메뉴 건너뛰기




Volumn 2, Issue JULY, 2011, Pages

Protein secretion systems in Pseudomonas aeruginosa: An essay on diversity, evolution, and function

Author keywords

Cell envelope; Channel; Macromolecular complex; Nanomachine; Targeting

Indexed keywords

BACTERIA (MICROORGANISMS); EUKARYOTA; NEGIBACTERIA; PSEUDOMONAS AERUGINOSA;

EID: 84864578935     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2011.00155     Document Type: Review
Times cited : (140)

References (250)
  • 1
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a Type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
    • Agrain, C., Callebaut, I., Journet, L., Sorg, I., Paroz, C., Mota, L. J., and Cornelis, G. R. (2005). Characterization of a Type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol. Microbiol. 56, 54-67.
    • (2005) Mol. Microbiol. , vol.56 , pp. 54-67
    • Agrain, C.1    Callebaut, I.2    Journet, L.3    Sorg, I.4    Paroz, C.5    Mota, L.J.6    Cornelis, G.R.7
  • 3
    • 0027436744 scopus 로고
    • Tommassen, J., Teerink, H., Filloux, A., and Lazdunski, A
    • Akrim, M., Bally, M., Ball, G., Tommassen, J., Teerink, H., Filloux, A., and Lazdunski, A. (1993). Xcp-mediated protein secretion in Pseudomonas aeruginosa: identifi-cation of two additional genes and evidence for regulation of xcp gene expression. Mol. Microbiol. 10, 431-443.
    • (1993) Mol. Microbiol. , vol.10 , pp. 431-443
    • Akrim, M.1    Bally, M.2    Ball, G.3
  • 4
    • 72649083410 scopus 로고    scopus 로고
    • Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system
    • Alphonse, S., Durand, E., Douzi, B., Waegele, B., Darbon, H., Filloux, A., Voulhoux, R., and Bernard, C. (2010). Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system. J. Struct. Biol. 169, 75-80.
    • (2010) J. Struct. Biol. , vol.169 , pp. 75-80
    • Alphonse, S.1    Durand, E.2    Douzi, B.3    Waegele, B.4    Darbon, H.5    Filloux, A.6    Voulhoux, R.7    Bernard, C.8
  • 5
    • 1842413699 scopus 로고    scopus 로고
    • A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica
    • Anderson, D. M., and Schneewind, O. (1997). A mRNA signal for the type III secretion of Yop proteins by Yersinia enterocolitica. Science 278, 1140-1143.
    • (1997) Science , vol.278 , pp. 1140-1143
    • Anderson, D.M.1    Schneewind, O.2
  • 7
    • 33947360771 scopus 로고    scopus 로고
    • Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway
    • Arts, J., van Boxtel, R., Filloux, A., Tommassen, J., and Koster, M. (2007). Export of the pseudopilin XcpT of the Pseudomonas aeruginosa type II secretion system via the signal recognition particle-Sec pathway. J. Bacteriol. 189, 2069-2076.
    • (2007) J. Bacteriol. , vol.189 , pp. 2069-2076
    • Arts, J.1    van Boxtel, R.2    Filloux, A.3    Tommassen, J.4    Koster, M.5
  • 8
    • 55549118213 scopus 로고    scopus 로고
    • SciN is an outer membrane lipoprotein required for type VI secretion in enteroaggregative Escherichia coli
    • Aschtgen, M. S., Bernard, C. S., De Bentzmann, S., Lloubes, R., and Cascales, E. (2008). SciN is an outer membrane lipoprotein required for type VI secretion in enteroaggregative Escherichia coli. J. Bacteriol. 190, 7523-7531.
    • (2008) J. Bacteriol. , vol.190 , pp. 7523-7531
    • Aschtgen, M.S.1    Bernard, C.S.2    De Bentzmann, S.3    Lloubes, R.4    Cascales, E.5
  • 10
    • 35348963630 scopus 로고    scopus 로고
    • Two electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery
    • Bageshwar, U. K., and Musser, S. M. (2007). Two electrical potential-dependent steps are required for transport by the Escherichia coli Tat machinery. J. Cell Biol. 179, 87-99.
    • (2007) J. Cell Biol. , vol.179 , pp. 87-99
    • Bageshwar, U.K.1    Musser, S.M.2
  • 11
    • 0032948809 scopus 로고    scopus 로고
    • Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa
    • Ball, G., Chapon-Herve, V., Bleves, S., Michel, G., and Bally, M. (1999). Assembly of XcpR in the cytoplasmic membrane is required for extracellular protein secretion in Pseudomonas aeruginosa. J. Bacteriol. 181, 382-388.
    • (1999) J. Bacteriol. , vol.181 , pp. 382-388
    • Ball, G.1    Chapon-Herve, V.2    Bleves, S.3    Michel, G.4    Bally, M.5
  • 12
    • 0036173113 scopus 로고    scopus 로고
    • A novel type II secretion system in Pseudomonas aeruginosa
    • Ball, G., Durand, E., Lazdunski, A., and Filloux, A. (2002). A novel type II secretion system in Pseudomonas aeruginosa. Mol. Microbiol. 43, 475-485.
    • (2002) Mol. Microbiol. , vol.43 , pp. 475-485
    • Ball, G.1    Durand, E.2    Lazdunski, A.3    Filloux, A.4
  • 14
    • 0026074370 scopus 로고
    • Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO
    • Bally, M., Ball, G., Badere, A., and Laz-dunski, A. (1991). Protein secretion in Pseudomonas aeruginosa: the xcpA gene encodes an integral inner membrane protein homologous to Klebsiella pneumoniae secretion function protein PulO. J. Bacteriol. 173, 479-486.
    • (1991) J. Bacteriol. , vol.173 , pp. 479-486
    • Bally, M.1    Ball, G.2    Badere, A.3    Laz-dunski, A.4
  • 15
    • 0026505643 scopus 로고
    • Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase
    • Bally, M., Filloux, A., Akrim, M., Ball, G., Lazdunski, A., and Tommassen, J. (1992). Protein secretion in Pseudomonas aeruginosa: characterization of seven xcp genes and processing of secretory apparatus components by prepilin peptidase. Mol. Microbiol. 6, 1121-1131.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1121-1131
    • Bally, M.1    Filloux, A.2    Akrim, M.3    Ball, G.4    Lazdunski, A.5    Tommassen, J.6
  • 16
    • 1642365547 scopus 로고    scopus 로고
    • Patatin-like proteins: a new family of lipolytic enzymes present in bacteria?
    • Banerji, S., and Flieger, A. (2004). Patatin-like proteins: a new family of lipolytic enzymes present in bacteria? Microbiology 150,522-525.
    • (2004) Microbiology , vol.150 , pp. 522-525
    • Banerji, S.1    Flieger, A.2
  • 17
    • 4344703018 scopus 로고    scopus 로고
    • A novel extracellular phospholipase C of Pseudomonas aeruginosa is required for phospholipid chemotaxis
    • Barker, A. P., Vasil, A. I., Filloux, A., Ball, G., Wilderman, P. J., and Vasil, M. L. (2004). A novel extracellular phospholipase C of Pseudomonas aeruginosa is required for phospholipid chemotaxis. Mol. Microbiol. 53, 1089-1098.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1089-1098
    • Barker, A.P.1    Vasil, A.I.2    Filloux, A.3    Ball, G.4    Wilderman, P.J.5    Vasil, M.L.6
  • 18
    • 0027292152 scopus 로고
    • Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif
    • Baumann, U., Wu, S., Flaherty, K. M., and McKay, D. B. (1993). Three-dimensional structure of the alkaline protease of Pseudomonas aeruginosa: a two-domain protein with a calcium binding parallel beta roll motif. EMBO J. 12, 3357-3364.
    • (1993) EMBO J , vol.12 , pp. 3357-3364
    • Baumann, U.1    Wu, S.2    Flaherty, K.M.3    McKay, D.B.4
  • 19
    • 0344405700 scopus 로고    scopus 로고
    • A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A
    • Benabdelhak, H., Kiontke, S., Horn, C., Ernst, R., Blight, M. A., Holland, I. B., and Schmitt, L. (2003). A specific interaction between the NBD of the ABC-transporter HlyB and a C-terminal fragment of its transport substrate haemolysin A. J. Mol. Biol. 327, 1169-1179.
    • (2003) J. Mol. Biol. , vol.327 , pp. 1169-1179
    • Benabdelhak, H.1    Kiontke, S.2    Horn, C.3    Ernst, R.4    Blight, M.A.5    Holland, I.B.6    Schmitt, L.7
  • 20
    • 0041440107 scopus 로고    scopus 로고
    • Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates: evidence for a possible association between O serotypes and exo genes
    • Berthelot, P., Attree, I., Plesiat, P., Chabert, J., de Bentzmann, S., Pozzetto, B., and Grattard, F. (2003). Genotypic and phenotypic analysis of type III secretion system in a cohort of Pseudomonas aeruginosa bacteremia isolates: evidence for a possible association between O serotypes and exo genes. J. Infect. Dis. 188, 512-518.
    • (2003) J. Infect. Dis. , vol.188 , pp. 512-518
    • Berthelot, P.1    Attree, I.2    Plesiat, P.3    Chabert, J.4    de Bentzmann, S.5    Pozzetto, B.6    Grattard, F.7
  • 21
    • 0024078229 scopus 로고
    • Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene
    • Bever, R. A., and Iglewski, B. H. (1988). Molecular characterization and nucleotide sequence of the Pseudomonas aeruginosa elastase structural gene. J. Bacteriol. 170, 4309-4314.
    • (1988) J. Bacteriol. , vol.170 , pp. 4309-4314
    • Bever, R.A.1    Iglewski, B.H.2
  • 22
    • 0031983616 scopus 로고    scopus 로고
    • Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa
    • Bitter, W., Koster, M., Latijnhouw-ers, M., de Cock, H., and Tom-massen, J. (1998). Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa. Mol. Microbiol. 27, 209-219.
    • (1998) Mol. Microbiol. , vol.27 , pp. 209-219
    • Bitter, W.1    Koster, M.2    Latijnhouw-ers, M.3    de Cock, H.4    Tom-massen, J.5
  • 23
    • 0345593398 scopus 로고    scopus 로고
    • Structure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosa
    • Bleves, S., Gerard-Vincent, M., Laz-dunski, A., and Filloux, A. (1999). Structure-function analysis of XcpP, a component involved in general secretory pathway-dependent protein secretion in Pseudomonas aeruginosa. J. Bacteriol. 181, 4012-4019.
    • (1999) J. Bacteriol. , vol.181 , pp. 4012-4019
    • Bleves, S.1    Gerard-Vincent, M.2    Laz-dunski, A.3    Filloux, A.4
  • 24
    • 0030013762 scopus 로고    scopus 로고
    • Membrane topology of three Xcp proteins involved in exoprotein transport by Pseudomonas aeruginosa
    • Bleves, S., Lazdunski, A., and Filloux, A. (1996). Membrane topology of three Xcp proteins involved in exoprotein transport by Pseudomonas aeruginosa. J. Bacteriol. 178, 4297-4300.
    • (1996) J. Bacteriol. , vol.178 , pp. 4297-4300
    • Bleves, S.1    Lazdunski, A.2    Filloux, A.3
  • 26
    • 0031983197 scopus 로고    scopus 로고
    • The secretion apparatus of Pseudomonas aeruginosa: identification of a fifth pseudopilin XcpX (GspK family)
    • Bleves, S.,Voulhoux, R., Michel, G., Laz-dunski, A., Tommassen, J., and Fil-loux, A. (1998). The secretion apparatus of Pseudomonas aeruginosa: identification of a fifth pseudopilin, XcpX (GspK family). Mol. Microbiol. 27, 31-40.
    • (1998) Mol. Microbiol. , vol.27 , pp. 31-40
    • Bleves, S.1    Voulhoux, R.2    Michel, G.3    Laz-dunski, A.4    Tommassen, J.5    Fil-loux, A.6
  • 27
    • 0037453098 scopus 로고    scopus 로고
    • Type III secretion systems and bacterial flagella: insights into their function from structural similarities
    • Blocker, A., Komoriya, K., and Aizawa, S. (2003). Type III secretion systems and bacterial flagella: insights into their function from structural similarities. Proc. Natl. Acad. Sci. U.S.A. 100, 3027-3030.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3027-3030
    • Blocker, A.1    Komoriya, K.2    Aizawa, S.3
  • 29
    • 60549104572 scopus 로고    scopus 로고
    • Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion
    • Bonemann, G., Pietrosiuk, A., Diemand,A.,Zentgraf, H.,and Mogk,A. (2009). Remodelling of VipA/VipB tubules by ClpV-mediated threading is crucial for type VI protein secretion. EMBO J. 28, 315-325.
    • (2009) EMBO J , vol.28 , pp. 315-325
    • Bonemann, G.1    Pietrosiuk, A.2    Diemand, A.3    Zentgraf, H.4    Mogk, A.5
  • 30
    • 77952139886 scopus 로고    scopus 로고
    • Tubules and donuts: a type VI secretion story
    • Bonemann, G., Pietrosiuk, A., and Mogk, A. (2010). Tubules and donuts: a type VI secretion story. Mol. Microbiol. 76, 815-821.
    • (2010) Mol. Microbiol. , vol.76 , pp. 815-821
    • Bonemann, G.1    Pietrosiuk, A.2    Mogk, A.3
  • 31
    • 76449122382 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix
    • Borlee, B. R., Goldman, A. D., Murakami, K., Samudrala, R., Woz-niak, D. J., and Parsek, M. R. (2010). Pseudomonas aeruginosa uses a cyclic-di-GMP-regulated adhesin to reinforce the biofilm extracellular matrix. Mol. Microbiol. 75, 827-842.
    • (2010) Mol. Microbiol. , vol.75 , pp. 827-842
    • Borlee, B.R.1    Goldman, A.D.2    Murakami, K.3    Samudrala, R.4    Woz-niak, D.J.5    Parsek, M.R.6
  • 32
    • 0031781189 scopus 로고    scopus 로고
    • Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa
    • Braun, P., de Groot, A., Bitter, W., and Tommassen, J. (1998). Secretion of elastinolytic enzymes and their propeptides by Pseudomonas aeruginosa. J. Bacteriol. 180, 3467-3469.
    • (1998) J. Bacteriol. , vol.180 , pp. 3467-3469
    • Braun, P.1    de Groot, A.2    Bitter, W.3    Tommassen, J.4
  • 33
    • 0030029288 scopus 로고    scopus 로고
    • Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa
    • Braun, P., Tommassen, J., and Filloux, A. (1996). Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa. Mol. Microbiol. 19, 297-306.
    • (1996) Mol. Microbiol. , vol.19 , pp. 297-306
    • Braun, P.1    Tommassen, J.2    Filloux, A.3
  • 35
    • 0141701277 scopus 로고    scopus 로고
    • PcrH of Pseudomonas aeruginosa is essential for secretion and assembly of the type III translocon
    • Broms, J. E., Forslund, A. L., Forsberg, A., and Francis, M. S. (2003). PcrH of Pseudomonas aeruginosa is essential for secretion and assembly of the type III translocon. J. Infect. Dis. 188, 1909-1921.
    • (2003) J. Infect. Dis. , vol.188 , pp. 1909-1921
    • Broms, J.E.1    Forslund, A.L.2    Forsberg, A.3    Francis, M.S.4
  • 37
    • 41749108855 scopus 로고    scopus 로고
    • Characterization of ExsA and of ExsA-dependent promoters required for expression of the Pseudomonas aeruginosa type III secretion system
    • Brutinel, E. D., Vakulskas, C. A., Brady, K. M., and Yahr, T. L. (2008). Characterization of ExsA and of ExsA-dependent promoters required for expression of the Pseudomonas aeruginosa type III secretion system. Mol. Microbiol. 68, 657-671.
    • (2008) Mol. Microbiol. , vol.68 , pp. 657-671
    • Brutinel, E.D.1    Vakulskas, C.A.2    Brady, K.M.3    Yahr, T.L.4
  • 38
    • 79851515749 scopus 로고    scopus 로고
    • Modeling pilus structures from sparse data
    • Campos, M., Francetic, O., and Nilges, M. (2011). Modeling pilus structures from sparse data. J. Struct. Biol. 173, 436-444.
    • (2011) J. Struct. Biol. , vol.173 , pp. 436-444
    • Campos, M.1    Francetic, O.2    Nilges, M.3
  • 39
    • 77955628595 scopus 로고    scopus 로고
    • Detailed structural and assembly model of the type II secretion pilus from sparse data
    • Campos, M., Nilges, M., Cisneros, D. A., and Francetic, O. (2010). Detailed structural and assembly model of the type II secretion pilus from sparse data. Proc. Natl.Acad. Sci. U.S.A. 107, 13081-13086.
    • (2010) Proc. Natl.Acad. Sci. U.S.A. , vol.107 , pp. 13081-13086
    • Campos, M.1    Nilges, M.2    Cisneros, D.A.3    Francetic, O.4
  • 40
    • 1842456892 scopus 로고    scopus 로고
    • The versatile bacterial type IV secretion systems
    • Cascales, E., and Christie, P. J. (2003). The versatile bacterial type IV secretion systems. Nat. Rev. Microbiol. 1, 137-149.
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 137-149
    • Cascales, E.1    Christie, P.J.2
  • 42
    • 72949109740 scopus 로고    scopus 로고
    • Structure of the outer membrane complex of a type IV secretion system
    • Chandran, V., Fronzes, R., Duquerroy, S., Cronin, N., Navaza, J., and Waks-man, G. (2009). Structure of the outer membrane complex of a type IV secretion system. Nature 462, 1011-1015.
    • (2009) Nature , vol.462 , pp. 1011-1015
    • Chandran, V.1    Fronzes, R.2    Duquerroy, S.3    Cronin, N.4    Navaza, J.5    Waks-man, G.6
  • 43
    • 43849098574 scopus 로고    scopus 로고
    • Coordinating assembly of a bacterial macromolecular machine
    • Chevance, F. F., and Hughes, K. T. (2008). Coordinating assembly of a bacterial macromolecular machine. Nat. Rev. Microbiol. 6, 455-465.
    • (2008) Nat. Rev. Microbiol. , vol.6 , pp. 455-465
    • Chevance, F.F.1    Hughes, K.T.2
  • 44
    • 38849174766 scopus 로고    scopus 로고
    • Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aeruginosa type IV pilus motor proteins PilBPilT and PilU
    • Chiang, P., Sampaleanu, L. M., Ayers, M., Pahuta, M., Howell, P. L., and Burrows, L. L. (2008). Functional role of conserved residues in the characteristic secretion NTPase motifs of the Pseudomonas aerugi-nosa type IV pilus motor proteins PilB, PilT and PilU. Microbiology 154, 114-126.
    • (2008) Microbiology , vol.154 , pp. 114-126
    • Chiang, P.1    Sampaleanu, L.M.2    Ayers, M.3    Pahuta, M.4    Howell, P.L.5    Burrows, L.L.6
  • 45
    • 71549149451 scopus 로고    scopus 로고
    • A comprehen-sive assessment of N-terminal signal peptides prediction methods.
    • doi: 10.1186/1471-2105-10-S15-S2
    • Choo, K. H., Tan, T. W., and Ranganathan, S. (2009). A comprehen-sive assessment of N-terminal signal peptides prediction methods. BMC Bioinformatics 10(Suppl. 15), S2. doi: 10.1186/1471-2105-10-S15-S2
    • (2009) BMC Bioinformatics , vol.10 , Issue.SUPPL. 15
    • Choo, K.H.1    Tan, T.W.2    Ranganathan, S.3
  • 46
    • 0024805123 scopus 로고
    • A gene required for transfer of T-DNA to plants encodes an ATPase with autophosphorylating activity.
    • Christie, P. J., Ward, J. E. Jr., Gordon, M. P., and Nester, E. W. (1989). A gene required for transfer of T-DNA to plants encodes an ATPase with autophosphorylating activity. Proc. Natl. Acad. Sci. U.S.A. 86, 9677-9681.
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9677-9681
    • Christie, P.J.1    Ward Jr, J.E.2    Gordon, M.P.3    Nester, E.W.4
  • 47
    • 60949100697 scopus 로고    scopus 로고
    • Export of recombinant proteins in Escherichia coli using ABC transporter with an attached lipase ABC transporter recognition domain (LARD)
    • Chung, C. W., You, J., Kim, K., Moon, Y., Kim, H., and Ahn, J. H. (2009). Export of recombinant proteins in Escherichia coli using ABC transporter with an attached lipase ABC transporter recognition domain (LARD). Microb.CellFact. 8, 11.
    • (2009) Microb.CellFact. , vol.8 , pp. 11
    • Chung, C.W.1    You, J.2    Kim, K.3    Moon, Y.4    Kim, H.5    Ahn, J.H.6
  • 49
    • 0037389450 scopus 로고    scopus 로고
    • Three-dimensional structure of the Neisseria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy
    • Collins, R. F., Ford, R. C., Kit-mitto, A., Olsen, R. O., Tonjum, T., and Derrick, J. P. (2003). Three-dimensional structure of the Neisse-ria meningitidis secretin PilQ determined from negative-stain transmission electron microscopy. J. Bacteriol. 185, 2611-2617.
    • (2003) J. Bacteriol. , vol.185 , pp. 2611-2617
    • Collins, R.F.1    Ford, R.C.2    Kit-mitto, A.3    Olsen, R.O.4    Tonjum, T.5    Derrick, J.P.6
  • 50
    • 33750110911 scopus 로고    scopus 로고
    • The type III secretion injectisome
    • Cornelis, G. R. (2006). The type III secretion injectisome. Nat. Rev.Microbiol. 4, 811-825.
    • (2006) Nat. Rev.Microbiol. , vol.4 , pp. 811-825
    • Cornelis, G.R.1
  • 51
    • 77954597457 scopus 로고    scopus 로고
    • The type III secretion injectisome, a complex nanomachine for intracellular "toxin" delivery
    • Cornelis, G. R. (2010). The type III secretion injectisome, a complex nanomachine for intracellular "toxin" delivery. Biol. Chem. 391, 745-751.
    • (2010) Biol. Chem. , vol.391 , pp. 745-751
    • Cornelis, G.R.1
  • 52
    • 1842430006 scopus 로고    scopus 로고
    • Bacterial invasion: the paradigms of enteroinvasive pathogens
    • Cossart, P., and Sansonetti, P. J. (2004). Bacterial invasion: the paradigms of enteroinvasive pathogens. Science 304, 242-248.
    • (2004) Science , vol.304 , pp. 242-248
    • Cossart, P.1    Sansonetti, P.J.2
  • 54
    • 0035047787 scopus 로고    scopus 로고
    • Poreforming activity of type III system-secreted proteins leads to oncosis of Pseudomonas aeruginosa-infected macrophages
    • Dacheux, D., Goure, J., Chabert, J., Usson,Y., and Attree, I. (2001). Poreforming activity of type III system-secreted proteins leads to oncosis of Pseudomonas aeruginosa-infected macrophages. Mol. Microbiol. 40, 76-85.
    • (2001) Mol. Microbiol. , vol.40 , pp. 76-85
    • Dacheux, D.1    Goure, J.2    Chabert, J.3    Usson, Y.4    Attree, I.5
  • 55
    • 0030965150 scopus 로고    scopus 로고
    • The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function
    • Daefler, S., Guilvout, I., Hardie, K. R., Pugsley, A. P., and Russel, M. (1997). The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on pIVf1 function. Mol. Microbiol. 24, 465-475.
    • (1997) Mol. Microbiol. , vol.24 , pp. 465-475
    • Daefler, S.1    Guilvout, I.2    Hardie, K.R.3    Pugsley, A.P.4    Russel, M.5
  • 56
    • 0345602998 scopus 로고    scopus 로고
    • Identification of a unique IAHP (IcmF associated homologous proteins) cluster in Vibrio cholerae and other proteobacteria through in silico analysis
    • Das, S., and Chaudhuri, K. (2003). Identification of a unique IAHP (IcmF associated homologous proteins) cluster in Vibrio cholerae and other proteobacteria through in silico analysis. In silico Biol. 3, 287-300.
    • (2003) In silico Biol , vol.3 , pp. 287-300
    • Das, S.1    Chaudhuri, K.2
  • 57
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria via the autotrans-porter pathway
    • Dautin, N., and Bernstein, H. D. (2007). Protein secretion in gram-negative bacteria via the autotrans-porter pathway. Annu.Rev.Microbiol. 61, 89-112.
    • (2007) Annu.Rev.Microbiol. , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 58
    • 0026056071 scopus 로고
    • Conservation of xcp genes, involved in the two-step protein secretion process, in different Pseudomonas species and other gram-negative bacteria
    • de Groot, A., Filloux, A., and Tommassen, J. (1991). Conservation of xcp genes, involved in the two-step protein secretion process, in different Pseudomonas species and other gram-negative bacteria. Mol. Gen. Genet. 229, 278-284.
    • (1991) Mol. Gen. Genet. , vol.229 , pp. 278-284
    • de Groot, A.1    Filloux, A.2    Tommassen, J.3
  • 59
    • 0035148762 scopus 로고    scopus 로고
    • Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes: species specificity unrelated to substrate recognition
    • de Groot, A., Koster, M., Gerard-Vincent, M., Gerritse, G., Laz-dunski, A., Tommassen, J., and Filloux, A. (2001). Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes: species specificity unrelated to substrate recognition. J. Bacteriol. 183, 959-967.
    • (2001) J. Bacteriol. , vol.183 , pp. 959-967
    • de Groot, A.1    Koster, M.2    Gerard-Vincent, M.3    Gerritse, G.4    Laz-dunski, A.5    Tommassen, J.6    Filloux, A.7
  • 60
    • 0029976327 scopus 로고    scopus 로고
    • Characterization of type II protein secretion (xcp) genes in the plant growth-stimulating Pseudomonas putida, strain WCS358
    • de Groot, A., Krijger, J. J., Filloux, A., and Tommassen, J. (1996). Characterization of type II protein secretion (xcp) genes in the plant growth-stimulating Pseudomonas putida, strain WCS358. Mol. Gen. Genet. 250, 491-504.
    • (1996) Mol. Gen. Genet. , vol.250 , pp. 491-504
    • de Groot, A.1    Krijger, J.J.2    Filloux, A.3    Tommassen, J.4
  • 61
    • 0023441713 scopus 로고
    • Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase
    • dEnfert, C., Ryter, A., and Pugsley, A. P. (1987). Cloning and expression in Escherichia coli of the Klebsiella pneumoniae genes for production, surface localization and secretion of the lipoprotein pullulanase. EMBO J. 6, 3531-3538.
    • (1987) EMBO J , vol.6 , pp. 3531-3538
    • dEnfert, C.1    Ryter, A.2    Pugsley, A.P.3
  • 62
    • 53849133471 scopus 로고    scopus 로고
    • Molecular mechanisms of the cyto-toxicity of ADP-ribosylating tox-ins
    • Deng, Q., and Barbieri, J. T. (2008). Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins. Annu.Rev.Microbiol.62, 271-288.
    • (2008) Annu.Rev.Microbiol.62 , pp. 271-288
    • Deng, Q.1    Barbieri, J.T.2
  • 64
    • 63549137674 scopus 로고    scopus 로고
    • Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue
    • Desvaux, M., Hebraud, M., Talon, R., and Henderson, I. R. (2009). Secretion and subcellular localizations of bacterial proteins: a semantic awareness issue. Trends Microbiol. 17, 139-145.
    • (2009) Trends Microbiol , vol.17 , pp. 139-145
    • Desvaux, M.1    Hebraud, M.2    Talon, R.3    Henderson, I.R.4
  • 65
    • 33750892424 scopus 로고    scopus 로고
    • Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein
    • Dong, C., Beis, K., Nesper, J., Brunkan-Lamontagne, A. L., Clarke, B. R., Whitfield, C., and Naismith, J. H. (2006). Wza the translocon for E. coli capsular polysaccharides defines a new class of membrane protein. Nature 444, 226-229.
    • (2006) Nature , vol.444 , pp. 226-229
    • Dong, C.1    Beis, K.2    Nesper, J.3    Brunkan-Lamontagne, A.L.4    Clarke, B.R.5    Whitfield, C.6    Naismith, J.H.7
  • 66
    • 71749119395 scopus 로고    scopus 로고
    • The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus
    • Douzi, B., Durand, E., Bernard, C., Alphonse, S., Cambillau, C., Filloux, A., Tegoni, M., and Voulhoux, R. (2009). The XcpV/GspI pseudopilin has a central role in the assembly of a quaternary complex within the T2SS pseudopilus. J. Biol. Chem. 284, 34580-34589.
    • (2009) J. Biol. Chem. , vol.284 , pp. 34580-34589
    • Douzi, B.1    Durand, E.2    Bernard, C.3    Alphonse, S.4    Cambillau, C.5    Filloux, A.6    Tegoni, M.7    Voulhoux, R.8
  • 67
    • 0035834925 scopus 로고    scopus 로고
    • The AprX protein of Pseudomonas aeruginosa: a new substrate for the Apr type I secretion system
    • Duong, F., Bonnet, E., Geli, V., Laz-dunski, A., Murgier, M., and Fil-loux, A. (2001). The AprX protein of Pseudomonas aeruginosa: a new substrate for the Apr type I secretion system. Gene 262, 147-153.
    • (2001) Gene , vol.262 , pp. 147-153
    • Duong, F.1    Bonnet, E.2    Geli, V.3    Laz-dunski, A.4    Murgier, M.5    Fil-loux, A.6
  • 68
    • 0026475721 scopus 로고
    • Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways
    • Duong, F., Lazdunski, A., Cami, B., and Murgier, M. (1992). Sequence of a cluster of genes controlling synthesis and secretion of alkaline protease in Pseudomonas aeruginosa: relationships to other secretory pathways. Gene 121, 47-54.
    • (1992) Gene , vol.121 , pp. 47-54
    • Duong, F.1    Lazdunski, A.2    Cami, B.3    Murgier, M.4
  • 69
    • 0029815310 scopus 로고    scopus 로고
    • Protein secretion by heterologous bacterial ABC-transporters: the C-terminus secretion signal of the secreted protein confers high recognition specificity
    • Duong, F., Lazdunski, A., and Murgier, M. (1996). Protein secretion by heterologous bacterial ABC-transporters: the C-terminus secretion signal of the secreted protein confers high recognition specificity. Mol. Microbiol. 21, 459-470.
    • (1996) Mol. Microbiol. , vol.21 , pp. 459-470
    • Duong, F.1    Lazdunski, A.2    Murgier, M.3
  • 71
    • 0037406829 scopus 로고    scopus 로고
    • Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure
    • Durand, E., Bernadac, A., Ball, G., Laz-dunski, A., Sturgis, J. N., and Filloux, A. (2003). Type II protein secretion in Pseudomonas aeruginosa: the pseudopilus is a multifibrillar and adhesive structure. J. Bacteriol. 185, 2749-2758.
    • (2003) J. Bacteriol. , vol.185 , pp. 2749-2758
    • Durand, E.1    Bernadac, A.2    Ball, G.3    Laz-dunski, A.4    Sturgis, J.N.5    Filloux, A.6
  • 72
    • 24744442588 scopus 로고    scopus 로고
    • XcpX controls biogenesis of the Pseudomonas aeruginosa XcpT-containing pseudopilus
    • Durand, E., Michel, G., Voulhoux, R., Kurner, J., Bernadac, A., and Filloux, A. (2005). XcpX controls biogenesis of the Pseudomonas aeruginosa XcpT-containing pseudopilus. J. Biol. Chem. 280, 31378-31389.
    • (2005) J. Biol. Chem. , vol.280 , pp. 31378-31389
    • Durand, E.1    Michel, G.2    Voulhoux, R.3    Kurner, J.4    Bernadac, A.5    Filloux, A.6
  • 73
    • 70349529642 scopus 로고    scopus 로고
    • Structural biology of bacterial secretion systems in gramnegative pathogens -potential for new drug targets
    • Durand, E., Verger, D., Rego, A. T., Chandran, V., Meng, G., Fronzes, R., and Waksman, G. (2009). Structural biology of bacterial secretion systems in gramnegative pathogens -potential for new drug targets. Infect. Disord. Drug Targets 9, 518-547.
    • (2009) Infect. Disord. Drug Targets , vol.9 , pp. 518-547
    • Durand, E.1    Verger, D.2    Rego, A.T.3    Chandran, V.4    Meng, G.5    Fronzes, R.6    Waksman, G.7
  • 74
    • 0036436338 scopus 로고    scopus 로고
    • SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system
    • Feldman,M. F.,Muller,S.,Wuest,E.,and Cornelis, G. R. (2002). SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system. Mol. Microbiol. 46, 1183-1197.
    • (2002) Mol. Microbiol. , vol.46 , pp. 1183-1197
    • Feldman, M.F.1    Muller, S.2    Wuest, E.3    Cornelis, G.R.4
  • 75
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux, A. (2004). The underlying mechanisms of type II protein secretion. Biochim. Biophys. Acta 1694, 163-179.
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 163-179
    • Filloux, A.1
  • 76
    • 60549109437 scopus 로고    scopus 로고
    • The type VI secretion system: a tubular story
    • Filloux,A. (2009). The type VI secretion system: a tubular story. EMBO J. 28, 309-310.
    • (2009) EMBO J , vol.28 , pp. 309-310
    • Filloux, A.1
  • 77
    • 77955296751 scopus 로고    scopus 로고
    • Secretion signal and protein targeting in bacteria: a biological puzzle
    • Filloux, A. (2010). Secretion signal and protein targeting in bacteria: a biological puzzle. J. Bacteriol. 192, 3847-3849.
    • (2010) J. Bacteriol. , vol.192 , pp. 3847-3849
    • Filloux, A.1
  • 78
    • 0025608578 scopus 로고
    • Protein secretion in gram-negative bacteria: transport across the outer membrane involves common mechanisms in different bacteria
    • Filloux, A., Bally, M., Ball, G., Akrim, M., Tommassen, J., and Lazdun-ski, A. (1990). Protein secretion in gram-negative bacteria: transport across the outer membrane involves common mechanisms in different bacteria. EMBO J. 9, 4323-4329.
    • (1990) EMBO J , vol.9 , pp. 4323-4329
    • Filloux, A.1    Bally, M.2    Ball, G.3    Akrim, M.4    Tommassen, J.5    Lazdun-ski, A.6
  • 79
    • 0024447283 scopus 로고
    • Cloning of Xcp-genes located at the 55-min region of the chromosome and involved in protein secretion in Pseudomonas aeruginosa
    • Filloux, A., Bally, M., Murgier, M., Wretlind, B., and Lazdunski, A. (1989). Cloning of Xcp-genes located at the 55-min region of the chromosome and involved in protein secretion in Pseudomonas aeruginosa. Mol. Microbiol. 3, 261-265.
    • (1989) Mol. Microbiol. , vol.3 , pp. 261-265
    • Filloux, A.1    Bally, M.2    Murgier, M.3    Wretlind, B.4    Lazdunski, A.5
  • 80
    • 0023924421 scopus 로고
    • Phosphate regulation in Pseudomonas aeruginosa: cloning of the alkaline phosphatase gene and identification of phoB-and phoR-like genes
    • Filloux,A.,Bally,M.,Soscia,C.,Murgier, M., and Lazdunski, A. (1988). Phosphate regulation in Pseudomonas aeruginosa: cloning of the alkaline phosphatase gene and identification of phoB-and phoR-like genes. Mol. Gen. Genet. 212, 510-513.
    • (1988) Mol. Gen. Genet. , vol.212 , pp. 510-513
    • Filloux, A.1    Bally, M.2    Soscia, C.3    Murgier, M.4    Lazdunski, A.5
  • 81
    • 48449086943 scopus 로고    scopus 로고
    • The bacterial type VI secretion machine: yet another player for protein transport across membranes
    • Filloux, A., Hachani, A., and Bleves, S. (2008). The bacterial type VI secretion machine: yet another player for protein transport across membranes. Microbiology 154, 1570-1583.
    • (2008) Microbiology 154, 1570- , pp. 1583
    • Filloux, A.1    Hachani, A.2    Bleves, S.3
  • 82
    • 22444454869 scopus 로고    scopus 로고
    • A systematic approach to the study of protein secretion in Gram-negative bacteria
    • Filloux, A., and Hardie, K. R. (1998). A systematic approach to the study of protein secretion in Gram-negative bacteria. Methods Microbiol. 27, 301-318.
    • (1998) Methods Microbiol , vol.27 , pp. 301-318
    • Filloux, A.1    Hardie, K.R.2
  • 83
    • 0023097732 scopus 로고
    • Characterization of 2 Pseudomonas aeruginosa mutants with defective secretion of extracellular proteins and comparison with other mutants
    • Filloux, A., Murgier, M., Wretlind, B., and Lazdunski, A. (1987). Characterization of 2 Pseudomonas aeruginosa mutants with defective secretion of extracellular proteins and comparison with other mutants. FEMS Microbiol. Lett. 40, 159-163.
    • (1987) FEMS Microbiol. Lett. , vol.40 , pp. 159-163
    • Filloux, A.1    Murgier, M.2    Wretlind, B.3    Lazdunski, A.4
  • 85
    • 0031785949 scopus 로고    scopus 로고
    • Identification and characterization of SpcU, a chaperone required for efficient secretion of the ExoU cytotoxin
    • Finck-Barbancon, V., Yahr, T. L., and Frank, D. W. (1998). Identification and characterization of SpcU, a chaperone required for efficient secretion of the ExoU cytotoxin. J. Bacteriol. 180, 6224-6231.
    • (1998) J. Bacteriol. , vol.180 , pp. 6224-6231
    • Finck-Barbancon, V.1    Yahr, T.L.2    Frank, D.W.3
  • 87
    • 0035212668 scopus 로고    scopus 로고
    • Characterization of Pseudomonas aeruginosa chitinase, a gradually secreted protein
    • Folders, J., Algra, J., Roelofs, M. S., van Loon, L. C., Tommassen, J., and Bitter, W. (2001). Characterization of Pseudomonas aeruginosa chitinase, a gradually secreted protein. J. Bacteriol. 183, 7044-7052.
    • (2001) J. Bacteriol. , vol.183 , pp. 7044-7052
    • Folders, J.1    Algra, J.2    Roelofs, M.S.3    van Loon, L.C.4    Tommassen, J.5    Bitter, W.6
  • 88
    • 0033953969 scopus 로고    scopus 로고
    • Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa
    • Folders, J., Tommassen, J., van Loon, L. C., and Bitter, W. (2000). Identification of a chitin-binding protein secreted by Pseudomonas aeruginosa. J. Bacteriol. 182, 1257-1263.
    • (2000) J. Bacteriol. , vol.182 , pp. 1257-1263
    • Folders, J.1    Tommassen, J.2    van Loon, L.C.3    Bitter, W.4
  • 89
    • 40849086263 scopus 로고    scopus 로고
    • Emergence of secretion-defective sublines of Pseudomonas aeruginosa PAO1 resulting from spontaneous mutations in the vfr global regulatory gene
    • Fox, A., Haas, D., Reimmann, C., Heeb, S., Filloux, A., and Voulhoux, R. (2008). Emergence of secretion-defective sublines of Pseudomonas aeruginosa PAO1 resulting from spontaneous mutations in the vfr global regulatory gene. Appl. Environ. Microbiol. 74, 1902-1908.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1902-1908
    • Fox, A.1    Haas, D.2    Reimmann, C.3    Heeb, S.4    Filloux, A.5    Voulhoux, R.6
  • 90
    • 26444506255 scopus 로고    scopus 로고
    • Towards the identification of type II secretion signals in a nonacy-lated variant of pullulanase from Klebsiella oxytoca
    • Francetic, O., and Pugsley, A. P. (2005). Towards the identification of type II secretion signals in a nonacy-lated variant of pullulanase from Klebsiella oxytoca. J. Bacteriol. 187, 7045-7055.
    • (2005) J. Bacteriol. , vol.187 , pp. 7045-7055
    • Francetic, O.1    Pugsley, A.P.2
  • 91
    • 0030726075 scopus 로고    scopus 로고
    • The exoenzyme S regulon of Pseudomonas aeruginosa
    • Frank, D. W. (1997). The exoenzyme S regulon of Pseudomonas aeruginosa. Mol. Microbiol. 26, 621-629.
    • (1997) Mol. Microbiol. , vol.26 , pp. 621-629
    • Frank, D.W.1
  • 92
    • 0036616572 scopus 로고    scopus 로고
    • Identification of XcpP domains that confer functionality and specificity to the Pseudomonas aeruginosa type II secretion apparatus
    • Gerard-Vincent, M., Robert, V., Ball, G., Bleves, S., Michel, G. P., Lazdunski, A., and Filloux, A. (2002). Identification of XcpP domains that confer functionality and specificity to the Pseudomonas aeruginosa type II secretion apparatus. Mol. Microbiol. 44, 1651-1665.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1651-1665
    • Gerard-Vincent, M.1    Robert, V.2    Ball, G.3    Bleves, S.4    Michel, G.P.5    Lazdunski, A.6    Filloux, A.7
  • 93
    • 1842326840 scopus 로고    scopus 로고
    • A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli
    • Ghigo, J. M., Letoffe, S., and Wandersman, C. (1997). A new type of hemophore-dependent heme acquisition system of Serratia marcescens reconstituted in Escherichia coli. J. Bacteriol. 179, 3572-3579.
    • (1997) J. Bacteriol. , vol.179 , pp. 3572-3579
    • Ghigo, J.M.1    Letoffe, S.2    Wandersman, C.3
  • 94
    • 79952085920 scopus 로고    scopus 로고
    • The PprA-PprB two-component system activates CupE, the first non-archetypal Pseudomonas aeruginosa chaperone-usher pathway system assembling fimbriae
    • Giraud, C., Bernard, C. S., Calderon, V., Yang, L., Filloux, A., Molin, S., Fichant, G., Bordi, C., and de Bentzmann, S. (2011). The PprA-PprB two-component system activates CupE, the first non-archetypal Pseudomonas aeruginosa chaperone-usher pathway system assembling fimbriae. Environ. Microbiol. 13, 666-683.
    • (2011) Environ. Microbiol. , vol.13 , pp. 666-683
    • Giraud, C.1    Bernard, C.S.2    Calderon, V.3    Yang, L.4    Filloux, A.5    Molin, S.6    Fichant, G.7    Bordi, C.8    de Bentzmann, S.9
  • 95
    • 58849118157 scopus 로고    scopus 로고
    • Direct interaction between sensor kinase proteins mediates acute and chronic disease phenotypes in a bacterial pathogen
    • Goodman, A. L., Merighi, M., Hyodo, M., Ventre, I., Filloux, A., and Lory, S. (2009). Direct interaction between sensor kinase proteins mediates acute and chronic disease phenotypes in a bacterial pathogen. Genes Dev. 23, 249-259.
    • (2009) Genes Dev , vol.23 , pp. 249-259
    • Goodman, A.L.1    Merighi, M.2    Hyodo, M.3    Ventre, I.4    Filloux, A.5    Lory, S.6
  • 96
    • 22244476683 scopus 로고    scopus 로고
    • Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host mem-branes
    • Goure, J., Broz, P., Attree, O., Cornelis, G. R., and Attree, I. (2005). Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes. J. Infect. Dis. 192, 218-225.
    • (2005) J. Infect. Dis. , vol.192 , pp. 218-225
    • Goure, J.1    Broz, P.2    Attree, O.3    Cornelis, G.R.4    Attree, I.5
  • 97
    • 3343006984 scopus 로고    scopus 로고
    • The V antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes
    • Goure, J., Pastor,A., Faudry, E., Chabert, J., Dessen, A., and Attree, I. (2004). The V antigen of Pseudomonas aeruginosa is required for assembly of the functional PopB/PopD translocation pore in host cell membranes. Infect. Immun. 72, 4741-4750.
    • (2004) Infect. Immun. , vol.72 , pp. 4741-4750
    • Goure, J.1    Pastor, A.2    Faudry, E.3    Chabert, J.4    Dessen, A.5    Attree, I.6
  • 98
    • 0025173979 scopus 로고
    • Cloning of the Pseudomonas aeruginosa alka-line protease gene and secretion of the protease into the medium by Escherichia coli
    • Guzzo, J., Murgier, M., Filloux, A., and Lazdunski, A. (1990). Cloning of the Pseudomonas aeruginosa alka-line protease gene and secretion of the protease into the medium by Escherichia coli. J. Bacteriol. 172, 942-948.
    • (1990) J. Bacteriol. , vol.172 , pp. 942-948
    • Guzzo, J.1    Murgier, M.2    Filloux, A.3    Lazdunski, A.4
  • 99
    • 0026009410 scopus 로고
    • Pseudomonas aeruginosa alkaline protease: evidence for secretion genes and study of secretion mechanism
    • Guzzo, J., Pages, J. M., Duong, F., Lazdunski, A., and Murgier, M. (1991a). Pseudomonas aeruginosa alkaline protease: evidence for secretion genes and study of secretion mechanism. J. Bacteriol. 173, 5290-5297.
    • (1991) J. Bacteriol. , vol.173 , pp. 5290-5297
    • Guzzo, J.1    Pages, J.M.2    Duong, F.3    Lazdunski, A.4    Murgier, M.5
  • 100
    • 0026088819 scopus 로고
    • The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysan-themi proteases and Escherichia coli alpha-haemolysin
    • Guzzo, J., Duong, F., Wandersman, C., Murgier, M., and Lazdun-ski, A. (1991b). The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysan-themi proteases and Escherichia coli alpha-haemolysin. Mol. Microbiol. 5, 447-453.
    • (1991) Mol. Microbiol. , vol.5 , pp. 447-453
    • Guzzo, J.1    Duong, F.2    Wandersman, C.3    Murgier, M.4    Lazdun-ski, A.5
  • 101
    • 79953311518 scopus 로고    scopus 로고
    • TypeVI secretion system in Pseudomonas Aeruginosa: secretion and multimerization of VgrG proteins
    • Hachani, A., Lossi, N. S., Hamilton, A., Jones, C., Bleves, S., Albesa-Jove, D., and Filloux,A. (2011). TypeVI secretion system in Pseudomonas Aerugi-nosa: secretion and multimerization of VgrG proteins. J. Biol. Chem. 286, 12317-12327.
    • (2011) J. Biol. Chem. , vol.286 , pp. 12317-12327
    • Hachani, A.1    Lossi, N.S.2    Hamilton, A.3    Jones, C.4    Bleves, S.5    Albesa-Jove, D.6    Filloux, A.7
  • 102
    • 0029870545 scopus 로고    scopus 로고
    • Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein
    • Hardie, K. R., Lory, S., and Pugsley, A. P. (1996). Insertion of an outer membrane protein in Escherichia coli requires a chaperone-like protein. EMBO J. 15, 978-988.
    • (1996) EMBO J , vol.15 , pp. 978-988
    • Hardie, K.R.1    Lory, S.2    Pugsley, A.P.3
  • 103
    • 69249157248 scopus 로고    scopus 로고
    • The type III secretion system of Pseudomonas aeruginosa: infection by injection
    • Hauser, A. R. (2009). The type III secretion system of Pseudomonas aeruginosa: infection by injection. Nat. Rev. Microbiol. 7, 654-665.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 654-665
    • Hauser, A.R.1
  • 104
    • 0036191393 scopus 로고    scopus 로고
    • Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa
    • Hauser, A. R., Cobb, E., Bodi, M., Mariscal, D., Valles, J., Engel, J. N., and Rello, J. (2002). Type III protein secretion is associated with poor clinical outcomes in patients with ventilator-associated pneumonia caused by Pseudomonas aeruginosa. Crit. Care Med. 30, 521-528.
    • (2002) Crit. Care Med. , vol.30 , pp. 521-528
    • Hauser, A.R.1    Cobb, E.2    Bodi, M.3    Mariscal, D.4    Valles, J.5    Engel, J.N.6    Rello, J.7
  • 106
    • 0034745728 scopus 로고    scopus 로고
    • Role of the Tat ransport system in nitrous oxide reductase translocation and cytochrome cd1 biosynthesis in Pseudomonas stutzeri
    • Heikkila, M. P., Honisch, U., Wun-sch, P., and Zumft, W. G. (2001). Role of the Tat ransport system in nitrous oxide reductase translocation and cytochrome cd1 biosynthesis in Pseudomonas stutzeri. J. Bacteriol. 183, 1663-1671.
    • (2001) J. Bacteriol. , vol.183 , pp. 1663-1671
    • Heikkila, M.P.1    Honisch, U.2    Wun-sch, P.3    Zumft, W.G.4
  • 107
    • 0035019469 scopus 로고    scopus 로고
    • ABC transporters: physiology, structure and mechanism-anoverview
    • Higgins, C. F. (2001). ABC transporters: physiology, structure and mechanism-anoverview.Res. Microbiol. 152, 205-210.
    • (2001) Res. Microbiol. , vol.152 , pp. 205-210
    • Higgins, C.F.1
  • 109
    • 0042065283 scopus 로고    scopus 로고
    • Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein
    • Hinsa, S. M., Espinosa-Urgel, M., Ramos, J. L., and OToole, G. A. (2003). Transition from reversible to irreversible attachment during biofilm formation by Pseudomonas fluorescens WCS365 requires an ABC transporter and a large secreted protein. Mol. Microbiol. 49, 905-918.
    • (2003) Mol. Microbiol. , vol.49 , pp. 905-918
    • Hinsa, S.M.1    Espinosa-Urgel, M.2    Ramos, J.L.3    O'Toole, G.A.4
  • 110
    • 0027489247 scopus 로고
    • Common components in the assembly of type 4 fimbriae,DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein com-plexes
    • Hobbs, M., and Mattick, J. S. (1993). Common components in the assembly of type 4 fimbriae,DNA transfer systems, filamentous phage and protein-secretion apparatus: a general system for the formation of surface-associated protein com-plexes. Mol. Microbiol. 10, 233-243.
    • (1993) Mol. Microbiol. , vol.10 , pp. 233-243
    • Hobbs, M.1    Mattick, J.S.2
  • 111
    • 33748496461 scopus 로고    scopus 로고
    • Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate
    • Hodak, H., Clantin, B., Willery, E., Villeret, V., Locht, C., and Jacob-Dubuisson, F. (2006). Secretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate. Mol. Microbiol. 61, 368-382.
    • (2006) Mol. Microbiol. , vol.61 , pp. 368-382
    • Hodak, H.1    Clantin, B.2    Willery, E.3    Villeret, V.4    Locht, C.5    Jacob-Dubuisson, F.6
  • 113
    • 18844428872 scopus 로고    scopus 로고
    • Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review)
    • Holland, I. B., Schmitt, L., and Young, J. (2005). Type 1 protein secretion in bacteria, the ABC-transporter dependent pathway (review). Mol. Membr. Biol. 22, 29-39.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 29-39
    • Holland, I.B.1    Schmitt, L.2    Young, J.3
  • 115
    • 0035035580 scopus 로고    scopus 로고
    • Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins
    • Jacob-Dubuisson, F., Locht, C., and Antoine, R. (2001). Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins. Mol. Microbiol. 40, 306-313.
    • (2001) Mol. Microbiol. , vol.40 , pp. 306-313
    • Jacob-Dubuisson, F.1    Locht, C.2    Antoine, R.3
  • 118
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet, L.,Agrain, C., Broz, P., and Cornelis,G. R. (2003). The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302, 1757-1760.
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 119
    • 60649098853 scopus 로고    scopus 로고
    • Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion
    • Junker, M., Besingi, R. N., and Clark, P. L. (2009). Vectorial transport and folding of an autotransporter virulence protein during outer membrane secretion. Mol. Microbiol. 71, 1323-1332.
    • (2009) Mol. Microbiol. , vol.71 , pp. 1323-1332
    • Junker, M.1    Besingi, R.N.2    Clark, P.L.3
  • 120
    • 33747790227 scopus 로고    scopus 로고
    • The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins
    • Kajava, A. V., and Steven, A. C. (2006). The turn of the screw: variations of the abundant beta-solenoid motif in passenger domains of Type V secretory proteins. J. Struct. Biol. 155, 306-315.
    • (2006) J. Struct. Biol. , vol.155 , pp. 306-315
    • Kajava, A.V.1    Steven, A.C.2
  • 122
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: a case study using the Phyre server
    • Kelley,L. A.,and Sternberg, M. J. (2009). Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 4, 363-371.
    • (2009) Nat. Protoc. , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.2
  • 123
    • 0028021766 scopus 로고
    • The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor
    • Kessler, E., and Safrin, M. (1994). The propeptide of Pseudomonas aeruginosa elastase acts an elastase inhibitor. J. Biol. Chem. 269, 22726-22731.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22726-22731
    • Kessler, E.1    Safrin, M.2
  • 124
    • 45249083027 scopus 로고    scopus 로고
    • A novel secreted protease from Pseudomonas aeruginosa activates NF-kappaB through protease-activated receptors
    • Kida, Y., Higashimoto, Y., Inoue, H., Shimizu, T., and Kuwano, K. (2008). A novel secreted protease from Pseudomonas aeruginosa activates NF-kappaB through protease-activated receptors. Cell. Microbiol. 10, 1491-1504.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1491-1504
    • Kida, Y.1    Higashimoto, Y.2    Inoue, H.3    Shimizu, T.4    Kuwano, K.5
  • 125
    • 0038385185 scopus 로고    scopus 로고
    • Secretion of a soluble col-onization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae
    • Kirn, T. J., Bose, N., and Taylor, R. K. (2003). Secretion of a soluble col-onization factor by the TCP type 4 pilus biogenesis pathway in Vibrio cholerae. Mol. Microbiol. 49, 81-92.
    • (2003) Mol. Microbiol. , vol.49 , pp. 81-92
    • Kirn, T.J.1    Bose, N.2    Taylor, R.K.3
  • 126
    • 0024386073 scopus 로고
    • Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes
    • Koronakis, V., Koronakis, E., and Hughes, C. (1989). Isolation and analysis of the C-terminal signal directing export of Escherichia coli hemolysin protein across both bacterial membranes. EMBO J. 8, 595-605.
    • (1989) EMBO J , vol.8 , pp. 595-605
    • Koronakis, V.1    Koronakis, E.2    Hughes, C.3
  • 127
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis, V., Sharff, A., Koronakis, E., Luisi, B., and Hughes, C. (2000). Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 405, 914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 128
    • 79961171407 scopus 로고    scopus 로고
    • Secretins: dynamic channels for protein transport across membranes
    • PMID: 21565514.[Epub ahead of print]
    • Korotkov, K. V., Gonen, T., and Hol, W. G. (2011). Secretins: dynamic channels for protein transport across membranes. Trends Biochem. Sci. PMID: 21565514. [Epub ahead of print].
    • (2011) Trends Biochem. Sci.
    • Korotkov, K.V.1    Gonen, T.2    Hol, W.G.3
  • 129
    • 43249092408 scopus 로고    scopus 로고
    • Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type2secretion system
    • Korotkov, K. V., and Hol, W. G. (2008). Structure of the GspK-GspI-GspJ complex from the enterotoxigenic Escherichia coli type2secretion system. Nat. Struct. Mol. Biol. 15, 462-468.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 462-468
    • Korotkov, K.V.1    Hol, W.G.2
  • 130
    • 59649092183 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody
    • Korotkov, K. V., Pardon, E., Steyaert, J., and Hol, W. G. (2009). Crystal structure of the N-terminal domain of the secretin GspD from ETEC determined with the assistance of a nanobody. Structure 17, 255-265.
    • (2009) Structure , vol.17 , pp. 255-265
    • Korotkov, K.V.1    Pardon, E.2    Steyaert, J.3    Hol, W.G.4
  • 131
    • 0030716279 scopus 로고    scopus 로고
    • The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex
    • Koster, M., Bitter, W., de Cock, H., Allaoui,A.,Cornelis,G. R.,and Tommassen, J. (1997). The outer membrane component, YscC, of the Yop secretion machinery of Yersinia enterocolitica forms a ring-shaped multimeric complex. Mol. Microbiol. 26, 789-797.
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-797
    • Koster, M.1    Bitter, W.2    de Cock, H.3    Allaoui, A.4    Cornelis, G.R.5    Tommassen, J.6
  • 133
    • 72149103792 scopus 로고    scopus 로고
    • The C-terminal amphipathic alpha-helix of Pseudomonas aeruginosa PelC outer membrane protein is required for its function
    • Kowalska, K., Soscia, C., Combe, H., Vasseur, P., Voulhoux, R., and Filloux, A. (2010). The C-terminal amphipathic alpha-helix of Pseudomonas aeruginosa PelC outer membrane protein is required for its function. Biochimie 92, 33-40.
    • (2010) Biochimie , vol.92 , pp. 33-40
    • Kowalska, K.1    Soscia, C.2    Combe, H.3    Vasseur, P.4    Voulhoux, R.5    Filloux, A.6
  • 136
    • 15444363295 scopus 로고    scopus 로고
    • Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography
    • Lambert, O., Benabdelhak, H., Chami, M., Jouan, L., Nouaille, E., Ducruix, A., and Brisson, A. (2005). Trimeric structure of OprN and OprM efflux proteins from Pseudomonas aeruginosa, by 2D electron crystallography. J. Struct. Biol. 150, 50-57.
    • (2005) J. Struct. Biol. , vol.150 , pp. 50-57
    • Lambert, O.1    Benabdelhak, H.2    Chami, M.3    Jouan, L.4    Nouaille, E.5    Ducruix, A.6    Brisson, A.7
  • 140
    • 0029908021 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding
    • Letoffe, S., Delepelaire, P., and Wandersman, C. (1996). Protein secretion in gram-negative bacteria: assembly of the three components of ABC protein-mediated exporters is ordered and promoted by substrate binding. EMBO J. 15, 5804-5811.
    • (1996) EMBO J , vol.15 , pp. 5804-5811
    • Letoffe, S.1    Delepelaire, P.2    Wandersman, C.3
  • 141
    • 0042990231 scopus 로고    scopus 로고
    • Interactions of HasA, a bacterial haemophore, with haemoglobin and with its outer membrane receptor HasR
    • Letoffe, S., Nato, F., Goldberg, M. E., and Wandersman, C. (1999). Interactions of HasA, a bacterial haemophore, with haemoglobin and with its outer membrane receptor HasR. Mol. Microbiol. 33, 546-555.
    • (1999) Mol. Microbiol. , vol.33 , pp. 546-555
    • Letoffe, S.1    Nato, F.2    Goldberg, M.E.3    Wandersman, C.4
  • 142
    • 0031775913 scopus 로고    scopus 로고
    • Isolation and characterization of an extracellular haem-binding protein from Pseudomonas aeruginosa that shares function and sequence similarities with the Serratia marcescens HasA haemophore
    • Letoffe, S., Redeker, V., and Wandersman, C. (1998). Isolation and characterization of an extracellular haem-binding protein from Pseudomonas aeruginosa that shares function and sequence similarities with the Serratia marcescens HasA haemophore. Mol. Microbiol. 28, 1223-1234.
    • (1998) Mol. Microbiol. , vol.28 , pp. 1223-1234
    • Letoffe, S.1    Redeker, V.2    Wandersman, C.3
  • 144
    • 34248359106 scopus 로고    scopus 로고
    • A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps
    • Lobedanz, S., Bokma, E., Symmons, M. F., Koronakis, E., Hughes, C., and Koronakis, V. (2007). A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps. Proc. Natl. Acad. Sci. U.S.A. 104, 4612-4617.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 4612-4617
    • Lobedanz, S.1    Bokma, E.2    Symmons, M.F.3    Koronakis, E.4    Hughes, C.5    Koronakis, V.6
  • 145
    • 0036829647 scopus 로고    scopus 로고
    • The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2002). The "LSGGQ" motif in each nucleotide-binding domain of human P-glycoprotein is adjacent to the opposing walker A sequence. J. Biol. Chem. 277, 41303-41306.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41303-41306
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 146
    • 0027372041 scopus 로고
    • A periplasmic intermediate in the extracellular secretion pathway of Pseudomonas aeruginosa exotoxin A
    • Lu, H. M., Mizushima, S., and Lory, S. (1993). A periplasmic intermediate in the extracellular secretion pathway of Pseudomonas aeruginosa exotoxin A. J. Bacteriol. 175, 7463-7467.
    • (1993) J. Bacteriol. , vol.175 , pp. 7463-7467
    • Lu, H.M.1    Mizushima, S.2    Lory, S.3
  • 147
    • 61849114089 scopus 로고    scopus 로고
    • Translocation of a Vibrio cholerae type VI secretion effector requires bacterial endocytosis by host cells
    • Ma, A. T., McAuley, S., Pukatzki, S., and Mekalanos, J. J. (2009). Translocation of a Vibrio cholerae type VI secretion effector requires bacterial endocytosis by host cells. Cell Host Microbe 5, 234-243.
    • (2009) Cell Host Microbe , vol.5 , pp. 234-243
    • Ma, A.T.1    McAuley, S.2    Pukatzki, S.3    Mekalanos, J.J.4
  • 148
    • 0022411845 scopus 로고
    • Identification of polypeptides required for the export of haemolysin 2001 from E. coli
    • Mackman, N., Nicaud, J. M., Gray, L., and Holland, I. B. (1985). Identification of polypeptides required for the export of haemolysin 2001 from E. coli. Mol. Gen. Genet. 201, 529-536.
    • (1985) Mol. Gen. Genet. , vol.201 , pp. 529-536
    • Mackman, N.1    Nicaud, J.M.2    Gray, L.3    Holland, I.B.4
  • 149
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R. M. (2003). How bacteria assemble flagella. Annu.Rev.Microbiol. 57, 77-100.
    • (2003) Annu.Rev.Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 150
    • 0032874098 scopus 로고    scopus 로고
    • LipC, a second lipase of Pseudomonas aeruginosa, is LipB and Xcp dependent and is transcriptionally regulated by pilus biogenesis components
    • Martinez, A., Ostrovsky, P., and Nunn, D. N. (1999). LipC, a second lipase of Pseudomonas aeruginosa, is LipB and Xcp dependent and is transcriptionally regulated by pilus biogenesis components. Mol. Microbiol. 34, 317-326.
    • (1999) Mol. Microbiol. , vol.34 , pp. 317-326
    • Martinez, A.1    Ostrovsky, P.2    Nunn, D.N.3
  • 151
    • 77955296461 scopus 로고    scopus 로고
    • Multiple signals direct the assembly and function of a type 1 secretion system
    • Masi, M., and Wandersman, C. (2010). Multiple signals direct the assembly and function of a type 1 secretion system. J. Bacteriol. 192, 3861-3869.
    • (2010) J. Bacteriol. , vol.192 , pp. 3861-3869
    • Masi, M.1    Wandersman, C.2
  • 152
    • 0036405357 scopus 로고    scopus 로고
    • Type IV pili and twitching motility
    • Mattick, J. S. (2002). Type IV pili and twitching motility. Annu. Rev. Microbiol. 56, 289-314.
    • (2002) Annu. Rev. Microbiol. , vol.56 , pp. 289-314
    • Mattick, J.S.1
  • 153
    • 36048935998 scopus 로고    scopus 로고
    • New insight into the molecular mechanisms of two-partner secretion
    • Mazar, J., and Cotter, P. A. (2007). New insight into the molecular mechanisms of two-partner secretion. Trends Microbiol. 15, 508-515.
    • (2007) Trends Microbiol , vol.15 , pp. 508-515
    • Mazar, J.1    Cotter, P.A.2
  • 154
    • 11044223673 scopus 로고    scopus 로고
    • Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities
    • McIver, K. S., Kessler, E., and Ohman, D. E. (2004). Identification of residues in the Pseudomonas aeruginosa elastase propeptide required for chaperone and secretion activities. Microbiology 150, 3969-3977.
    • (2004) Microbiology , vol.150 , pp. 3969-3977
    • McIver, K.S.1    Kessler, E.2    Ohman, D.E.3
  • 155
    • 0029612321 scopus 로고
    • The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa
    • McIver, K. S., Kessler, E., Olson, J. C., and Ohman, D. E. (1995). The elastase propeptide functions as an intramolecular chaperone required for elastase activity and secretion in Pseudomonas aeruginosa. Mol. Microbiol. 18, 877-889.
    • (1995) Mol. Microbiol. , vol.18 , pp. 877-889
    • McIver, K.S.1    Kessler, E.2    Olson, J.C.3    Ohman, D.E.4
  • 156
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotrans-porter
    • Meng, G., Surana, N. K., St Geme, J. W. III, and Waksman, G. (2006). Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotrans-porter. EMBO J. 25, 2297-2304.
    • (2006) EMBO J , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    St Geme III, J.W.3    Waksman, G.4
  • 157
    • 3142544236 scopus 로고    scopus 로고
    • Frontal and stealth attack strategies in microbial pathogenesis
    • Merrell, D. S., and Falkow, S. (2004). Frontal and stealth attack strategies in microbial pathogenesis. Nature 430, 250-256.
    • (2004) Nature , vol.430 , pp. 250-256
    • Merrell, D.S.1    Falkow, S.2
  • 158
    • 0032434689 scopus 로고    scopus 로고
    • Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa
    • Michel, G., Bleves, S., Ball, G., Laz-dunski, A., and Filloux, A. (1998). Mutual stabilization of the XcpZ and XcpY components of the secretory apparatus in Pseudomonas aeruginosa. Microbiology 144(Pt 12), 3379-3386.
    • (1998) Microbiology , vol.144 , Issue.PART 12 , pp. 3379-3386
    • Michel, G.1    Bleves, S.2    Ball, G.3    Laz-dunski, A.4    Filloux, A.5
  • 159
    • 34248402363 scopus 로고    scopus 로고
    • XphA/XqhA, a novel GspCD subunit for type II secretion in Pseudomonas aeruginosa
    • Michel, G. P., Durand, E., and Fil-loux,A. (2007). XphA/XqhA, a novel GspCD subunit for type II secretion in Pseudomonas aeruginosa. J. Bacteriol. 189, 3776-3783.
    • (2007) J. Bacteriol. , vol.189 , pp. 3776-3783
    • Michel, G.P.1    Durand, E.2    Fil-loux, A.3
  • 160
    • 0028982630 scopus 로고
    • Specificity of the protein secretory apparatus: secretion of the heat-labile entero-toxin B subunit pentamers by different species of gram-bacteria
    • Michel, L. O., Sandkvist, M., and Bagdasarian, M. (1995). Specificity of the protein secretory apparatus: secretion of the heat-labile entero-toxin B subunit pentamers by different species of gram-bacteria. Gene 152, 41-45.
    • (1995) Gene , vol.152 , pp. 41-45
    • Michel, L.O.1    Sandkvist, M.2    Bagdasarian, M.3
  • 163
    • 33644833626 scopus 로고    scopus 로고
    • Mikolosko, J., Bobyk, K., Zgurskaya, H. I., and Ghosh, P. (2006). Conformational flexibility in the multidrug efflux system protein AcrA. Structure 14, 577-587.
    • (2006) , vol.14 , pp. 577-587
    • Mikolosko, J.1    Bobyk, K.2    Zgurskaya, H.I.3    Ghosh, P.4
  • 164
    • 77954623239 scopus 로고    scopus 로고
    • P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor
    • Misic, A. M., Satyshur, K. A., and Forest, K. T. (2010). P. aeruginosa PilT structures with and without nucleotide reveal a dynamic type IV pilus retraction motor. J. Mol. Biol. 400, 1011-1021.
    • (2010) J. Mol. Biol. , vol.400 , pp. 1011-1021
    • Misic, A.M.1    Satyshur, K.A.2    Forest, K.T.3
  • 165
  • 167
    • 14144249589 scopus 로고    scopus 로고
    • A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells
    • Nagai, H., Cambronne, E. D., Kagan, J. C., Amor, J. C., Kahn, R. A., and Roy, C. R. (2005). A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells. Proc. Natl. Acad. Sci. U.S.A. 102, 826-831.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 826-831
    • Nagai, H.1    Cambronne, E.D.2    Kagan, J.C.3    Amor, J.C.4    Kahn, R.A.5    Roy, C.R.6
  • 168
    • 71049164676 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa PA14 cupD transcription is activated by the RcsB response regulator, but repressed by its putative cognate sensor RcsC
    • Nicastro, G. G., Boechat, A. L., Abe, C. M., Kaihami, G. H., and Baldini, R. L. (2009). Pseudomonas aeruginosa PA14 cupD transcription is activated by the RcsB response regulator, but repressed by its putative cognate sensor RcsC. FEMS Microbiol. Lett. 301, 115-123.
    • (2009) FEMS Microbiol. Lett. , vol.301 , pp. 115-123
    • Nicastro, G.G.1    Boechat, A.L.2    Abe, C.M.3    Kaihami, G.H.4    Baldini, R.L.5
  • 169
    • 0026345424 scopus 로고
    • Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader pepti-dase
    • Nunn, D. N., and Lory, S. (1991). Product of the Pseudomonas aeruginosa gene pilD is a prepilin leader pepti-dase. Proc. Natl. Acad. Sci. U.S.A. 88, 3281-3285.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 3281-3285
    • Nunn, D.N.1    Lory, S.2
  • 170
    • 0026502111 scopus 로고
    • Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase
    • Nunn, D. N., and Lory, S. (1992). Components of the protein-excretion apparatus of Pseudomonas aeruginosa are processed by the type IV prepilin peptidase. Proc. Natl. Acad. Sci. U.S.A. 89, 47-51.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 47-51
    • Nunn, D.N.1    Lory, S.2
  • 171
    • 0027273016 scopus 로고
    • Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W
    • Nunn, D. N., and Lory, S. (1993). Cleavage, methylation, and localization of the Pseudomonas aeruginosa export proteins XcpT, -U, -V, and -W. J. Bacteriol. 175, 4375-4382.
    • (1993) J. Bacteriol. , vol.175 , pp. 4375-4382
    • Nunn, D.N.1    Lory, S.2
  • 172
    • 1942471665 scopus 로고    scopus 로고
    • Structure of the translocator domain of a bacterial autotransporter
    • Oomen, C. J., van Ulsen, P., van Gelder, P., Feijen, M., Tommassen, J., and Gros, P. (2004). Structure of the translocator domain of a bacterial autotransporter. EMBO J. 23, 1257-1266.
    • (2004) EMBO J , vol.23 , pp. 1257-1266
    • Oomen, C.J.1    van Ulsen, P.2    van Gelder, P.3    Feijen, M.4    Tommassen, J.5    Gros, P.6
  • 173
    • 0023612039 scopus 로고
    • Identification of a new phos-pholipase C activity by analysis of an insertional mutation in the hemolytic phospholipase C structural gene of Pseudomonas aeruginosa
    • Ostroff, R. M., and Vasil, M. L. (1987). Identification of a new phos-pholipase C activity by analysis of an insertional mutation in the hemolytic phospholipase C structural gene of Pseudomonas aeruginosa. J. Bacteriol. 169, 4597-4601.
    • (1987) J. Bacteriol. , vol.169 , pp. 4597-4601
    • Ostroff, R.M.1    Vasil, M.L.2
  • 174
    • 0037352234 scopus 로고    scopus 로고
    • Moving folded proteins across the bacterial cell membrane
    • Palmer,T.,and Berks,B. C. (2003). Moving folded proteins across the bacterial cell membrane. Microbiology 149, 547-556.
    • (2003) Microbiology , vol.149 , pp. 547-556
    • Palmer, T.1    Berks, B.C.2
  • 175
    • 77954739358 scopus 로고    scopus 로고
    • Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli
    • Palmer, T., Berks, B. C., and Sargent, F. (2010). Analysis of Tat targeting function and twin-arginine signal peptide activity in Escherichia coli. Methods Mol. Biol. 619, 191-216.
    • (2010) Methods Mol. Biol. , vol.619 , pp. 191-216
    • Palmer, T.1    Berks, B.C.2    Sargent, F.3
  • 176
    • 35348908966 scopus 로고    scopus 로고
    • Bacterial protein secretion through the translo-case nanomachine
    • Papanikou, E., Karamanou, S., and Economou, A. (2007). Bacterial protein secretion through the translo-case nanomachine. Nat. Rev. Microbiol. 5, 839-851.
    • (2007) Nat. Rev. Microbiol. , vol.5 , pp. 839-851
    • Papanikou, E.1    Karamanou, S.2    Economou, A.3
  • 177
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot, C., Hamiaux, C., and Page, A. L. (2003). The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6, 7-14.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.L.3
  • 178
    • 27744455122 scopus 로고    scopus 로고
    • PscF is a major component of the Pseudomonas aeruginosa type III secretion needle
    • Pastor, A., Chabert, J., Louwagie, M., Garin, J., and Attree, I. (2005). PscF is a major component of the Pseudomonas aeruginosa type III secretion needle. FEMS Microbiol. Lett. 253, 95-101.
    • (2005) FEMS Microbiol. Lett. , vol.253 , pp. 95-101
    • Pastor, A.1    Chabert, J.2    Louwagie, M.3    Garin, J.4    Attree, I.5
  • 179
    • 0031973716 scopus 로고    scopus 로고
    • The AAA team: related ATPases with diverse functions
    • Patel, S., and Latterich, M. (1998). The AAA team: related ATPases with diverse functions. Trends Cell Biol. 8, 65-71.
    • (1998) Trends Cell Biol , vol.8 , pp. 65-71
    • Patel, S.1    Latterich, M.2
  • 182
    • 0035957004 scopus 로고    scopus 로고
    • Phylogeny of genes for secretion NTPases: identification of the wide-spread tadA subfamily and development of a diagnostic key for gene classification
    • Planet, P. J., Kachlany, S. C., DeSalle, R., and Figurski, D. H. (2001). Phylogeny of genes for secretion NTPases: identification of the wide-spread tadA subfamily and development of a diagnostic key for gene classification. Proc. Natl. Acad. Sci. U.S.A. 98, 2503-2508.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 2503-2508
    • Planet, P.J.1    Kachlany, S.C.2    DeSalle, R.3    Figurski, D.H.4
  • 183
    • 77954394940 scopus 로고    scopus 로고
    • Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa
    • Ple, S., Job, V., Dessen, A., and Attree, I. (2010). Cochaperone interactions in export of the type III needle component PscF of Pseudomonas aeruginosa. J. Bacteriol. 192, 3801-3808.
    • (2010) J. Bacteriol. , vol.192 , pp. 3801-3808
    • Ple, S.1    Job, V.2    Dessen, A.3    Attree, I.4
  • 184
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner, J., Halter, R., Beyreuther, K., and Meyer, T. F. (1987). Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 325, 458-462.
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 185
    • 0028242862 scopus 로고
    • Molecular characterization of PulE, a protein required for pullulanase secretion
    • Possot, O., and Pugsley, A. P. (1994). Molecular characterization of PulE, a protein required for pullulanase secretion. Mol. Microbiol. 12, 287-299.
    • (1994) Mol. Microbiol. , vol.12 , pp. 287-299
    • Possot, O.1    Pugsley, A.P.2
  • 187
    • 34848882221 scopus 로고    scopus 로고
    • Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin
    • Pukatzki, S., Ma, A. T., Revel, A. T., Sturtevant, D., and Mekalanos, J. J. (2007). Type VI secretion system translocates a phage tail spike-like protein into target cells where it cross-links actin. Proc. Natl. Acad. Sci. U.S.A. 104, 15508-15513.
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 15508-15513
    • Pukatzki, S.1    Ma, A.T.2    Revel, A.T.3    Sturtevant, D.4    Mekalanos, J.J.5
  • 189
    • 33845924185 scopus 로고    scopus 로고
    • Interstrain transfer of the large pathogenicity island (PAPI-1) of Pseudomonas aeruginosa
    • Qiu, X., Gurkar, A. U., and Lory, S. (2006). Interstrain transfer of the large pathogenicity island (PAPI-1) of Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U.S.A. 103, 19830-19835.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 19830-19835
    • Qiu, X.1    Gurkar, A.U.2    Lory, S.3
  • 191
    • 77957813869 scopus 로고    scopus 로고
    • Structure of the cholera toxin secretion channel in its closed state
    • Reichow, S. L., Korotkov, K. V., Hol, W. G., and Gonen, T. (2010). Structure of the cholera toxin secretion channel in its closed state. Nat. Struct. Mol. Biol. 17, 1226-1232.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1226-1232
    • Reichow, S.L.1    Korotkov, K.V.2    Hol, W.G.3    Gonen, T.4
  • 192
    • 26844457990 scopus 로고    scopus 로고
    • Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa
    • Robert, V., Filloux, A., and Michel, G. P. (2005a). Subcomplexes from the Xcp secretion system of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 252, 43-50.
    • (2005) FEMS Microbiol. Lett. , vol.252 , pp. 43-50
    • Robert, V.1    Filloux, A.2    Michel, G.P.3
  • 193
    • 26044455889 scopus 로고    scopus 로고
    • Role of XcpP in the functionality of the Pseudomonas aeruginosa secreton
    • Robert, V., Filloux, A., and Michel, G. P. (2005b). Role of XcpP in the functionality of the Pseudomonas aeruginosa secreton. Res. Microbiol. 156, 880-886.
    • (2005) Res. Microbiol. , vol.156 , pp. 880-886
    • Robert, V.1    Filloux, A.2    Michel, G.P.3
  • 194
    • 0141862137 scopus 로고    scopus 로고
    • Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae
    • Robien, M. A., Krumm, B. E., Sandkvist, M., and Hol, W. G. (2003). Crystal structure of the extracellular protein secretion NTPase EpsE of Vibrio cholerae. J. Mol. Biol. 333, 657-674.
    • (2003) J. Mol. Biol. , vol.333 , pp. 657-674
    • Robien, M.A.1    Krumm, B.E.2    Sandkvist, M.3    Hol, W.G.4
  • 197
    • 54349103449 scopus 로고    scopus 로고
    • The P-usher, a novel protein transporter involved in fimbrial assembly and TpsA secretion
    • Ruer, S., Ball, G., Filloux, A., and de Bentzmann, S. (2008). The "P-usher", a novel protein trans-porter involved in fimbrial assembly and TpsA secretion. EMBO J. 27, 2669-2680.
    • (2008) EMBO J , vol.27 , pp. 2669-2680
    • Ruer, S.1    Ball, G.2    Filloux, A.3    de Bentzmann, S.4
  • 198
    • 0034805637 scopus 로고    scopus 로고
    • Role of Agrobacterium VirB11 ATPase in T-pilus assembly and substrate selection
    • Sagulenko, E., Sagulenko, V., Chen, J., and Christie, P. J. (2001). Role of Agrobacterium VirB11 ATPase in T-pilus assembly and substrate selection. J. Bacteriol. 183, 5813-5825.
    • (2001) J. Bacteriol. , vol.183 , pp. 5813-5825
    • Sagulenko, E.1    Sagulenko, V.2    Chen, J.3    Christie, P.J.4
  • 199
    • 34447116519 scopus 로고    scopus 로고
    • Protein secretion and membrane insertion systems in gram-negative bacteria
    • Saier, M. H. Jr. (2006). Protein secretion and membrane insertion systems in gram-negative bacteria. J. Membr. Biol. 214, 75-90.
    • (2006) J. Membr. Biol. , vol.214 , pp. 75-90
    • Saier Jr, M.H.1
  • 201
    • 77952850206 scopus 로고    scopus 로고
    • SecA: a tale of two protomers
    • Sardis, M. F., and Economou, A. (2010). SecA: a tale of two protomers. Mol. Microbiol. 76, 1070-1081.
    • (2010) Mol. Microbiol. , vol.76 , pp. 1070-1081
    • Sardis, M.F.1    Economou, A.2
  • 202
    • 36749045913 scopus 로고    scopus 로고
    • The twin-arginine transport system: moving folded proteins across membranes
    • Sargent, F. (2007). The twin-arginine transport system: moving folded proteins across membranes. Biochem. Soc. Trans. 35, 835-847.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 835-847
    • Sargent, F.1
  • 203
    • 4444342607 scopus 로고    scopus 로고
    • ExoU is a potent intracellular phospholipase
    • Sato, H., and Frank, D. W. (2004). ExoU is a potent intracellular phospholipase. Mol. Microbiol. 53, 1279-1290.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1279-1290
    • Sato, H.1    Frank, D.W.2
  • 205
    • 0034657719 scopus 로고    scopus 로고
    • Pilus formation and protein secretion by the same machinery in Escherichia coli
    • Sauvonnet, N., Vignon, G., Pugsley, A. P., and Gounon, P. (2000). Pilus formation and protein secretion by the same machinery in Escherichia coli. EMBO J. 19, 2221-2228.
    • (2000) EMBO J , vol.19 , pp. 2221-2228
    • Sauvonnet, N.1    Vignon, G.2    Pugsley, A.P.3    Gounon, P.4
  • 206
    • 0032907634 scopus 로고    scopus 로고
    • Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury
    • Sawa, T., Yahr, T. L., Ohara, M., Kurahashi, K., Gropper, M. A., Wiener-Kronish, J. P., and Frank, D. W. (1999). Active and passive immunization with the Pseudomonas V antigen protects against type III intoxication and lung injury. Nat. Med. 5, 392-398.
    • (1999) Nat. Med. , vol.5 , pp. 392-398
    • Sawa, T.1    Yahr, T.L.2    Ohara, M.3    Kurahashi, K.4    Gropper, M.A.5    Wiener-Kronish, J.P.6    Frank, D.W.7
  • 207
    • 0038799733 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains
    • Schmitt, L., Benabdelhak, H., Blight, M. A., Holland, I. B., and Stubbs, M. T. (2003). Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains. J. Mol. Biol. 330, 333-342.
    • (2003) J. Mol. Biol. , vol.330 , pp. 333-342
    • Schmitt, L.1    Benabdelhak, H.2    Blight, M.A.3    Holland, I.B.4    Stubbs, M.T.5
  • 208
    • 0141642035 scopus 로고    scopus 로고
    • Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas
    • Schoehn, G., Di Guilmi, A. M., Lemaire, D., Attree, I., Weissenhorn, W., and Dessen, A. (2003). Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22, 4957-4967.
    • (2003) EMBO J , vol.22 , pp. 4957-4967
    • Schoehn, G.1    Di Guilmi, A.M.2    Lemaire, D.3    Attree, I.4    Weissenhorn, W.5    Dessen, A.6
  • 210
    • 79952262440 scopus 로고    scopus 로고
    • Three-dimensional model of Salmonellas needle complex at subnanometer resolution
    • Schraidt, O., and Marlovits, T. C. (2011). Three-dimensional model of Salmonellas needle complex at subnanometer resolution. Science 331, 1192-1195.
    • (2011) Science , vol.331 , pp. 1192-1195
    • Schraidt, O.1    Marlovits, T.C.2
  • 211
    • 55549109423 scopus 로고    scopus 로고
    • Polar secretion of proteins via the Xcp type II secretion system in Pseudomonas aeruginosa
    • Senf, F., Tommassen, J., and Koster, M. (2008). Polar secretion of proteins via the Xcp type II secretion system in Pseudomonas aeruginosa. Microbiology 154, 3025-3032.
    • (2008) Microbiology , vol.154 , pp. 3025-3032
    • Senf, F.1    Tommassen, J.2    Koster, M.3
  • 212
    • 0036112267 scopus 로고    scopus 로고
    • Type IVB secretion by intracellular pathogens
    • Sexton, J. A., and Vogel, J. P. (2002). Type IVB secretion by intracellular pathogens. Traffic 3, 178-185.
    • (2002) Traffic , vol.3 , pp. 178-185
    • Sexton, J.A.1    Vogel, J.P.2
  • 214
    • 0031736546 scopus 로고    scopus 로고
    • Functional characterization of the Erwinia chrysanthemi OutS protein,an element of a type II secretion system
    • Shevchik, V. E., and Condemine, G. (1998). Functional characterization of the Erwinia chrysanthemi OutS protein,an element of a type II secretion system. Microbiology 144 (Pt 11): 3219-3228.
    • (1998) Microbiology , vol.144 , Issue.PART 11 , pp. 3219-3228
    • Shevchik, V.E.1    Condemine, G.2
  • 215
    • 0030911423 scopus 로고    scopus 로고
    • Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins
    • Shevchik, V. E., Robert-Baudouy, J., and Condemine, G. (1997). Specific interaction between OutD, an Erwinia chrysanthemi outer membrane protein of the general secretory pathway, and secreted proteins. EMBO J. 16, 3007-3016.
    • (1997) EMBO J , vol.16 , pp. 3007-3016
    • Shevchik, V.E.1    Robert-Baudouy, J.2    Condemine, G.3
  • 218
    • 73849101081 scopus 로고    scopus 로고
    • A type VI secretion system effector protein, VgrG1, from Aeromonas hydrophila that induces host cell toxicity by ADP ribosylation of actin
    • Suarez, G., Sierra, J. C., Erova, T. E., Sha, J., Horneman, A. J., and Chopra, A. K. (2010). A type VI secretion system effector protein, VgrG1, from Aeromonas hydrophila that induces host cell toxicity by ADP ribosylation of actin. J. Bacteriol. 192, 155-168.
    • (2010) J. Bacteriol. , vol.192 , pp. 155-168
    • Suarez, G.1    Sierra, J.C.2    Erova, T.E.3    Sha, J.4    Horneman, A.J.5    Chopra, A.K.6
  • 220
    • 0032538793 scopus 로고    scopus 로고
    • Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translo-case to an outer membrane exit pore
    • Thanabalu, T., Koronakis, E., Hughes, C., and Koronakis, V. (1998). Substrate-induced assembly of a contiguous channel for protein export from E. coli: reversible bridging of an inner-membrane translo-case to an outer membrane exit pore. EMBO J. 17, 6487-6496.
    • (1998) EMBO J , vol.17 , pp. 6487-6496
    • Thanabalu, T.1    Koronakis, E.2    Hughes, C.3    Koronakis, V.4
  • 221
    • 0346252347 scopus 로고    scopus 로고
    • Attachment to and biofilm formation on abiotic surfaces by Acinetobacter baumannii: involvement of a novel chaperoneusher pili assembly system
    • Tomaras, A. P., Dorsey, C. W., Edelmann, R. E., and Actis, L. A. (2003). Attachment to and biofilm formation on abiotic surfaces by Acinetobacter baumannii: involvement of a novel chaperone-usher pili assembly system. Microbiology 149, 3473-3484.
    • (2003) Microbiology , vol.149 , pp. 3473-3484
    • Tomaras, A.P.1    Dorsey, C.W.2    Edelmann, R.E.3    Actis, L.A.4
  • 224
    • 0027208681 scopus 로고
    • Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate extracellular protein secretion and pilus bio-genesis in Pseudomonas aeruginosa
    • Turner, L. R., Lara, J. C., Nunn, D. N., and Lory, S. (1993). Mutations in the consensus ATP-binding sites of XcpR and PilB eliminate extracellular protein secretion and pilus bio-genesis in Pseudomonas aeruginosa. J. Bacteriol. 175, 4962-4969.
    • (1993) J. Bacteriol. , vol.175 , pp. 4962-4969
    • Turner, L.R.1    Lara, J.C.2    Nunn, D.N.3    Lory, S.4
  • 225
    • 0035811059 scopus 로고    scopus 로고
    • The chaperone/usher pathways of Pseudomonas aeruginosa: identification of fimbrial gene clusters (cup) and their involvement in biofilm formation
    • Vallet, I., Olson, J. W., Lory, S., Laz-dunski, A., and Filloux, A. (2001). The chaperone/usher pathways of Pseudomonas aeruginosa: identification of fimbrial gene clusters (cup) and their involvement in biofilm formation. Proc. Natl. Acad. Sci. U.S.A. 98, 6911-6916.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 6911-6916
    • Vallet, I.1    Olson, J.W.2    Lory, S.3    Laz-dunski, A.4    Filloux, A.5
  • 226
    • 77949323924 scopus 로고    scopus 로고
    • Crystal structure of a full-length autotransporter
    • van den Berg, B. (2010). Crystal structure of a full-length autotransporter. J. Mol. Biol. 396, 627-633.
    • (2010) J. Mol. Biol. , vol.396 , pp. 627-633
    • van den Berg, B.1
  • 227
    • 53649103131 scopus 로고    scopus 로고
    • Two-partner secretion systems of Neisseria menin-gitidis associated with invasive clonal complexes
    • van Ulsen, P., Rutten, L., Feller, M., Tommassen, J., and van der Ende, A. (2008). Two-partner secretion systems of Neisseria menin-gitidis associated with invasive clonal complexes. Infect. Immun. 76, 4649-4658.
    • (2008) Infect. Immun. , vol.76 , pp. 4649-4658
    • van Ulsen, P.1    Rutten, L.2    Feller, M.3    Tommassen, J.4    van der Ende, A.5
  • 228
    • 1242341934 scopus 로고    scopus 로고
    • The opportunistic pathogen Pseudomonas aeruginosa carries a secretable arachidonate 15-lipoxygenase
    • Vance, R. E., Hong, S., Gronert, K., Serhan, C. N., and Mekalanos, J. J. (2004). The opportunistic pathogen Pseudomonas aeruginosa carries a secretable arachidonate 15-lipoxygenase. Proc. Natl. Acad. Sci. U.S.A. 101, 2135-2139.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2135-2139
    • Vance, R.E.1    Hong, S.2    Gronert, K.3    Serhan, C.N.4    Mekalanos, J.J.5
  • 229
    • 71749120639 scopus 로고    scopus 로고
    • HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor
    • Viarre, V., Cascales, E., Ball, G., Michel, G. P., Filloux, A., and Voulhoux, R. (2009). HxcQ liposecretin is self-piloted to the outer membrane by its N-terminal lipid anchor. J. Biol. Chem. 284, 33815-33823.
    • (2009) J. Biol. Chem. , vol.284 , pp. 33815-33823
    • Viarre, V.1    Cascales, E.2    Ball, G.3    Michel, G.P.4    Filloux, A.5    Voulhoux, R.6
  • 230
    • 0021856417 scopus 로고
    • Signal sequences -the limits of variation
    • Vonheijne, G. (1985). Signal sequences -the limits of variation. J. Mol. Biol. 184, 99-105.
    • (1985) J. Mol. Biol. , vol.184 , pp. 99-105
    • Vonheijne, G.1
  • 231
    • 0035803406 scopus 로고    scopus 로고
    • Involvement of the twin-arginine translocation system in protein secretion via the type II pathway
    • Voulhoux, R., Ball, G., Ize, B., Vasil, M. L., Lazdunski, A., Wu, L. F., and Fil-loux, A. (2001). Involvement of the twin-arginine translocation system in protein secretion via the type II pathway. EMBO J. 20, 6735-6741.
    • (2001) EMBO J , vol.20 , pp. 6735-6741
    • Voulhoux, R.1    Ball, G.2    Ize, B.3    Vasil, M.L.4    Lazdunski, A.5    Wu, L.F.6    Fil-loux, A.7
  • 232
    • 0033917666 scopus 로고    scopus 로고
    • Influence of deletions within domain II of exotoxin A on its extra-cellular secretion from Pseudomonas aeruginosa
    • Voulhoux, R., Taupiac, M. P., Czjzek, M., Beaumelle, B., and Filloux, A. (2000). Influence of deletions within domain II of exotoxin A on its extra-cellular secretion from Pseudomonas aeruginosa. J. Bacteriol. 182, 4051-4058.
    • (2000) J. Bacteriol. , vol.182 , pp. 4051-4058
    • Voulhoux, R.1    Taupiac, M.P.2    Czjzek, M.3    Beaumelle, B.4    Filloux, A.5
  • 233
    • 70350211420 scopus 로고    scopus 로고
    • Structural biology of the chaperone-usher pathway of pilus biogenesis
    • Waksman,G.,and Hultgren,S. J. (2009). Structural biology of the chaperone-usher pathway of pilus biogenesis. Nat. Rev. Microbiol. 7, 765-774.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 765-774
    • Waksman, G.1    Hultgren, S.J.2
  • 234
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to hemophores
    • Wandersman, C., and Delepelaire, P. (2004). Bacterial iron sources: from siderophores to hemophores. Annu. Rev. Microbiol. 58, 611-647.
    • (2004) Annu. Rev. Microbiol. , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 235
    • 0032721432 scopus 로고    scopus 로고
    • A novel lipolytic enzyme located in the outer mem-brane of Pseudomonas aeruginosa
    • Wilhelm, S., Tommassen, J., and Jaeger, K. E. (1999). A novel lipolytic enzyme located in the outer mem-brane of Pseudomonas aeruginosa. J. Bacteriol. 181, 6977-6986.
    • (1999) J. Bacteriol. , vol.181 , pp. 6977-6986
    • Wilhelm, S.1    Tommassen, J.2    Jaeger, K.E.3
  • 236
    • 0029968272 scopus 로고    scopus 로고
    • Adaptation of a conjugal transfer system for the export of pathogenic macromolecules
    • Winans, S. C., Burns, D. L., and Christie, P. J. (1996). Adaptation of a conjugal transfer system for the export of pathogenic macromolecules. Trends Microbiol. 4, 64-68.
    • (1996) Trends Microbiol , vol.4 , pp. 64-68
    • Winans, S.C.1    Burns, D.L.2    Christie, P.J.3
  • 237
    • 0026700544 scopus 로고
    • Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1
    • Wohlfarth, S., Hoesche, C., Strunk, C., and Winkler, U. K. (1992). Molecular genetics of the extracellular lipase of Pseudomonas aeruginosa PAO1. J. Gen. Microbiol. 138, 1325-1335.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 1325-1335
    • Wohlfarth, S.1    Hoesche, C.2    Strunk, C.3    Winkler, U.K.4
  • 238
    • 0034406525 scopus 로고    scopus 로고
    • Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili
    • Wolfgang, M., van Putten, J. P., Hayes, S. F., Dorward, D., and Koomey, M. (2000). Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J. 19, 6408-6418.
    • (2000) EMBO J , vol.19 , pp. 6408-6418
    • Wolfgang, M.1    van Putten, J.P.2    Hayes, S.F.3    Dorward, D.4    Koomey, M.5
  • 239
    • 0038153119 scopus 로고    scopus 로고
    • Conservation of genome content and virulence determinants among clinical and environmental isolates of Pseudomonas aeruginosa
    • Wolfgang, M. C., Kulasekara, B. R., Liang, X., Boyd, D., Wu, K., Yang, Q., Miyada, C. G., and Lory, S. (2003). Conservation of genome content and virulence determinants among clinical and environmental isolates of Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. U.S.A. 100, 8484-8489.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 8484-8489
    • Wolfgang, M.C.1    Kulasekara, B.R.2    Liang, X.3    Boyd, D.4    Wu, K.5    Yang, Q.6    Miyada, C.G.7    Lory, S.8
  • 241
    • 0021187550 scopus 로고
    • Genetic mapping and characterization of Pseudomonas aeruginosa mutants defective in the formation of extracellular proteins
    • Wretlind, B., and Pavlovskis, O. R. (1984). Genetic mapping and characterization of Pseudomonas aeruginosa mutants defective in the formation of extracellular proteins. J. Bacteriol. 158, 801-808.
    • (1984) J. Bacteriol. , vol.158 , pp. 801-808
    • Wretlind, B.1    Pavlovskis, O.R.2
  • 242
    • 0029801248 scopus 로고    scopus 로고
    • Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway
    • Yahr, T. L., Goranson, J., and Frank, D. W. (1996). Exoenzyme S of Pseudomonas aeruginosa is secreted by a type III pathway. Mol. Microbiol. 22, 991-1003.
    • (1996) Mol. Microbiol. , vol.22 , pp. 991-1003
    • Yahr, T.L.1    Goranson, J.2    Frank, D.W.3
  • 243
    • 0030731178 scopus 로고    scopus 로고
    • Identification of type III secreted products of the Pseudomonas aeruginosa exoenzyme S regulon
    • Yahr, T. L., Mende-Mueller, L. M., Friese, M. B.,and Frank,D. W. (1997). Identification of type III secreted products of the Pseudomonas aeruginosa exoenzyme S regulon. J. Bacteriol. 179, 7165-7168.
    • (1997) J. Bacteriol. , vol.179 , pp. 7165-7168
    • Yahr, T.L.1    Mende-Mueller, L.M.2    Friese, M.B.3    Frank, D.W.4
  • 245
    • 73149122099 scopus 로고    scopus 로고
    • The baseplate wedges of bacterio-phage T4 spontaneously assemble into hubless baseplate-like structure in vitro
    • Yap, M. L., Mio, K., Leiman, P. G., Kanamaru, S., and Arisaka, F. (2010). The baseplate wedges of bacterio-phage T4 spontaneously assemble into hubless baseplate-like structure in vitro. J. Mol. Biol. 395, 349-360.
    • (2010) J. Mol. Biol. , vol.395 , pp. 349-360
    • Yap, M.L.1    Mio, K.2    Leiman, P.G.3    Kanamaru, S.4    Arisaka, F.5
  • 246
    • 48149101623 scopus 로고    scopus 로고
    • Common themes and variations in serine protease autotransporters
    • Yen, Y. T., Kostakioti, M., Henderson, I. R., and Stathopoulos, C. (2008). Common themes and variations in serine protease autotransporters. Trends Microbiol. 16, 370-379.
    • (2008) Trends Microbiol , vol.16 , pp. 370-379
    • Yen, Y.T.1    Kostakioti, M.2    Henderson, I.R.3    Stathopoulos, C.4
  • 247
    • 0033033304 scopus 로고    scopus 로고
    • A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system
    • Young,G. M.,Schmiel,D. H.,and Miller, V. L. (1999). A new pathway for the secretion of virulence factors by bacteria: the flagellar export apparatus functions as a protein-secretion system. Proc. Natl. Acad. Sci. U.S.A. 96, 6456-6461.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 6456-6461
    • Young, G.M.1    Schmiel, D.H.2    Miller, V.L.3
  • 248
    • 77955237448 scopus 로고    scopus 로고
    • Kinetic and spectroscopic studies of hemin acquisition in the hemophore HasAp from Pseudomonas aeruginosa
    • Yukl, E. T., Jepkorir, G., Alontaga, A. Y., Pautsch, L., Rodriguez, J. C., Rivera, M., and Moenne-Loccoz, P. (2010). Kinetic and spectroscopic studies of hemin acquisition in the hemophore HasAp from Pseudomonas aeruginosa. Biochemistry 49, 6646-6654.
    • (2010) Biochemistry , vol.49 , pp. 6646-6654
    • Yukl, E.T.1    Jepkorir, G.2    Alontaga, A.Y.3    Pautsch, L.4    Rodriguez, J.C.5    Rivera, M.6    Moenne-Loccoz, P.7
  • 249
    • 0029154874 scopus 로고
    • Genetic analysis of the colicin V secretion pathway
    • Zhang, L. H., Fath, M. J., Mahanty, H. K., Tai, P. C., and Kolter, R. (1995). Genetic analysis of the colicin V secretion pathway. Genetics 141, 25-32.
    • (1995) Genetics , vol.141 , pp. 25-32
    • Zhang, L.H.1    Fath, M.J.2    Mahanty, H.K.3    Tai, P.C.4    Kolter, R.5
  • 250
    • 0029905197 scopus 로고    scopus 로고
    • Processing of colicin V-1, a secretable marker protein of a bacterial ATP binding cassette export system, requires membrane integrity, energy, and cytosolic factors
    • Zhong, X., Kolter, R., and Tai, P. C. (1996). Processing of colicin V-1, a secretable marker protein of a bacterial ATP binding cassette export system, requires membrane integrity, energy, and cytosolic factors. J. Biol. Chem. 271, 28057-28063.
    • (1996) J. Biol. Chem , vol.271 , pp. 28057-28063
    • Zhong, X.1    Kolter, R.2    Tai, P.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.