메뉴 건너뛰기




Volumn 67, Issue 6, 2013, Pages 688-695

How are the non-classically secreted bacterial proteins released into the extracellular milieu?

Author keywords

[No Author keywords available]

Indexed keywords

AUTOLYSIN; BACTERIAL PROTEIN; CYTOPLASM PROTEIN; ENOLASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; NONCLASSICALLY SECRETED PROTEIN; PROTEIN SECA; PROTEIN SECA2; UNCLASSIFIED DRUG;

EID: 84886589440     PISSN: 03438651     EISSN: 14320991     Source Type: Journal    
DOI: 10.1007/s00284-013-0422-6     Document Type: Review
Times cited : (45)

References (65)
  • 1
    • 84860266041 scopus 로고    scopus 로고
    • Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli
    • 22433988 10.1016/j.biocel.2012.03.002 1:CAS:528:DC%2BC38XltVyjur4%3D
    • Aguilera L, Ferreira E, Giménez R, Fernández FJ, Taulés M, Aguilar J, Vega MC, Badia J, Baldomà L (2012) Secretion of the housekeeping protein glyceraldehyde-3-phosphate dehydrogenase by the LEE-encoded type III secretion system in enteropathogenic Escherichia coli. Int J Biochem Cell Biol 44(6):955-962
    • (2012) Int J Biochem Cell Biol , vol.44 , Issue.6 , pp. 955-962
    • Aguilera, L.1    Ferreira, E.2    Giménez, R.3    Fernández, F.J.4    Taulés, M.5    Aguilar, J.6    Vega, M.C.7    Badia, J.8    Baldomà, L.9
  • 2
    • 84872135257 scopus 로고    scopus 로고
    • Proteomic survey through secretome of Bacillus subtilis
    • 16929680 1:CAS:528:DC%2BD28XhtVOgtL%2FK
    • Antelmann H, Van Dijl JM, Bron S, Hecker M (2006) Proteomic survey through secretome of Bacillus subtilis. Methods Biochem Anal 49:179-208
    • (2006) Methods Biochem Anal , vol.49 , pp. 179-208
    • Antelmann, H.1    Van Dijl, J.M.2    Bron, S.3    Hecker, M.4
  • 3
    • 34250333853 scopus 로고    scopus 로고
    • PH dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids
    • 17449624 10.1128/JB.00378-07 1:CAS:528:DC%2BD2sXms1altbw%3D
    • Antikainen J, Kuparinen V, Lähteenmäki K, Korhonen TK (2007) pH dependent association of enolase and glyceraldehyde-3-phosphate dehydrogenase of Lactobacillus crispatus with the cell wall and lipoteichoic acids. J Bacteriol 189:4539-4543
    • (2007) J Bacteriol , vol.189 , pp. 4539-4543
    • Antikainen, J.1    Kuparinen, V.2    Lähteenmäki, K.3    Korhonen, T.K.4
  • 4
    • 35948951215 scopus 로고    scopus 로고
    • Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits
    • 17892475 10.1111/j.1574-695X.2007.00330.x 1:CAS:528:DC%2BD2sXhsVeit7rO
    • Antikainen J, Kuparinen V, Lähteenmäki K, Korhonen TK (2007) Enolases from Gram-positive bacterial pathogens and commensal lactobacilli share functional similarity in virulence-associated traits. FEMS Immunol Med Microbiol 51:526-534
    • (2007) FEMS Immunol Med Microbiol , vol.51 , pp. 526-534
    • Antikainen, J.1    Kuparinen, V.2    Lähteenmäki, K.3    Korhonen, T.K.4
  • 5
    • 0034462749 scopus 로고    scopus 로고
    • Catalase-peroxidases of Legionella pneumophila: Cloning of the katA gene and studies of KatA function
    • 11073912 10.1128/JB.182.23.6679-6686.2000 1:CAS:528:DC%2BD3MXitVCnu7k%3D
    • Bandyopadhyay P, Steinman HM (2000) Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function. J Bacteriol 182:6679-6686
    • (2000) J Bacteriol , vol.182 , pp. 6679-6686
    • Bandyopadhyay, P.1    Steinman, H.M.2
  • 9
    • 0034931519 scopus 로고    scopus 로고
    • Alpha enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface
    • 11442827 10.1046/j.1365-2958.2001.02448.x 1:CAS:528:DC%2BD3MXlt1Ggu7w%3D
    • Bergmann S, Rohde M, Chhatwal GS, Hammerschmidt S (2001) Alpha enolase of Streptococcus pneumoniae is a plasmin(ogen)-binding protein displayed on the bacterial cell surface. Mol Microbiol 40:1273-1287
    • (2001) Mol Microbiol , vol.40 , pp. 1273-1287
    • Bergmann, S.1    Rohde, M.2    Chhatwal, G.S.3    Hammerschmidt, S.4
  • 11
    • 25444529704 scopus 로고    scopus 로고
    • Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties
    • 16177295 10.1128/IAI.73.10.6237-6248.2005
    • Boël G, Jin H, Pancholi V (2005) Inhibition of cell surface export of group A streptococcal anchorless surface dehydrogenase affects bacterial adherence and antiphagocytic properties. Infect Immun 73:6237-6624
    • (2005) Infect Immun , vol.73 , pp. 6237-6624
    • Boël, G.1    Jin, H.2    Pancholi, V.3
  • 12
    • 0037673252 scopus 로고    scopus 로고
    • SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis
    • 12675804 10.1046/j.1365-2958.2003.03438.x 1:CAS:528:DC%2BD3sXjsVajtb4%3D
    • Braunstein M, Espinosa BJ, Chan J, Belisle JT, Jacobs WR Jr (2003) SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol Microbiol 48:453-464
    • (2003) Mol Microbiol , vol.48 , pp. 453-464
    • Braunstein, M.1    Espinosa, B.J.2    Chan, J.3    Belisle, J.T.4    Jacobs, Jr.W.R.5
  • 13
    • 77953221206 scopus 로고    scopus 로고
    • DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts
    • 20167618 10.1099/mic.0.038307-0 1:CAS:528:DC%2BC3cXptVehs7g%3D
    • Candela M, Centanni M, Fiori J, Biagi E, Turroni S, Orrico C, Bergmann S, Hammerschmidt S, Brigidi P (2010) DnaK from Bifidobacterium animalis subsp. lactis is a surface-exposed human plasminogen receptor upregulated in response to bile salts. Microbiology 156:1609-1618
    • (2010) Microbiology , vol.156 , pp. 1609-1618
    • Candela, M.1    Centanni, M.2    Fiori, J.3    Biagi, E.4    Turroni, S.5    Orrico, C.6    Bergmann, S.7    Hammerschmidt, S.8    Brigidi, P.9
  • 14
    • 84862827384 scopus 로고    scopus 로고
    • Analysis of Streptococcus pneumoniae secreted antigens by immuno-proteomic approach
    • 22306351 10.1016/j.diagmicrobio.2011.12.013 1:CAS:528: DC%2BC38Xktleqtr4%3D
    • Choi CW, Lee YG, Kwon SO, Kim HY, Lee JC, Chung YH, Yun CY, Kim SI (2012) Analysis of Streptococcus pneumoniae secreted antigens by immuno-proteomic approach. Diagn Microbiol Infect Dis 72(4):318-327
    • (2012) Diagn Microbiol Infect Dis , vol.72 , Issue.4 , pp. 318-327
    • Choi, C.W.1    Lee, Y.G.2    Kwon, S.O.3    Kim, H.Y.4    Lee, J.C.5    Chung, Y.H.6    Yun, C.Y.7    Kim, S.I.8
  • 15
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: A semantic awareness issue
    • 19299134 10.1016/j.tim.2009.01.004 1:CAS:528:DC%2BD1MXkt1SktL0%3D
    • Desvaux M, Hébraud M, Talon R, Henderson IR (2009) Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol 17(4):139-145
    • (2009) Trends Microbiol , vol.17 , Issue.4 , pp. 139-145
    • Desvaux, M.1    Hébraud, M.2    Talon, R.3    Henderson, I.R.4
  • 16
    • 77957352841 scopus 로고    scopus 로고
    • Comprehensive appraisal of the extracellular proteins from a monoderm bacterium: Theoretical and empirical exoproteomes of Listeria monocytogenes EGD-e by secretomics
    • 20839850 10.1021/pr1003642 1:CAS:528:DC%2BC3cXhtFGrurzE
    • Desvaux M, Dumas E, Chafsey I, Chambon C, Hébraud M (2010) Comprehensive appraisal of the extracellular proteins from a monoderm bacterium: theoretical and empirical exoproteomes of Listeria monocytogenes EGD-e by secretomics. J Proteome Res 9(10):5076-5092
    • (2010) J Proteome Res , vol.9 , Issue.10 , pp. 5076-5092
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Chambon, C.4    Hébraud, M.5
  • 17
    • 77956120742 scopus 로고    scopus 로고
    • Profiling the surfacome of Staphylococcus aureus
    • 20662103 10.1002/pmic.201000062 1:CAS:528:DC%2BC3cXhtV2gsbrO
    • Dreisbach A, Hempel K, Buist G, Hecker M, Becher D, van Dijl JM (2010) Profiling the surfacome of Staphylococcus aureus. Proteomics 10:3082-3096
    • (2010) Proteomics , vol.10 , pp. 3082-3096
    • Dreisbach, A.1    Hempel, K.2    Buist, G.3    Hecker, M.4    Becher, D.5    Van Dijl, J.M.6
  • 18
    • 0029967327 scopus 로고    scopus 로고
    • Iron starvation causes release from the group A streptococcus of the ADP-ribosylating protein called plasmin receptor or surface glyceraldehyde-3- phosphate-dehydrogenase
    • 8675293 1:CAS:528:DyaK28Xjt1OqtL4%3D
    • Eichenbaum Z, Green BD, Scott JR (1996) Iron starvation causes release from the group A streptococcus of the ADP-ribosylating protein called plasmin receptor or surface glyceraldehyde-3-phosphate-dehydrogenase. Infect Immun 64:1956-1960
    • (1996) Infect Immun , vol.64 , pp. 1956-1960
    • Eichenbaum, Z.1    Green, B.D.2    Scott, J.R.3
  • 19
    • 25844455216 scopus 로고    scopus 로고
    • A comparative study of Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis extracellular proteomes
    • 16167365 10.1002/pmic.200401225 1:CAS:528:DC%2BD2MXhtVygtLjE
    • Gohar M, Gilois N, Graveline R, Garreau C, Sanchis V, Lereclus D (2005) A comparative study of Bacillus cereus, Bacillus thuringiensis and Bacillus anthracis extracellular proteomes. Proteomics 5:3696-3711
    • (2005) Proteomics , vol.5 , pp. 3696-3711
    • Gohar, M.1    Gilois, N.2    Graveline, R.3    Garreau, C.4    Sanchis, V.5    Lereclus, D.6
  • 20
    • 0030928121 scopus 로고    scopus 로고
    • Expression and efficient export of enzymatically active Mycobacterium tuberculosis glutamine synthetase in Mycobacterium smegmatis and evidence that the information for export is contained within the protein
    • 9278431 10.1074/jbc.272.36.22728 1:CAS:528:DyaK2sXlvFGitbY%3D
    • Harth G, Horwitz MA (1997) Expression and efficient export of enzymatically active Mycobacterium tuberculosis glutamine synthetase in Mycobacterium smegmatis and evidence that the information for export is contained within the protein. J Biol Chem 272:22728-22735
    • (1997) J Biol Chem , vol.272 , pp. 22728-22735
    • Harth, G.1    Horwitz, M.A.2
  • 21
    • 0033548095 scopus 로고    scopus 로고
    • Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria
    • 9933629 10.1074/jbc.274.7.4281 1:CAS:528:DyaK1MXhslags70%3D
    • Harth G, Horwitz MA (1999) Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria. J Biol Chem 274:4281-4292
    • (1999) J Biol Chem , vol.274 , pp. 4281-4292
    • Harth, G.1    Horwitz, M.A.2
  • 22
    • 80052329723 scopus 로고    scopus 로고
    • Bacterial virulence in the moonlight: Multitasking bacterial moonlighting proteins are virulence determinants in infectious disease
    • 21646455 10.1128/IAI.00179-11 1:CAS:528:DC%2BC3MXhtFSqt77M
    • Henderson B, Martin A (2011) Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious disease. Infect Immun 79:3476-3491
    • (2011) Infect Immun , vol.79 , pp. 3476-3491
    • Henderson, B.1    Martin, A.2
  • 24
    • 62949096122 scopus 로고    scopus 로고
    • Moonlighting proteins-an update
    • 19396370 10.1039/b900658n 1:CAS:528:DC%2BD1MXjt1Kms7k%3D
    • Jeffery CJ (2009) Moonlighting proteins-an update. Mol BioSyst 5:345-350
    • (2009) Mol BioSyst , vol.5 , pp. 345-350
    • Jeffery, C.J.1
  • 25
    • 77954368576 scopus 로고    scopus 로고
    • Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates
    • 20497499 10.1111/j.1365-2958.2010.07227.x 1:CAS:528:DC%2BC3cXpsl2jtro%3D
    • Jers C, Pedersen MM, Paspaliari DK, Schütz W, Johnsson C, Soufi B, Macek B, Jensen PR, Mijakovic I (2010) Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates. Mol Microbiol 77(2):287-299
    • (2010) Mol Microbiol , vol.77 , Issue.2 , pp. 287-299
    • Jers, C.1    Pedersen, M.M.2    Paspaliari, D.K.3    Schütz, W.4    Johnsson, C.5    Soufi, B.6    MacEk, B.7    Jensen, P.R.8    Mijakovic, I.9
  • 26
    • 84861361412 scopus 로고    scopus 로고
    • Glutamine synthetase and glucose-6-phosphate isomerase are adhesive moonlighting proteins of Lactobacillus crispatus released by epithelial cathelicidin LL-37
    • 22389474 10.1128/JB.06704-11 1:CAS:528:DC%2BC38XmslOnsrs%3D
    • Kainulainen V, Loimaranta V, Pekkala A, Edelman S, Antikainen J, Kylväjä R, Laaksonen M, Laakkonen L, Finne J, Korhonen TK (2012) Glutamine synthetase and glucose-6-phosphate isomerase are adhesive moonlighting proteins of Lactobacillus crispatus released by epithelial cathelicidin LL-37. J Bacteriol 194(10):2509-2519
    • (2012) J Bacteriol , vol.194 , Issue.10 , pp. 2509-2519
    • Kainulainen, V.1    Loimaranta, V.2    Pekkala, A.3    Edelman, S.4    Antikainen, J.5    Kylväjä, R.6    Laaksonen, M.7    Laakkonen, L.8    Finne, J.9    Korhonen, T.K.10
  • 27
    • 77149147111 scopus 로고    scopus 로고
    • Lactic acid bacteria display on the cell surface cytosolic proteins that recognize yeast mannan
    • 19898842 10.1007/s00253-009-2295-y 1:CAS:528:DC%2BC3cXhvFKnsr0%3D
    • Katakura Y, Sano R, Hashimoto T, Ninomiya K, Shioya S (2010) Lactic acid bacteria display on the cell surface cytosolic proteins that recognize yeast mannan. Appl Microbiol Biotechnol 86(1):319-326
    • (2010) Appl Microbiol Biotechnol , vol.86 , Issue.1 , pp. 319-326
    • Katakura, Y.1    Sano, R.2    Hashimoto, T.3    Ninomiya, K.4    Shioya, S.5
  • 28
    • 61349135377 scopus 로고    scopus 로고
    • MscL of Bacillus subtilis prevents selective release of cytoplasmic proteins in a hypotonic environment
    • 19160392 10.1002/pmic.200800483 1:CAS:528:DC%2BD1MXjt12nsLw%3D
    • Kouwen TR, Antelmann H, van der Ploeg R, Denham EL, Hecker M, van Dijl JM (2009) MscL of Bacillus subtilis prevents selective release of cytoplasmic proteins in a hypotonic environment. Proteomics 9(4):1033-1043
    • (2009) Proteomics , vol.9 , Issue.4 , pp. 1033-1043
    • Kouwen, T.R.1    Antelmann, H.2    Van Der Ploeg, R.3    Denham, E.L.4    Hecker, M.5    Van Dijl, J.M.6
  • 29
    • 0024352026 scopus 로고
    • Cloning of the flagellin gene from Bacillus subtilis and complementation studies of an in vitro-derived deletion mutation
    • 2498283 1:CAS:528:DyaK3cXhtFaqtbY%3D
    • LaVallie ER, Stahl ML (1989) Cloning of the flagellin gene from Bacillus subtilis and complementation studies of an in vitro-derived deletion mutation. J Bacteriol 171(6):3085-3094
    • (1989) J Bacteriol , vol.171 , Issue.6 , pp. 3085-3094
    • Lavallie, E.R.1    Stahl, M.L.2
  • 31
    • 0034442652 scopus 로고    scopus 로고
    • Identification and immunogenicity of group A streptococcus culture supernatant proteins
    • 11083799 10.1128/IAI.68.12.6807-6818.2000 1:CAS:528:DC%2BD3MXjslCktLs%3D
    • Lei B, Mackie S, Lukomski S, Musser JM (2000) Identification and immunogenicity of group A streptococcus culture supernatant proteins. Infect Immun 68:6807-6818
    • (2000) Infect Immun , vol.68 , pp. 6807-6818
    • Lei, B.1    MacKie, S.2    Lukomski, S.3    Musser, J.M.4
  • 32
    • 0142091351 scopus 로고    scopus 로고
    • SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis
    • 14527997 10.1073/pnas.2133653100 1:CAS:528:DC%2BD3sXotlGktr4%3D
    • Lenz LL, Mohammadi S, Geissler A, Portnoy DA (2003) SecA2-dependent secretion of autolytic enzymes promotes Listeria monocytogenes pathogenesis. Proc Natl Acad Sci USA 100:12432-12437
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 12432-12437
    • Lenz, L.L.1    Mohammadi, S.2    Geissler, A.3    Portnoy, D.A.4
  • 33
    • 8144221393 scopus 로고    scopus 로고
    • Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse
    • 15498039 10.1111/j.1365-2249.2004.02628.x 1:CAS:528:DC%2BD2cXhtVaksbrJ
    • Ling E, Feldman G, Portnoi M, Dagan R, Overweg K, Mulholland F, Chalifa-Caspi V, Wells J, Mizrachi-Nebenzahl Y (2004) Glycolytic enzymes associated with the cell surface of Streptococcus pneumoniae are antigenic in humans and elicit protective immune responses in the mouse. Clin Exp Immunol 138(2):290-298
    • (2004) Clin Exp Immunol , vol.138 , Issue.2 , pp. 290-298
    • Ling, E.1    Feldman, G.2    Portnoi, M.3    Dagan, R.4    Overweg, K.5    Mulholland, F.6    Chalifa-Caspi, V.7    Wells, J.8    Mizrachi-Nebenzahl, Y.9
  • 34
    • 0028789409 scopus 로고
    • Bacillus subtilis vegetative catalase is an extracellular enzyme
    • 16535198 1:CAS:528:DyaK2MXpslCmtL0%3D
    • Naclerio G, Baccigalupi L, Caruso C, De Felice M, Ricca E (1995) Bacillus subtilis vegetative catalase is an extracellular enzyme. Appl Environ Microbiol 61(12):4471-4473
    • (1995) Appl Environ Microbiol , vol.61 , Issue.12 , pp. 4471-4473
    • Naclerio, G.1    Baccigalupi, L.2    Caruso, C.3    De Felice, M.4    Ricca, E.5
  • 35
    • 33646550516 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Escherichia coli W3110
    • 16674104 10.1021/pr050401j 1:CAS:528:DC%2BD28XjtlWgsL4%3D
    • Nandakumar MP, Cheung A, Marten MR (2006) Proteomic analysis of extracellular proteins from Escherichia coli W3110. J Proteome Res 5:1155-1161
    • (2006) J Proteome Res , vol.5 , pp. 1155-1161
    • Nandakumar, M.P.1    Cheung, A.2    Marten, M.R.3
  • 36
    • 0034986066 scopus 로고    scopus 로고
    • PH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: Purification, characterization, and cloning of the gene encoding this enzyme
    • 11269731 10.1177/00220345010800011301 1:CAS:528:DC%2BD3MXivVOmtL4%3D
    • Nelson D, Goldstein JM, Boatright K, Harty DW, Cook SL, Hickman PJ, Potempa J, Travis J, Mayo JA (2001) pH-regulated secretion of a glyceraldehyde-3-phosphate dehydrogenase from Streptococcus gordonii FSS2: purification, characterization, and cloning of the gene encoding this enzyme. J Dent Res 80:371-377
    • (2001) J Dent Res , vol.80 , pp. 371-377
    • Nelson, D.1    Goldstein, J.M.2    Boatright, K.3    Harty, D.W.4    Cook, S.L.5    Hickman, P.J.6    Potempa, J.7    Travis, J.8    Mayo, J.A.9
  • 37
    • 0038701886 scopus 로고    scopus 로고
    • The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes
    • 12752430 10.1046/j.1432-1033.2003.03577.x 1:CAS:528:DC%2BD3sXjvFOrtr8%3D
    • Nickel W (2003) The mystery of nonclassical protein secretion. A current view on cargo proteins and potential export routes. Eur J Biochem 270(10):2109-2119
    • (2003) Eur J Biochem , vol.270 , Issue.10 , pp. 2109-2119
    • Nickel, W.1
  • 38
    • 84856120822 scopus 로고    scopus 로고
    • Group B streptococcus GAPDH is released upon cell lysis, associates with bacterial surface, and induces apoptosis in murine macrophages
    • 22291899 10.1371/journal.pone.0029963 1:CAS:528:DC%2BC38Xit1ChsLk%3D
    • Oliveira L, Madureira P, Andrade EB, Bouaboud A, Morello E, Ferreira P, Poyart C, Trieu-Cuot P, Dramsi S (2012) Group B streptococcus GAPDH is released upon cell lysis, associates with bacterial surface, and induces apoptosis in murine macrophages. PLoS ONE 7(1):e29963
    • (2012) PLoS ONE , vol.7 , Issue.1 , pp. 29963
    • Oliveira, L.1    Madureira, P.2    Andrade, E.B.3    Bouaboud, A.4    Morello, E.5    Ferreira, P.6    Poyart, C.7    Trieu-Cuot, P.8    Dramsi, S.9
  • 40
    • 0036568776 scopus 로고    scopus 로고
    • The ESTA-6/WXG100 superfamily - And a new gram-positive secretion system?
    • 11973144 10.1016/S0966-842X(02)02345-4 1:CAS:528:DC%2BD38XjsFGntrc%3D
    • Pallen MJ (2002) The ESTA-6/WXG100 superfamily - and a new gram-positive secretion system? Trends Microbiol 10(5):209-212
    • (2002) Trends Microbiol , vol.10 , Issue.5 , pp. 209-212
    • Pallen, M.J.1
  • 41
    • 0347753321 scopus 로고    scopus 로고
    • Housekeeping enzymes as virulence factors for pathogens
    • 14760970 10.1078/1438-4221-00283 1:CAS:528:DC%2BD2cXitVejt7k%3D
    • Pancholi V, Chhatwal GS (2003) Housekeeping enzymes as virulence factors for pathogens. Int J Med Microbiol 293:391-401
    • (2003) Int J Med Microbiol , vol.293 , pp. 391-401
    • Pancholi, V.1    Chhatwal, G.S.2
  • 43
    • 84875093430 scopus 로고    scopus 로고
    • Protein-phospholipid interactions in nonclassical protein secretion: Problem and methods of study
    • 23396106 10.3390/ijms14023734 1:CAS:528:DC%2BC3sXjtFKhtLw%3D
    • Prudovsky I, Kumar TK, Sterling S, Neivandt D (2013) Protein-phospholipid interactions in nonclassical protein secretion: problem and methods of study. Int J Mol Sci 14(2):3734-3772
    • (2013) Int J Mol Sci , vol.14 , Issue.2 , pp. 3734-3772
    • Prudovsky, I.1    Kumar, T.K.2    Sterling, S.3    Neivandt, D.4
  • 44
    • 84865035715 scopus 로고    scopus 로고
    • Subcellular localization of extracytoplasmic proteins in monoderm bacteria: Rational secretomics-based strategy for genomic and proteomic analyses
    • 22912771 10.1371/journal.pone.0042982 1:CAS:528:DC%2BC38Xht1Srs7vE
    • Renier S, Micheau P, Talon R, Hébraud M, Desvaux M (2012) Subcellular localization of extracytoplasmic proteins in monoderm bacteria: rational secretomics-based strategy for genomic and proteomic analyses. PLoS One 7(8):e42982
    • (2012) PLoS One , vol.7 , Issue.8 , pp. 42982
    • Renier, S.1    Micheau, P.2    Talon, R.3    Hébraud, M.4    Desvaux, M.5
  • 45
    • 0030716878 scopus 로고    scopus 로고
    • The ins and outs of protein translocation
    • 9411792 10.1126/science.278.5344.1728 1:CAS:528:DyaK2sXnvFCns7s%3D
    • Riezman H (1997) The ins and outs of protein translocation. Science 278:1728-1729
    • (1997) Science , vol.278 , pp. 1728-1729
    • Riezman, H.1
  • 46
    • 47249140823 scopus 로고    scopus 로고
    • A new twist on an old pathway-accessory Sec systems
    • 18544071 10.1111/j.1365-2958.2008.06294.x 1:CAS:528:DC%2BD1cXoslyjsbg%3D
    • Rigel NW, Braunstein M (2008) A new twist on an old pathway-accessory Sec systems. Mol Microbiol 69(2):291-302
    • (2008) Mol Microbiol , vol.69 , Issue.2 , pp. 291-302
    • Rigel, N.W.1    Braunstein, M.2
  • 47
    • 0034031272 scopus 로고    scopus 로고
    • Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection
    • 10768780 10.1002/(SICI)1522-2683(20000301)21:5<935: AID-ELPS935>3.0.CO;2-P 1:CAS:528:DC%2BD3cXisVWhtbY%3D
    • Rosenkrands I, Weldingh K, Jacobsen S, Hansen CV, Florio W, Gianetri I, Andersen P (2000) Mapping and identification of Mycobacterium tuberculosis proteins by two-dimensional gel electrophoresis, microsequencing and immunodetection. Electrophoresis 21(5):935-948
    • (2000) Electrophoresis , vol.21 , Issue.5 , pp. 935-948
    • Rosenkrands, I.1    Weldingh, K.2    Jacobsen, S.3    Hansen, C.V.4    Florio, W.5    Gianetri, I.6    Andersen, P.7
  • 48
    • 0036285253 scopus 로고    scopus 로고
    • Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins
    • 12057942 10.1128/JB.184.13.3485-3491.2002 1:CAS:528:DC%2BD38XkslyrsL0%3D
    • Rosenkrands I, Slayden RA, Crawford J, Aagaard C, Barry CE 3rd, Andersen P (2002) Hypoxic response of Mycobacterium tuberculosis studied by metabolic labeling and proteome analysis of cellular and extracellular proteins. J Bacteriol 184(13):3485-3491
    • (2002) J Bacteriol , vol.184 , Issue.13 , pp. 3485-3491
    • Rosenkrands, I.1    Slayden, R.A.2    Crawford, J.3    Aagaard, C.4    Barry III, C.E.5    Andersen, P.6
  • 49
    • 74749109630 scopus 로고    scopus 로고
    • Lactobacillus plantarum 299v surface-bound GAPDH: A new insight into enzyme cell walls location
    • 20075631 10.4014/jmb.0902.0102 1:CAS:528:DC%2BC3cXhtF2ks7g%3D
    • Saad N, Urdaci M, Vignoles C, Chaignepain S, Tallon R, Schmitter JM, Bressollier P (2009) Lactobacillus plantarum 299v surface-bound GAPDH: a new insight into enzyme cell walls location. J Microbiol Biotechnol 19:1635-1643
    • (2009) J Microbiol Biotechnol , vol.19 , pp. 1635-1643
    • Saad, N.1    Urdaci, M.2    Vignoles, C.3    Chaignepain, S.4    Tallon, R.5    Schmitter, J.M.6    Bressollier, P.7
  • 50
    • 56749163205 scopus 로고    scopus 로고
    • Identification of surface-associated proteins in the probiotic bacterium Lactobacillus rhamnosus GG
    • 10.1016/j.idairyj.2008.09.005
    • Sánchez B, Bressollier P, Chaignepain S, Schmitter JM, Urdaci MC (2009) Identification of surface-associated proteins in the probiotic bacterium Lactobacillus rhamnosus GG. Int Dairy J 19(2):85-88
    • (2009) Int Dairy J , vol.19 , Issue.2 , pp. 85-88
    • Sánchez, B.1    Bressollier, P.2    Chaignepain, S.3    Schmitter, J.M.4    Urdaci, M.C.5
  • 51
    • 0029979607 scopus 로고    scopus 로고
    • Common principles of protein translocation across membranes
    • 8599107 10.1126/science.271.5255.1519 1:CAS:528:DyaK28XhslSjsLo%3D
    • Schatz G, Dobberstein B (1996) Common principles of protein translocation across membranes. Science 271:1519-1526
    • (1996) Science , vol.271 , pp. 1519-1526
    • Schatz, G.1    Dobberstein, B.2
  • 53
    • 33750319466 scopus 로고    scopus 로고
    • Surface proteins of gram-positive bacteria and how they get there
    • 16753030 10.1146/annurev.micro.60.080805.142256 1:CAS:528: DC%2BD28Xht1Whtb3N
    • Scott JR, Barnett TC (2006) Surface proteins of gram-positive bacteria and how they get there. Annu Rev Microbiol 60:397-423
    • (2006) Annu Rev Microbiol , vol.60 , pp. 397-423
    • Scott, J.R.1    Barnett, T.C.2
  • 56
    • 84866321497 scopus 로고    scopus 로고
    • Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysisof a mycobacterial lgt mutant
    • 22609911 10.1128/JB.00127-12 1:CAS:528:DC%2BC38XhtV2ht7bE
    • Tschumi A, Grau T, Albrecht D, Rezwan M, Antelmann H, Sander P (2012) Functional analyses of mycobacterial lipoprotein diacylglyceryl transferase and comparative secretome analysisof a mycobacterial lgt mutant. J Bacteriol 194(15):3938-3949
    • (2012) J Bacteriol , vol.194 , Issue.15 , pp. 3938-3949
    • Tschumi, A.1    Grau, T.2    Albrecht, D.3    Rezwan, M.4    Antelmann, H.5    Sander, P.6
  • 57
    • 0034819306 scopus 로고    scopus 로고
    • High extracellular levels of Mycobacterium tuberculosis glutamine synthetase and superoxide dismutase in actively growing cultures are due to high expression and extracellular stability rather than to a protein-specific export mechanism
    • 11553579 10.1128/IAI.69.10.6348-6363.2001 1:CAS:528:DC%2BD3MXntFCjt78%3D
    • Tullius MV, Harth G, Horwitz MA (2001) High extracellular levels of Mycobacterium tuberculosis glutamine synthetase and superoxide dismutase in actively growing cultures are due to high expression and extracellular stability rather than to a protein-specific export mechanism. Infect Immun 69(10):6348-6363
    • (2001) Infect Immun , vol.69 , Issue.10 , pp. 6348-6363
    • Tullius, M.V.1    Harth, G.2    Horwitz, M.A.3
  • 58
    • 0031911053 scopus 로고    scopus 로고
    • Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins
    • 9488391 1:CAS:528:DyaK1cXhtlSkur8%3D
    • Vanet A, Labigne A (1998) Evidence for specific secretion rather than autolysis in the release of some Helicobacter pylori proteins. Infect Immun 66(3):1023-1027
    • (1998) Infect Immun , vol.66 , Issue.3 , pp. 1023-1027
    • Vanet, A.1    Labigne, A.2
  • 59
    • 2442446271 scopus 로고    scopus 로고
    • Structure function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis
    • 14976191 10.1074/jbc.M400861200 1:CAS:528:DC%2BD2cXjsVKmurY%3D
    • Vitikainen M, Lappalainen I, Seppala R, Antelmann H, Boer H, Taira S, Savilahti H, Hecker M, Vihinen M, Sarvas M, Kontinen VP (2004) Structure function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis. J Biol Chem 279:19302-19314
    • (2004) J Biol Chem , vol.279 , pp. 19302-19314
    • Vitikainen, M.1    Lappalainen, I.2    Seppala, R.3    Antelmann, H.4    Boer, H.5    Taira, S.6    Savilahti, H.7    Hecker, M.8    Vihinen, M.9    Sarvas, M.10    Kontinen, V.P.11
  • 60
    • 0025183758 scopus 로고
    • Protein targeting signals
    • 10.1016/0955-0674(90)90100-S
    • von Heijne G (1990) Protein targeting signals. Curr Oppin Cell Biol 2:604-608
    • (1990) Curr Oppin Cell Biol , vol.2 , pp. 604-608
    • Von Heijne, G.1
  • 61
    • 0032511879 scopus 로고    scopus 로고
    • Life and death of a signal peptide
    • 10.1038/24036
    • von Heijne G (1998) Life and death of a signal peptide. Nature 396:111-113
    • (1998) Nature , vol.396 , pp. 111-113
    • Von Heijne, G.1
  • 63
    • 44649118664 scopus 로고    scopus 로고
    • Comparison of the extracellular proteomes of Escherichia coli B and K-12 strains during high cell density cultivation
    • 18425732 10.1002/pmic.200700826 1:CAS:528:DC%2BD1cXmvFWktbs%3D
    • Xia XX, Han MJ, Lee SY, Yoo JS (2008) Comparison of the extracellular proteomes of Escherichia coli B and K-12 strains during high cell density cultivation. Proteomics 8(10):2089-2103
    • (2008) Proteomics , vol.8 , Issue.10 , pp. 2089-2103
    • Xia, X.X.1    Han, M.J.2    Lee, S.Y.3    Yoo, J.S.4
  • 64
    • 80053578297 scopus 로고    scopus 로고
    • Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis
    • 21856851 10.1128/JB.05897-11 1:CAS:528:DC%2BC3MXhtlWitbzJ
    • Yang CK, Ewis HE, Zhang X, Lu CD, Hu HJ, Pan Y, Abdelal AT, Tai PC (2011) Nonclassical protein secretion by Bacillus subtilis in the stationary phase is not due to cell lysis. J Bacteriol 193:5607-5615
    • (2011) J Bacteriol , vol.193 , pp. 5607-5615
    • Yang, C.K.1    Ewis, H.E.2    Zhang, X.3    Lu, C.D.4    Hu, H.J.5    Pan, Y.6    Abdelal, A.T.7    Tai, P.C.8
  • 65
    • 5644280025 scopus 로고    scopus 로고
    • The influence of agr and sigma B in growth phase dependent regulation of virulence factors in Staphylococcus aureus
    • 15378746 10.1002/pmic.200400937 1:CAS:528:DC%2BD2cXovVyntrs%3D
    • Ziebandt AK, Becher D, Ohlsen K, Hacker J, Hecker M, Engelmann S (2004) The influence of agr and sigma B in growth phase dependent regulation of virulence factors in Staphylococcus aureus. Proteomics 4(10):3034-3047
    • (2004) Proteomics , vol.4 , Issue.10 , pp. 3034-3047
    • Ziebandt, A.K.1    Becher, D.2    Ohlsen, K.3    Hacker, J.4    Hecker, M.5    Engelmann, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.