. 10.1006/jmbi.2000.3778, 10843862.
    • (2000) J Mol Biol , vol.299 , Issue.4 , pp. 1113-1119
    • Bateman, A.1    Bycroft, M.2
  • 25
    • 70449402308 scopus 로고    scopus 로고
    • PSIPRED
    • PSIPRED. , http://bioinf.cs.ucl.ac.uk/psipred/
  • 26
    • 0035793148 scopus 로고    scopus 로고
    • Display of green fluorescent protein on Escherichia coli cell surface
    • 10.1016/S0141-0229(00)00281-7, 11118595
    • Shi H, Wen Su W. Display of green fluorescent protein on Escherichia coli cell surface. Enzyme Microb Technol 2001, 28(1):25-34. 10.1016/S0141-0229(00)00281-7, 11118595.
    • (2001) Enzyme Microb Technol , vol.28 , Issue.1 , pp. 25-34
    • Shi, H.1    Wen Su, W.2
  • 27
    • 0942297855 scopus 로고    scopus 로고
    • Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein
    • 10.1002/bit.10892, 14705004
    • Li L, Kang DG, Cha HJ. Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein. Biotechnol Bioeng 2004, 85(2):214-221. 10.1002/bit.10892, 14705004.
    • (2004) Biotechnol Bioeng , vol.85 , Issue.2 , pp. 214-221
    • Li, L.1    Kang, D.G.2    Cha, H.J.3
  • 28
    • 33845946823 scopus 로고    scopus 로고
    • Protein secretion pathways in Bacillus subtilis : implication for optimization of heterologous protein secretion
    • 10.1016/j.biotechadv.2006.08.002, 16997527
    • Fu LL, Xu ZR, Li WF, Shuai JB, Lu P, Hu CX. Protein secretion pathways in Bacillus subtilis : implication for optimization of heterologous protein secretion. Biotechnol Adv 2007, 25(1):1-12. 10.1016/j.biotechadv.2006.08.002, 16997527.
    • (2007) Biotechnol Adv , vol.25 , Issue.1 , pp. 1-12
    • Fu, L.L.1    Xu, Z.R.2    Li, W.F.3    Shuai, J.B.4    Lu, P.5    Hu, C.X.6
  • 29
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis : a genome-based survey of the secretome
    • 10.1128/MMBR.64.3.515-547.2000, 99003, 10974125
    • Tjalsma H, Bolhuis A, Jongbloed JD, Bron S, van Dijl JM. Signal peptide-dependent protein transport in Bacillus subtilis : a genome-based survey of the secretome. Microbiol Mol Biol Rev 2000, 64(3):515-547. 10.1128/MMBR.64.3.515-547.2000, 99003, 10974125.
    • (2000) Microbiol Mol Biol Rev , vol.64 , Issue.3 , pp. 515-547
    • Tjalsma, H.1    Bolhuis, A.2    Jongbloed, J.D.3    Bron, S.4    van Dijl, J.M.5
  • 30
    • 0029058134 scopus 로고
    • Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168
    • 177106, 7601853
    • Smith TJ, Foster SJ. Characterization of the involvement of two compensatory autolysins in mother cell lysis during sporulation of Bacillus subtilis 168. J Bacteriol 1995, 177(13):3855-3862. 177106, 7601853.
    • (1995) J Bacteriol , vol.177 , Issue.13 , pp. 3855-3862
    • Smith, T.J.1    Foster, S.J.2
  • 31
    • 0026723753 scopus 로고
    • Genetic structure, isolation and characterization of a Bacillus licheniformis cell wall hydrolase
    • Kuroda A, Sugimoto Y, Funahashi T, Sekiguchi J. Genetic structure, isolation and characterization of a Bacillus licheniformis cell wall hydrolase. Mol Gen Genet 1992, 234(1):129-137.
    • (1992) Mol Gen Genet , vol.234 , Issue.1 , pp. 129-137
    • Kuroda, A.1    Sugimoto, Y.2    Funahashi, T.3    Sekiguchi, J.4
  • 32
    • 4544289558 scopus 로고    scopus 로고
    • Characterization of endo-beta-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125
    • 10.1271/bbb.68.1059, 15170110
    • Fujita K, Takami H, Yamamoto K, Takegawa K. Characterization of endo-beta-N-acetylglucosaminidase from alkaliphilic Bacillus halodurans C-125. Biosci Biotechnol Biochem 2004, 68(5):1059-1066. 10.1271/bbb.68.1059, 15170110.
    • (2004) Biosci Biotechnol Biochem , vol.68 , Issue.5 , pp. 1059-1066
    • Fujita, K.1    Takami, H.2    Yamamoto, K.3    Takegawa, K.4
  • 33
    • 0036968804 scopus 로고    scopus 로고
    • The structures and functions of ice crystal-controlling proteins from bacteria
    • Kawahara H. The structures and functions of ice crystal-controlling proteins from bacteria. J Biosci Bioeng 2002, 94(6):492-496.
    • (2002) J Biosci Bioeng , vol.94 , Issue.6 , pp. 492-496
    • Kawahara, H.1
  • 34
    • 34250810801 scopus 로고    scopus 로고
    • Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains
    • 10.1128/AEM.02628-06, 1932744, 17468268
    • Guillen D, Santiago M, Linares L, Perez R, Morlon J, Ruiz B, Sanchez S, Rodriguez-Sanoja R. Alpha-amylase starch binding domains: cooperative effects of binding to starch granules of multiple tandemly arranged domains. Appl Environ Microbiol 2007, 73(12):3833-3837. 10.1128/AEM.02628-06, 1932744, 17468268.
    • (2007) Appl Environ Microbiol , vol.73 , Issue.12 , pp. 3833-3837
    • Guillen, D.1    Santiago, M.2    Linares, L.3    Perez, R.4    Morlon, J.5    Ruiz, B.6    Sanchez, S.7    Rodriguez-Sanoja, R.8
  • 35
    • 2942752290 scopus 로고    scopus 로고
    • Improvement of cellulose-degrading ability of a yeast strain displaying Trichoderma reesei endoglucanase II by recombination of cellulose-binding domains
    • 10.1021/bp034332u, 15176869
    • Ito J, Fujita Y, Ueda M, Fukuda H, Kondo A. Improvement of cellulose-degrading ability of a yeast strain displaying Trichoderma reesei endoglucanase II by recombination of cellulose-binding domains. Biotechnol Prog 2004, 20(3):688-691. 10.1021/bp034332u, 15176869.
    • (2004) Biotechnol Prog , vol.20 , Issue.3 , pp. 688-691
    • Ito, J.1    Fujita, Y.2    Ueda, M.3    Fukuda, H.4    Kondo, A.5
  • 36
    • 0004136246 scopus 로고    scopus 로고
    • Molecular cloning: a laboratory manual
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y, 3
    • Sambrook J, Russell DW. Molecular cloning: a laboratory manual. 2001, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y, 3.
    • (2001)
    • Sambrook, J.1    Russell, D.W.2
  • 37
    • 0025824740 scopus 로고
    • Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene
    • 209238, 1682302
    • Kuroda A, Sekiguchi J. Molecular cloning and sequencing of a major Bacillus subtilis autolysin gene. J Bacteriol 1991, 173(22):7304-7312. 209238, 1682302.
    • (1991) J Bacteriol , vol.173 , Issue.22 , pp. 7304-7312
    • Kuroda, A.1    Sekiguchi, J.2
  • 38
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0, 5432063
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227(5259):680-685. 10.1038/227680a0, 5432063.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 39
    • 0025786601 scopus 로고
    • Construction of cloning vectors for Bacillus thuringiensis
    • 10.1016/0378-1119(91)90495-W, 1662180
    • Arantes O, Lereclus D. Construction of cloning vectors for Bacillus thuringiensis. Gene 1991, 108(1):115-119. 10.1016/0378-1119(91)90495-W, 1662180.
    • (1991) Gene , vol.108 , Issue.1 , pp. 115-119
    • Arantes, O.1    Lereclus, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.