메뉴 건너뛰기




Volumn 4, Issue 11, 2006, Pages 811-825

The type III secretion injectisome

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; NANOPARTICLE;

EID: 33750110911     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro1526     Document Type: Review
Times cited : (849)

References (155)
  • 1
    • 0031026828 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells
    • Cornelis, G. R. & Wolf-Watz, H. The Yersinia Yop virulon: A bacterial system for subverting eukaryotic cells. Mol. Microbiol. 23, 861-867 (1997).
    • (1997) Mol. Microbiol. , vol.23 , pp. 861-867
    • Cornelis, R.1    Wolf-Watz, H.2
  • 2
    • 0033591446 scopus 로고    scopus 로고
    • Type III secretion machines: Bacterial devices for protein delivery into host cells
    • Galan, J. E. & Collmer, A. Type III secretion machines: Bacterial devices for protein delivery into host cells. Science 284, 1322-1328 (1999).
    • (1999) Science , vol.284 , pp. 1322-1328
    • Galan, J.E.1    Collmer, A.2
  • 3
    • 0033764483 scopus 로고    scopus 로고
    • Assembly and function of type III secretory systems
    • Cornelis, G. R. & Van Gijsegem, F. Assembly and function of type III secretory systems. Annu. Rev. Microbiol. 54, 735-774 (2000).
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 4
    • 21344453525 scopus 로고    scopus 로고
    • The bacterial injection kit: Type III secretion systems
    • Mota, L. J. & Cornelis, G. R. The bacterial injection kit: Type III secretion systems. Ann. Med. 37, 234-249 (2005).
    • (2005) Ann. Med. , vol.37 , pp. 234-249
    • Mota, L.J.1    Cornelis, G.R.2
  • 5
    • 4744364745 scopus 로고    scopus 로고
    • Type III secretion system effector proteins: Double agents in bacterial disease and plant defense
    • Alfano, J. R. & Collmer, A. Type III secretion system effector proteins: double agents in bacterial disease and plant defense. Annu. Rev. Phytopathol. 42, 385-414 (2004).
    • (2004) Annu. Rev. Phytopathol. , vol.42 , pp. 385-414
    • Alfano, J.R.1    Collmer, A.2
  • 6
    • 33750097480 scopus 로고    scopus 로고
    • Subterfuge and manipulation: Type III effector proteins of phytopathogenic bacteria
    • 5 June [epub ahead of print]
    • Grant, S. R., Fisher, E. J., Chang, J. H., Mole, B. M. & Dangl, J. L. Subterfuge and manipulation: Type III effector proteins of phytopathogenic bacteria. Annu. Rev. Microbiol. 5 June 2006 [epub ahead of print].
    • (2006) Annu. Rev. Microbiol.
    • Grant, S.R.1    Fisher, E.J.2    Chang, J.H.3    Mole, B.M.4    Dangl, J.L.5
  • 7
    • 33645976151 scopus 로고    scopus 로고
    • New structural insights into the bacterial type III secretion system
    • Yip, C. K. & Strynadka, N. C. New structural insights into the bacterial type III secretion system. Trends Biochem. Sci. 31, 223-230 (2006).
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 223-230
    • Yip, C.K.1    Strynadka, N.C.2
  • 8
    • 0028951802 scopus 로고
    • The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex
    • Van Gijsegem, F. et al. The hrp gene locus of Pseudomonas solanacearum, which controls the production of a type III secretion system, encodes eight proteins related to components of the bacterial flagellar biogenesis complex. Mol. Microbiol. 15, 1095-1114 (1995).
    • (1995) Mol. Microbiol. , vol.15 , pp. 1095-1114
    • Van Gijsegem, F.1
  • 9
    • 0028178610 scopus 로고
    • 2+ response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis
    • 2+ response (LCR) secretion (ysc) locus lies within the lcrB region of the LCR plasmid in Yersinia pestis. J. Bacteriol. 176, 569-579 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 569-579
    • Fields, K.A.1    Plano, G.V.2    Straley, S.C.3
  • 10
    • 0028292926 scopus 로고
    • YscN, the putative energizer of the Yersinia Yop secretion machinery
    • Woestyn, S., Allaoui, A., Wattiau, P. & Cornelis, G. R. YscN, the putative energizer of the Yersinia Yop secretion machinery. J. Bacteriol. 176, 1561-1569 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 1561-1569
    • Woestyn, S.1    Allaoui, A.2    Wattiau, P.3    Cornelis, G.R.4
  • 11
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab, R. M. How bacteria assemble flagella. Annu. Rev. Microbiol. 57, 77-100 (2003).
    • (2003) Annu. Rev. Microbiol. , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 12
    • 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. & Miller, V. L. 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. USA 96, 6456-6461 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6456-6461
    • Young, G.M.1    Schmiel, D.H.2    Miller, V.L.3
  • 13
    • 0032562678 scopus 로고    scopus 로고
    • Supramolecular structure of the Salmonella typhimurium type III protein secretion system
    • Kubori, T. et al. Supramolecular structure of the Salmonella typhimurium type III protein secretion system. Science 280, 602-605 (1998).
    • (1998) Science , vol.280 , pp. 602-605
    • Kubori, T.1
  • 14
    • 0141430076 scopus 로고    scopus 로고
    • Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events
    • Gophna, U., Ron, E. Z. & Graur, D. Bacterial type III secretion systems are ancient and evolved by multiple horizontal-transfer events. Gene 312, 151-163 (2003).
    • (2003) Gene , vol.312 , pp. 151-163
    • Gophna, U.1    Ron, E.Z.2    Graur, D.3
  • 15
    • 15944409588 scopus 로고    scopus 로고
    • Bioinformatics, genomics and evolution of nonflagellar type III secretion systems: A Darwinian perspective
    • Pallen, M. J., Beatson, S. A. & Bailey, C. M. Bioinformatics, genomics and evolution of nonflagellar type III secretion systems: A Darwinian perspective. FEMS Microbiol. Rev. 29, 201-229 (2005).
    • (2005) FEMS Microbiol Rev. , vol.29 , pp. 201-229
    • Pallen, M.J.1    Beatson, S.A.2    Bailey, C.M.3
  • 16
    • 26844521751 scopus 로고    scopus 로고
    • Type III secretion: More systems than you think
    • Troisfontaines, P. & Cornelis, G. R. Type III secretion: More systems than you think. Physiology (Bethesda) 20, 326-339 (2005).
    • (2005) Physiology (Bethesda) , vol.20 , pp. 326-339
    • Troisfontaines, P.1    Cornelis, G.R.2
  • 17
    • 0035877065 scopus 로고    scopus 로고
    • Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections
    • Roy-Burman, A. et al. Type III protein secretion is associated with death in lower respiratory and systemic Pseudomonas aeruginosa infections. J. Infect. Dis. 183, 1767-1774 (2001).
    • (2001) J. Infect. Dis. , vol.183 , pp. 1767-1774
    • Roy-Burman, A.1
  • 18
    • 1442283765 scopus 로고    scopus 로고
    • Association of type III secretion genes with virulence of Aeromonas salmonicida subsp. salmonicida
    • Burr, S. E., Wahli, T., Segner, H., Pugovkin, D. & Frey, J. Association of type III secretion genes with virulence of Aeromonas salmonicida subsp. salmonicida. Dis. Aquat. Organ. 57, 167-171 (2003).
    • (2003) Dis. Aquat. Organ. , vol.57 , pp. 167-171
    • Burr, S.E.1    Wahli, T.2    Segner, H.3    Pugovkin, D.4    Frey, J.5
  • 19
    • 0035675043 scopus 로고    scopus 로고
    • Salmonella entry into host cells: The work in concert of type III secreted effector proteins
    • Zhou, D. & Galan, J. Salmonella entry into host cells: The work in concert of type III secreted effector proteins. Microbes Infect. 3, 1293-1298 (2001).
    • (2001) Microbes Infect. , vol.3 , pp. 1293-1298
    • Zhou, D.1    Galan, J.2
  • 20
    • 0042195926 scopus 로고    scopus 로고
    • Functions and effectors of the Salmonella pathogenicity island 2 type III secretion system
    • Waterman, S. R. & Holden, D. W. Functions and effectors of the Salmonella pathogenicity island 2 type III secretion system. Cell Microbiol. 5, 501-511 (2003).
    • (2003) Cell Microbiol. , vol.5 , pp. 501-511
    • Waterman, S.R.1    Holden, D.W.2
  • 21
    • 0035949491 scopus 로고    scopus 로고
    • Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheathlike structure
    • Sekiya, K. et al. Supermolecular structure of the enteropathogenic Escherichia coli type III secretion system and its direct interaction with the EspA-sheath-like structure. Proc. Natl Acad. Sci. USA 98, 11638-11643 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11638-11643
    • Sekiya, K.1
  • 22
    • 0034254475 scopus 로고    scopus 로고
    • Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors
    • Tamano, K. et al. Supramolecular structure of the Shigella type III secretion machinery: The needle part is changeable in length and essential for delivery of effectors. EMBO J. 19, 3876-3887 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3876-3887
    • Tamano, K.1
  • 23
    • 0033230438 scopus 로고    scopus 로고
    • The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes
    • Blocker, A. et al. The tripartite type III secreton of Shigella flexneri inserts IpaB and IpaC into host membranes. J. Cell Biol. 147, 683-693. (1999).
    • (1999) J. Cell Biol. , vol.147 , pp. 683-693
    • Blocker, A.1
  • 24
    • 0034718542 scopus 로고    scopus 로고
    • Contribution of Salmonella typhimurium type III secretion components to needle complex formation
    • Kimbrough, T. G. & Miller, S. I. Contribution of Salmonella typhimurium type III secretion components to needle complex formation. Proc. Natl Acad. Sci. USA 97, 11008-11013 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 11008-11013
    • Kimbrough, T.G.1    Miller, S.I.2
  • 25
    • 0035206531 scopus 로고    scopus 로고
    • The filamentous type III secretion translocon of enteropathogenic Escherichia coli
    • Daniell, S. J. et al. The filamentous type III secretion translocon of enteropathogenic Escherichia coli. Cell Microbiol. 3, 865-871 (2001).
    • (2001) Cell Microbiol. , vol.3 , pp. 865-871
    • Daniell, S.J.1
  • 26
    • 33645985137 scopus 로고    scopus 로고
    • Assembly of the type III secretion apparatus of enteropathogenic Escherichia coli
    • Ogino, T. et al. Assembly of the type III secretion apparatus of enteropathogenic Escherichia coli. J. Bacteriol. 188, 2801-2811 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 2801-2811
    • Ogino, T.1
  • 27
    • 33644860766 scopus 로고    scopus 로고
    • Shigella Spa33 is an essential C-ring component of type III secretion machinery
    • Morita-Ishihara, T. et al. Shigella Spa33 is an essential C-ring component of type III secretion machinery. J. Biol. Chem. 281, 599-607 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 599-607
    • Morita-Ishihara, T.1
  • 28
    • 0035133489 scopus 로고    scopus 로고
    • Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton
    • Blocker, A. et al. Structure and composition of the Shigella flexneri 'needle complex', a part of its type III secreton. Mol. Microbiol. 39, 652-663 (2001).
    • (2001) Mol. Microbiol. , vol.39 , pp. 652-663
    • Blocker, A.1
  • 29
    • 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. & Cornelis, G. R. SycE allows secretion of YopE-DHFR hybrids by the Yersinia enterocolitica type III Ysc system. Mol. Microbiol. 46, 1183-1197 (2002).
    • (2002) Mol. Microbiol. , vol.46 , pp. 1183-1197
    • Feldman, M.F.1    Muller, S.2    Wuest, E.3    Cornelis, G.R.4
  • 30
    • 8344258355 scopus 로고    scopus 로고
    • Structural insights into the assembly of the type III secretion needle complex
    • Marlovits, T. C. et al. Structural insights into the assembly of the type III secretion needle complex. Science 306, 1040-1042 (2004).
    • (2004) Science , vol.306 , pp. 1040-1042
    • Marlovits, T.C.1
  • 31
    • 12244302174 scopus 로고    scopus 로고
    • Variable symmetry in Salmonella typhimurium flagellar motors
    • Young, H. S., Dang, H., Lai, Y., DeRosier, D. J. & Khan, S. Variable symmetry in Salmonella typhimurium flagellar motors. Biophys. J. 84, 571-577 (2003).
    • (2003) Biophys. J. , vol.84 , pp. 571-577
    • Young, H.S.1    Dang, H.2    Lai, Y.3    DeRosier, D.J.4    Khan, S.5
  • 32
    • 0029998799 scopus 로고    scopus 로고
    • Unified nomenclature for broadly conserved hrp genes of phytopathogenic bacteria
    • Bogdanove, A. J. et al. Unified nomenclature for broadly conserved hrp genes of phytopathogenic bacteria. Mol. Microbiol. 20, 681-683 (1996).
    • (1996) Mol. Microbiol. , vol.20 , pp. 681-683
    • Bogdanove, A.J.1
  • 33
    • 0034730179 scopus 로고    scopus 로고
    • Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system
    • Kubori, T., Sukhan, A., Aizawa, S. I. & Galan, J. E. Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system. Proc. Natl Acad. Sci. USA 97, 10225-10230 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 10225-10230
    • Kubori, T.1    Sukhan, A.2    Aizawa, S.I.3    Galan, J.E.4
  • 34
    • 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. et al. 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).
    • (1997) Mol. Microbiol. , vol.26 , pp. 789-797
    • Koster, M.1
  • 35
    • 3042812521 scopus 로고    scopus 로고
    • Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica
    • Burghout, P. et al. Structure and electrophysiological properties of the YscC secretin from the type III secretion system of Yersinia enterocolitica J. Bacteriol. 186, 4645-4654 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 4645-4654
    • Burghout, P.1
  • 36
    • 27844581702 scopus 로고    scopus 로고
    • Structural insights into the secretin PulD and its trypsin-resistant core
    • Chami, M. et al. Structural insights into the secretin PulD and its trypsin-resistant core. J. Biol. Chem. 280, 37732-37741 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37732-37741
    • Chami, M.1
  • 37
    • 4544346057 scopus 로고    scopus 로고
    • Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution
    • Collins, R. F. et al. Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution. J. Biol. Chem. 279, 39750-39756 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 39750-39756
    • Collins, R.F.1
  • 38
    • 0027982566 scopus 로고
    • Phage assembly: A paradigm for bacterial virulence factor export?
    • Russel, M. Phage assembly: A paradigm for bacterial virulence factor export? Science 265, 612-614 (1994).
    • (1994) Science , vol.265 , pp. 612-614
    • Russel, M.1
  • 39
    • 3843152683 scopus 로고    scopus 로고
    • Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica
    • Burghout, P. et al. Role of the pilot protein YscW in the biogenesis of the YscC secretin in Yersinia enterocolitica. J. Bacteriol. 186, 5366-5375 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 5366-5375
    • Burghout, P.1
  • 40
    • 0031777144 scopus 로고    scopus 로고
    • The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG
    • Daefler, S. & Russel, M. The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG. Mol. Microbiol. 28, 1367-1380 (1998).
    • (1998) Mol. Microbiol. , vol.28 , pp. 1367-1380
    • Daefler, S.1    Russel, M.2
  • 41
    • 0031665154 scopus 로고    scopus 로고
    • Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization
    • Crago, A. M. & Koronakis, V. Salmonella InvG forms a ring-like multimer that requires the InvH lipoprotein for outer membrane localization. Mol. Microbiol. 30, 47-56 (1998).
    • (1998) Mol. Microbiol. , vol.30 , pp. 47-56
    • Crago, A.M.1    Koronakis, V.2
  • 42
    • 15944376254 scopus 로고    scopus 로고
    • Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ
    • Crepin, V. F. et al. Structural and functional studies of the enteropathogenic Escherichia coli type III needle complex protein EscJ. Mol. Microbiol. 55, 1658-1670 (2005).
    • (2005) Mol. Microbiol. , vol.55 , pp. 1658-1670
    • Crepin, V.F.1
  • 43
    • 20444488138 scopus 로고    scopus 로고
    • Structural characterization of the molecular platform for type III secretion system assembly
    • Yip, C. K. et al. Structural characterization of the molecular platform for type III secretion system assembly. Nature 435, 702-707 (2005).
    • (2005) Nature , vol.435 , pp. 702-707
    • Yip, C.K.1
  • 44
    • 0038190990 scopus 로고    scopus 로고
    • Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ
    • Sukhan, A., Kubori, T. & Galan, J. E. Synthesis and localization of the Salmonella SPI-1 type III secretion needle complex proteins PrgI and PrgJ. J. Bacteriol. 185, 3480-3483 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 3480-3483
    • Sukhan, A.1    Kubori, T.2    Galan, J.E.3
  • 45
    • 0345827609 scopus 로고    scopus 로고
    • Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems
    • Fadouloglou, V. E. et al. Structure of HrcQB-C, a conserved component of the bacterial type III secretion systems. Proc. Natl Acad. Sci. USA 101, 70-75 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 70-75
    • Fadouloglou, V.E.1
  • 46
    • 0036041918 scopus 로고    scopus 로고
    • Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway
    • Gonzalez-Pedrajo, B., Fraser, G. M., Minamino, T. & Macnab, R. M. Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway. Mol. Microbiol. 45, 967-982 (2002).
    • (2002) Mol. Microbiol. , vol.45 , pp. 967-982
    • Gonzalez-Pedrajo, B.1    Fraser, G.M.2    Minamino, T.3    Macnab, R.M.4
  • 47
    • 0034193707 scopus 로고    scopus 로고
    • Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system
    • Jackson, M. W. & Plano, G. V. Interactions between type III secretion apparatus components from Yersinia pestis detected using the yeast two-hybrid system. FEMS Microbiol. Lett. 186, 85-90 (2000).
    • (2000) FEMS Microbiol. Lett. , vol.186 , pp. 85-90
    • Jackson, M.W.1    Plano, G.V.2
  • 48
    • 33646543996 scopus 로고    scopus 로고
    • Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL
    • Blaylock, B., Riordan, K. E., Missiakas, D. M. & Schneewind, O. Characterization of the Yersinia enterocolitica type III secretion ATPase YscN and its regulator, YscL. J. Bacteriol. 188, 3525-3534 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 3525-3534
    • Blaylock, B.1    Riordan, K.E.2    Missiakas, D.M.3    Schneewind, O.4
  • 49
    • 0041663990 scopus 로고    scopus 로고
    • MxiK and MxiN interact with the Spa47 ATPase and are required for transit of the needle components MxiH and MxiI, but not of Ipa proteins, through the type III secretion apparatus of Shigella flexneri
    • Jouihri, N. et al. MxiK and MxiN interact with the Spa47 ATPase and are required for transit of the needle components MxiH and MxiI, but not of Ipa proteins, through the type III secretion apparatus of Shigella flexneri. Mol. Microbiol. 49, 755-767 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 755-767
    • Jouihri, N.1
  • 50
    • 0034011357 scopus 로고    scopus 로고
    • Interactions among components of the Salmonella flagellar export apparatus and its substrates
    • Minamino, T. & MacNab, R. M. Interactions among components of the Salmonella flagellar export apparatus and its substrates. Mol. Microbiol. 35, 1052-1064 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 1052-1064
    • Minamino, T.1    MacNab, R.M.2
  • 51
    • 0038507200 scopus 로고    scopus 로고
    • Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization
    • Pozidis, C. et al. Type III protein translocase: HrcN is a peripheral ATPase that is activated by oligomerization. J. Biol. Chem. 278, 25816-25824 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 25816-25824
    • Pozidis, C.1
  • 52
    • 33745219453 scopus 로고    scopus 로고
    • Double hexameric ring assembly of the type III protein translocase ATPase HrcN
    • Muller, S. A. et al. Double hexameric ring assembly of the type III protein translocase ATPase HrcN. Mol. Microbiol. 61, 119-125 (2006).
    • (2006) Mol. Microbiol. , vol.61 , pp. 119-125
    • Muller, S.A.1
  • 53
    • 0038460046 scopus 로고    scopus 로고
    • Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly
    • Claret, L., Calder, S. R., Higgins, M. & Hughes, C. Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. Mol. Microbiol. 48, 1349-1355 (2003).
    • (2003) Mol. Microbiol. , vol.48 , pp. 1349-1355
    • Claret, L.1    Calder, S.R.2    Higgins, M.3    Hughes, C.4
  • 54
    • 27144559247 scopus 로고    scopus 로고
    • Chaperone release and unfolding of substrates in type III secretion
    • Akeda, Y. & Galan, J. E. Chaperone release and unfolding of substrates in type III secretion. Nature 437, 911-915 (2005).
    • (2005) Nature , vol.437 , pp. 911-915
    • Akeda, Y.1    Galan, J.E.2
  • 55
    • 0035836714 scopus 로고    scopus 로고
    • Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells
    • Hoiczyk, E. & Blobel, G. Polymerization of a single protein of the pathogen Yersinia enterocolitica into needles punctures eukaryotic cells. Proc. Natl Acad. Sci. USA 98, 4669-4674 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 4669-4674
    • Hoiczyk, E.1    Blobel, G.2
  • 56
    • 0038608020 scopus 로고    scopus 로고
    • Helical structure of the needle of the type III secretion system of Shigella flexneri
    • Cordes, F. S. et al. Helical structure of the needle of the type III secretion system of Shigella flexneri. J Biol Chem 278, 17103-7 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 17103-17107
    • Cordes, F.S.1
  • 57
    • 33747613328 scopus 로고    scopus 로고
    • Molecular model of a type III secretion system needle: Implications for host-cell sensing
    • Deane, J. E. et al. Molecular model of a type III secretion system needle: Implications for host-cell sensing. Proc. Natl Acad. Sci. USA (2006).
    • (2006) Proc. Natl Acad. Sci. USA
    • Deane, J.E.1
  • 58
    • 0042238051 scopus 로고    scopus 로고
    • Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy
    • Yonekura, K., Maki-Yonekura, S. & Namba, K. Complete atomic model of the bacterial flagellar filament by electron cryomicroscopy. Nature 424, 643-650 (2003).
    • (2003) Nature , vol.424 , pp. 643-650
    • Yonekura, K.1    Maki-Yonekura, S.2    Namba, K.3
  • 59
    • 27344457144 scopus 로고    scopus 로고
    • The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles
    • Mueller, C. A. et al. The V-antigen of Yersinia forms a distinct structure at the tip of injectisome needles. Science 310, 674-676 (2005).
    • (2005) Science , vol.310 , pp. 674-676
    • Mueller, C.A.1
  • 60
    • 1242328668 scopus 로고    scopus 로고
    • The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague
    • Derewenda, U. et al. The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague. Structure (Camb) 12, 301-306 (2004).
    • (2004) Structure (Camb) , vol.12 , pp. 301-306
    • Derewenda, U.1
  • 61
    • 0035930715 scopus 로고    scopus 로고
    • Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae
    • Jin, Q. & He, S. Y. Role of the Hrp pilus in type III protein secretion in Pseudomonas syringae. Science 294, 2556-2558 (2001).
    • (2001) Science , vol.294 , pp. 2556-2558
    • Jin, Q.1    He, S.Y.2
  • 62
    • 0029930059 scopus 로고    scopus 로고
    • The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane
    • Hakansson, S., Galyov, E. E., Rosqvist, R. & Wolf-Watz, H. The Yersinia YpkA Ser/Thr kinase is translocated and subsequently targeted to the inner surface of the HeLa cell plasma membrane. Mol. Microbiol. 20, 593-603. (1996).
    • (1996) Mol. Microbiol. , vol.20 , pp. 593-603
    • Hakansson, S.1    Galyov, E.E.2    Rosqvist, R.3    Wolf-Watz, H.4
  • 63
    • 0032835828 scopus 로고    scopus 로고
    • Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: Requirement for translocators YopB and YopD, but not LcrG
    • Neyt, C. & Cornelis, G. R. Insertion of a Yop translocation pore into the macrophage plasma membrane by Yersinia enterocolitica: Requirement for translocators YopB and YopD, but not LcrG. Mol. Microbiol. 33, 971-981 (1999).
    • (1999) Mol. Microbiol. , vol.33 , pp. 971-981
    • Neyt, C.1    Cornelis, G.R.2
  • 64
    • 0027982852 scopus 로고
    • Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells
    • Rosqvist, R., Magnusson, K. E. & Wolf-Watz, H. Target cell contact triggers expression and polarized transfer of Yersinia YopE cytotoxin into mammalian cells. EMBO J. 13, 964-972 (1994).
    • (1994) EMBO J. , vol.13 , pp. 964-972
    • Rosqvist, R.1    Magnusson, K.E.2    Wolf-Watz, H.3
  • 65
    • 0028105015 scopus 로고
    • Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells
    • Sory, M. P. & Cornelis, G. R. Translocation of a hybrid YopE-adenylate cyclase from Yersinia enterocolitica into HeLa cells. Mol. Microbiol. 14, 583-594 (1994).
    • (1994) Mol. Microbiol. , vol.14 , pp. 583-594
    • Sory, M.P.1    Cornelis, G.R.2
  • 66
    • 0033027311 scopus 로고    scopus 로고
    • The V-antigen of Yersinia is surface exposed before target cell contact and involved in virulence protein translocation
    • Pettersson, J. et al. The V-antigen of Yersinia is surface exposed before target cell contact and involved in virulence protein translocation. Mol. Microbiol. 32, 961-976 (1999).
    • (1999) Mol. Microbiol. , vol.32 , pp. 961-976
    • Pettersson, J.1
  • 67
    • 0029814613 scopus 로고    scopus 로고
    • Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1. 8 macrophages by the YopB, D, N delivery apparatus
    • Boland, A. et al. Status of YopM and YopN in the Yersinia Yop virulon: YopM of Y. enterocolitica is internalized inside the cytosol of PU5-1. 8 macrophages by the YopB, D, N delivery apparatus. EMBO J. 15, 5191-5201 (1996).
    • (1996) EMBO J. , vol.15 , pp. 5191-5201
    • Boland, A.1
  • 68
    • 0031885218 scopus 로고    scopus 로고
    • The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD
    • Sarker, M. R., Neyt, C., Stainier, I. & Cornelis, G. R. The Yersinia Yop virulon: LcrV is required for extrusion of the translocators YopB and YopD. J. Bacteriol. 180, 1207-1214 (1998).
    • (1998) J. Bacteriol. , vol.180 , pp. 1207-1214
    • Sarker, M.R.1    Neyt, C.2    Stainier, I.3    Cornelis, G.R.4
  • 69
    • 0028113512 scopus 로고
    • Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri
    • Menard, R., Sansonetti, P., Parsot, C. & Vasselon, T. Extracellular association and cytoplasmic partitioning of the IpaB and IpaC invasins of S. flexneri. Cell 79, 515-525 (1994).
    • (1994) Cell , vol.79 , pp. 515-525
    • Menard, R.1    Sansonetti, P.2    Parsot, C.3    Vasselon, T.4
  • 70
    • 30744451417 scopus 로고    scopus 로고
    • Characterization of the interaction of single tryptophan containing mutants of IpaC from Shigella flexneri with phospholipid membranes
    • Harrington, A. et al. Characterization of the interaction of single tryptophan containing mutants of IpaC from Shigella flexneri with phospholipid membranes. Biochemistry 45, 626-636 (2006).
    • (2006) Biochemistry , vol.45 , pp. 626-636
    • Harrington, A.1
  • 71
    • 0038501071 scopus 로고    scopus 로고
    • The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology
    • Hume, P. J., McGhie, E. J., Hayward, R. D. & Koronakis, V. The purified Shigella IpaB and Salmonella SipB translocators share biochemical properties and membrane topology. Mol. Microbiol. 49, 425-439 (2003).
    • (2003) Mol. Microbiol. , vol.49 , pp. 425-439
    • Hume, P.J.1    McGhie, E.J.2    Hayward, R.D.3    Koronakis, V.4
  • 72
    • 0141642035 scopus 로고    scopus 로고
    • Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas
    • Schoehn, G. et al. Oligomerization of type III secretion proteins PopB and PopD precedes pore formation in Pseudomonas. EMBO J. 22, 4957-4967 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4957-4967
    • Schoehn, G.1
  • 73
    • 33745615443 scopus 로고    scopus 로고
    • Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa
    • Faudry, E., Vernier, G., Neumann, E., Forge, V. & Attree, I. Synergistic pore formation by type III toxin translocators of Pseudomonas aeruginosa. Biochemistry 45, 8117-8123 (2006).
    • (2006) Biochemistry , vol.45 , pp. 8117-8123
    • Faudry, E.1    Vernier, G.2    Neumann, E.3    Forge, V.4    Attree, I.5
  • 74
    • 0032833608 scopus 로고    scopus 로고
    • Virulence role of V antigen of Yersinia pestis at the bacterial surface
    • Fields, K. A., Nilles, M. L., Cowan, C. & Straley, S. C. Virulence role of V antigen of Yersinia pestis at the bacterial surface. Infect. Immun. 67, 5395-5408 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 5395-5408
    • Fields, K.A.1    Nilles, M.L.2    Cowan, C.3    Straley, S.C.4
  • 75
    • 0242321266 scopus 로고    scopus 로고
    • Genetic analysis of the formation of the Ysc-Yop translocation pore in macrophages by Yersinia enterocolitica: Role of LcrV, yscF and YopN
    • Marenne, M. N., Journet, L., Mota, L. J. & Cornelis, G. R. Genetic analysis of the formation of the Ysc-Yop translocation pore in macrophages by Yersinia enterocolitica: Role of LcrV, yscF and YopN. Microb. Pathogen. 35, 243-258 (2003).
    • (2003) Microb. Pathogen. , vol.35 , pp. 243-258
    • Marenne, M.N.1    Journet, L.2    Mota, L.J.3    Cornelis, G.R.4
  • 76
    • 0029908022 scopus 로고    scopus 로고
    • The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-dependent membrane disrupting activity
    • Hakansson, S. et al. The YopB protein of Yersinia pseudotuberculosis is essential for the translocation of Yop effector proteins across the target cell plasma membrane and displays a contact-dependent membrane disrupting activity. EMBO J. 15, 5812-5823. (1996).
    • (1996) EMBO J. , vol.15 , pp. 5812-5823
    • Hakansson, S.1
  • 77
    • 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. et al. 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).
    • (2004) Infect. Immun. , vol.72 , pp. 4741-4750
    • Goure, J.1
  • 78
    • 22244476683 scopus 로고    scopus 로고
    • Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes
    • Goure, J., Broz, P., Attree, O., Cornelis, G. R. & Attree, I. Protective anti-V antibodies inhibit Pseudomonas and Yersinia translocon assembly within host membranes. J. Infect. Dis. 192, 218-225 (2005).
    • (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
  • 79
    • 15544376398 scopus 로고    scopus 로고
    • IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes
    • Picking, W. L. et al. IpaD of Shigella flexneri is independently required for regulation of Ipa protein secretion and efficient insertion of IpaB and IpaC into host membranes. Infect. Immun. 73, 1432-1440 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 1432-1440
    • Picking, W.L.1
  • 80
    • 33746636397 scopus 로고    scopus 로고
    • IpaD localizes to the tip of the type III secretion system needle of Shigella flexneri
    • Espina, M. et al. IpaD localizes to the tip of the type III secretion system needle of Shigella flexneri. Infect. Immun. 74, 4391-4400 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 4391-4400
    • Espina, M.1
  • 81
    • 0032868135 scopus 로고    scopus 로고
    • Type III secretion-dependent hemolytic activity of enteropathogenic Escherichia coli
    • Warawa, J., Finlay, B. B. & Kenny, B. Type III secretion-dependent hemolytic activity of enteropathogenic Escherichia coli. Infect. Immun. 67, 5538-5540 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 5538-5540
    • Warawa, J.1    Finlay, B.B.2    Kenny, B.3
  • 82
    • 0034671834 scopus 로고    scopus 로고
    • The bacterial flagellar cap as the rotary promoter of flagellin self-assembly
    • Yonekura, K. et al. The bacterial flagellar cap as the rotary promoter of flagellin self-assembly. Science 290, 2148-2152 (2000).
    • (2000) Science , vol.290 , pp. 2148-2152
    • Yonekura, K.1
  • 83
    • 0037090775 scopus 로고    scopus 로고
    • The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ
    • Li, C. M. et al. The Hrp pilus of Pseudomonas syringae elongates from its tip and acts as a conduit for translocation of the effector protein HrpZ. EMBO J. 21, 1909-1915 (2002).
    • (2002) EMBO J. , vol.21 , pp. 1909-1915
    • Li, C.M.1
  • 84
    • 16844376367 scopus 로고    scopus 로고
    • Polarity of enteropathogenic Escherichia coli EspA filament assembly and protein secretion
    • Crepin, V. F., Shaw, R., Abe, C. M., Knutton, S. & Frankel, G. Polarity of enteropathogenic Escherichia coli EspA filament assembly and protein secretion. J. Bacteriol. 187, 2881-2889 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 2881-2889
    • Crepin, V.F.1    Shaw, R.2    Abe, C.M.3    Knutton, S.4    Frankel, G.5
  • 85
    • 33745279057 scopus 로고    scopus 로고
    • Assembly of the inner rod determines needle length in the type III secretion injectisome
    • Marlovits, T. C. et al. Assembly of the inner rod determines needle length in the type III secretion injectisome. Nature 441, 637-640 (2006).
    • (2006) Nature , vol.441 , pp. 637-640
    • Marlovits, T.C.1
  • 86
    • 0022429540 scopus 로고
    • 'Cap' on the tip of Salmonella flagella
    • Ikeda, T., Asakura, S. & Kamiya, R. 'Cap' on the tip of Salmonella flagella. J. Mol. Biol. 184, 735-737 (1985).
    • (1985) J. Mol. Biol. , vol.184 , pp. 735-737
    • Ikeda, T.1    Asakura, S.2    Kamiya, R.3
  • 87
    • 27744509836 scopus 로고    scopus 로고
    • The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa
    • Quinaud, M. et al. The PscE-PscF-PscG complex controls type III secretion needle biogenesis in Pseudomonas aeruginosa. J. Biol. Chem. 280, 36293-36300 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 36293-36300
    • Quinaud, M.1
  • 88
    • 0345600239 scopus 로고    scopus 로고
    • The needle length of bacterial injectisomes is determined by a molecular ruler
    • Journet, L., Agrain, C., Broz, P. & Cornelis, G. R. The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302, 1757-1760 (2003).
    • (2003) Science , vol.302 , pp. 1757-1760
    • Journet, L.1    Agrain, C.2    Broz, P.3    Cornelis, G.R.4
  • 89
    • 0029989240 scopus 로고    scopus 로고
    • Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium
    • Williams, A. W. et al. Mutations in fliK and flhB affecting flagellar hook and filament assembly in Salmonella typhimurium. J. Bacteriol. 178, 2960-2970 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 2960-2970
    • Williams, A.W.1
  • 90
    • 0036282334 scopus 로고    scopus 로고
    • Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins
    • Magdalena, J. et al. Spa32 regulates a switch in substrate specificity of the type III secreton of Shigella flexneri from needle components to Ipa proteins. J. Bacteriol. 184, 3433-3441 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 3433-3441
    • Magdalena, J.1
  • 91
    • 0035937441 scopus 로고    scopus 로고
    • Length of the flagellar hook and the capacity of the type III export apparatus
    • Makishima, S., Komoriya, K., Yamaguchi, S. & Aizawa, S. I. Length of the flagellar hook and the capacity of the type III export apparatus. Science 291, 2411-2413 (2001).
    • (2001) Science , vol.291 , pp. 2411-2413
    • Makishima, S.1    Komoriya, K.2    Yamaguchi, S.3    Aizawa, S.I.4
  • 92
    • 16244407371 scopus 로고    scopus 로고
    • Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica
    • Agrain, C. et al. Characterization of a type III secretion substrate specificity switch (T3S4) domain in YscP from Yersinia enterocolitica. Mol. Microbiol. 56, 54-67 (2005).
    • (2005) Mol. Microbiol. , vol.56 , pp. 54-67
    • Agrain, C.1
  • 93
    • 23844543359 scopus 로고    scopus 로고
    • Secretion of YscP from Yersinia enterocolitica is essential to control the length of the injectisome needle but not to change the type III secretion substrate specificity
    • Agrain, C., Sorg, I., Paroz, C. & Cornelis, G. R. Secretion of YscP from Yersinia enterocolitica is essential to control the length of the injectisome needle but not to change the type III secretion substrate specificity. Mol. Microbiol. 57, 1415-1427 (2005).
    • (2005) Mol. Microbiol. , vol.57 , pp. 1415-1427
    • Agrain, C.1    Sorg, I.2    Paroz, C.3    Cornelis, G.R.4
  • 95
    • 0028027526 scopus 로고
    • Isolation and characterization of FliK-independent flagellation mutants from Salmonella typhimurium
    • Kutsukake, K., Minamino, T. & Yokoseki, T. Isolation and characterization of FliK-independent flagellation mutants from Salmonella typhimurium. J. Bacteriol. 176, 7625-7629 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 7625-7629
    • Kutsukake, K.1    Minamino, T.2    Yokoseki, T.3
  • 96
    • 0028093390 scopus 로고
    • Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium
    • Hirano, T., Yamaguchi, S., Oosawa, K. & Aizawa, S. Roles of FliK and FlhB in determination of flagellar hook length in Salmonella typhimurium. J. Bacteriol. 176, 5439-5449 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 5439-5449
    • Hirano, T.1    Yamaguchi, S.2    Oosawa, K.3    Aizawa, S.4
  • 97
    • 0037379368 scopus 로고    scopus 로고
    • YscP and YscU regulate substrate specificity of the Yersinia type III secretion system
    • Edqvist, P. J. et al. YscP and YscU regulate substrate specificity of the Yersinia type III secretion system. J. Bacteriol. 185, 2259-2266 (2003).
    • (2003) J. Bacteriol. , vol.185 , pp. 2259-2266
    • Edqvist, P.J.1
  • 98
    • 3343019337 scopus 로고    scopus 로고
    • Domain organization and function of Salmonella FliK, a flagellar hook-length control protein
    • Minamino, T. et al. Domain organization and function of Salmonella FliK, a flagellar hook-length control protein. J. Mol. Biol. 341, 491-502 (2004).
    • (2004) J. Mol. Biol. , vol.341 , pp. 491-502
    • Minamino, T.1
  • 99
    • 0033900964 scopus 로고    scopus 로고
    • Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching
    • Minamino, T. & Macnab, R. M. Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching. J. Bacteriol. 182, 4906-4914 (2000)
    • (2000) J. Bacteriol. , vol.182 , pp. 4906-4914
    • Minamino, T.1    Macnab, R.M.2
  • 100
    • 33646202330 scopus 로고    scopus 로고
    • The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock
    • Moriya, N., Minamino, T., Hughes, K. T., Macnab, R. M. & Namba, K. The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock. J. Mol. Biol. 359, 466-477 (2006).
    • (2006) J. Mol. Biol. , vol.359 , pp. 466-477
    • Moriya, N.1    Minamino, T.2    Hughes, K.T.3    Macnab, R.M.4    Namba, K.5
  • 101
    • 0036178888 scopus 로고    scopus 로고
    • Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length
    • Tamano, K., Katayama, E., Toyotome, T. & Sasakawa, C. Shigella Spa32 is an essential secretory protein for functional type III secretion machinery and uniformity of its needle length. J. Bacteriol. 184, 1244-1252 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 1244-1252
    • Tamano, K.1    Katayama, E.2    Toyotome, T.3    Sasakawa, C.4
  • 102
    • 21244474421 scopus 로고    scopus 로고
    • Formation of a novel surface structure encoded by Salmonella pathogenicity island 2
    • Chakravortty, D., Rohde, M., Jager, L., Deiwick, J. & Hensel, M. Formation of a novel surface structure encoded by Salmonella pathogenicity island 2. EMBO J. 24, 2043-2052 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2043-2052
    • Chakravortty, D.1    Rohde, M.2    Jager, L.3    Deiwick, J.4    Hensel, M.5
  • 104
    • 20044379025 scopus 로고    scopus 로고
    • Optimization of virulence functions through glucosylation of Shigella LPS
    • West, N. P. et al. Optimization of virulence functions through glucosylation of Shigella LPS. Science 307, 1313-1317 (2005).
    • (2005) Science , vol.307 , pp. 1313-1317
    • West, N.P.1
  • 105
    • 0029787714 scopus 로고    scopus 로고
    • Modulation of virulence factor expression by pathogen target cell contact
    • Pettersson, J. et al. Modulation of virulence factor expression by pathogen target cell contact. Science 273, 1231-1233 (1996).
    • (1996) Science , vol.273 , pp. 1231-1233
    • Pettersson, J.1
  • 106
    • 0025762461 scopus 로고
    • The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis
    • Forsberg, A., Viitanen, A. M., Skurnik, M. & Wolf-Watz, H. The surface-located YopN protein is involved in calcium signal transduction in Yersinia pseudotuberculosis. Mol. Microbiol. 5, 977-986 (1991).
    • (1991) Mol. Microbiol. , vol.5 , pp. 977-986
    • Forsberg, A.1    Viitanen, A.M.2    Skurnik, M.3    Wolf-Watz, H.4
  • 107
    • 0031766236 scopus 로고    scopus 로고
    • A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis
    • Day, J. B. & Plano, G. V. A complex composed of SycN and YscB functions as a specific chaperone for YopN in Yersinia pestis. Mol. Microbiol. 30, 777-788 (1998).
    • (1998) Mol. Microbiol. , vol.30 , pp. 777-788
    • Day, J.B.1    Plano, G.V.2
  • 108
    • 0031880899 scopus 로고    scopus 로고
    • YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells
    • Iriarte, M. & Cornelis, G. R. YopT, a new Yersinia Yop effector protein, affects the cytoskeleton of host cells. Mol. Microbiol. 29, 915-929 (1998).
    • (1998) Mol. Microbiol. , vol.29 , pp. 915-929
    • Iriarte, M.1    Cornelis, G.R.2
  • 109
    • 0027229148 scopus 로고
    • LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis
    • Skryzpek, E. & Straley, S. C. LcrG, a secreted protein involved in negative regulation of the low-calcium response in Yersinia pestis. J. Bacteriol. 175, 3520-3528 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 3520-3528
    • Skryzpek, E.1    Straley, S.C.2
  • 110
    • 13444303937 scopus 로고    scopus 로고
    • Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis
    • Schubot, F. D. et al. Three-dimensional structure of a macromolecular assembly that regulates type III secretion in Yersinia pestis. J. Mol. Biol. 346, 1147-1161 (2005).
    • (2005) J. Mol. Biol. , vol.346 , pp. 1147-1161
    • Schubot, F.D.1
  • 112
    • 9144254025 scopus 로고    scopus 로고
    • Rafts can trigger contact-mediated secretion of bacterial effectors via a lipid-based mechanism
    • van der Goot, F. G., Tran van Nhieu, G., Allaoui, A., Sansonetti, P. & Lafont, F. Rafts can trigger contact-mediated secretion of bacterial effectors via a lipid-based mechanism. J. Biol. Chem. 279, 47792-47798 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 47792-47798
    • van der Goot, F.G.1    Tran van Nhieu, G.2    Allaoui, A.3    Sansonetti, P.4    Lafont, F.5
  • 113
    • 17644366419 scopus 로고    scopus 로고
    • Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells
    • Hayward, R. D. et al. Cholesterol binding by the bacterial type III translocon is essential for virulence effector delivery into mammalian cells. Mol. Microbiol. 56, 590-603 (2005).
    • (2005) Mol. Microbiol. , vol.56 , pp. 590-603
    • Hayward, R.D.1
  • 114
    • 30044445766 scopus 로고    scopus 로고
    • The needle component of the type III secreton of Shigella regulates the activity of the secretion apparatus
    • Kenjale, R. et al. The needle component of the type III secreton of Shigella regulates the activity of the secretion apparatus. J. Biol. Chem. 280, 42929-42937 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 42929-42937
    • Kenjale, R.1
  • 115
    • 0029948607 scopus 로고    scopus 로고
    • YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis
    • Andersson, K. et al. YopH of Yersinia pseudotuberculosis interrupts early phosphotyrosine signalling associated with phagocytosis. Mol. Microbiol. 20, 1057-10569 (1996).
    • (1996) Mol. Microbiol. , vol.20 , pp. 1057-10569
    • Andersson, K.1
  • 116
    • 24644474725 scopus 로고    scopus 로고
    • Real-time imaging of type III secretion: Salmonella SipA injection into host cells
    • Schlumberger, M. C. et al. Real-time imaging of type III secretion: Salmonella SipA injection into host cells. Proc. Natl Acad. Sci. USA 102, 12548-12553 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 12548-12553
    • Schlumberger, M.C.1
  • 118
    • 33645854351 scopus 로고    scopus 로고
    • Length control of extended protein structures in bacteria and bacteriophages
    • Cornelis, G. R., Agrain, C. & Sorg, I. Length control of extended protein structures in bacteria and bacteriophages. Curr. Opin. Microbiol. 9, 201-206 (2006).
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 201-206
    • Cornelis, G.R.1    Agrain, C.2    Sorg, I.3
  • 119
    • 0141618445 scopus 로고    scopus 로고
    • Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion
    • Evdokimov, A. G. et al. Similar modes of polypeptide recognition by export chaperones in flagellar biosynthesis and type III secretion. Nature Struct. Biol. 10, 789-793 (2003).
    • (2003) Nature Struct. Biol. , vol.10 , pp. 789-793
    • Evdokimov, A.G.1
  • 120
    • 0034753703 scopus 로고    scopus 로고
    • Structure of the Yersinia type III secretory system chaperone SycE
    • Birtalan, S. & Ghosh, P. Structure of the Yersinia type III secretory system chaperone SycE. Nature Struct. Biol. 8, 974-978 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 974-978
    • Birtalan, S.1    Ghosh, P.2
  • 121
    • 0036283512 scopus 로고    scopus 로고
    • Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens
    • Birtalan, S. C., Phillips, R. M. & Ghosh, P. Three-dimensional secretion signals in chaperone-effector complexes of bacterial pathogens. Mol. Cell. 9, 971-980 (2002).
    • (2002) Mol. Cell. , vol.9 , pp. 971-980
    • Birtalan, S.C.1    Phillips, R.M.2    Ghosh, P.3
  • 122
    • 0035499438 scopus 로고    scopus 로고
    • Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion
    • Stebbins, C. E. & Galan, J. E. Maintenance of an unfolded polypeptide by a cognate chaperone in bacterial type III secretion. Nature 414, 77-81 (2001).
    • (2001) Nature , vol.414 , pp. 77-81
    • Stebbins, C.E.1    Galan, J.E.2
  • 123
    • 0032906245 scopus 로고    scopus 로고
    • Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly
    • Fraser, G. M., Bennett, J. C. & Hughes, C. Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly. Mol. Microbiol. 32, 569-580 (1999).
    • (1999) Mol. Microbiol. , vol.32 , pp. 569-580
    • Fraser, G.M.1    Bennett, J.C.2    Hughes, C.3
  • 124
    • 0035957518 scopus 로고    scopus 로고
    • Flagellin polymerisation control by a cytosolic export chaperone
    • Auvray, F., Thomas, J., Fraser, G. M. & Hughes, C. Flagellin polymerisation control by a cytosolic export chaperone. J. Mol. Biol. 308, 221-229 (2001).
    • (2001) J. Mol. Biol. , vol.308 , pp. 221-229
    • Auvray, F.1    Thomas, J.2    Fraser, G.M.3    Hughes, C.4
  • 125
    • 0034194180 scopus 로고    scopus 로고
    • From flagellum assembly to virulence: The extended family of type III export chaperones
    • Bennett, J. C. & Hughes, C. From flagellum assembly to virulence: The extended family of type III export chaperones. Trends Microbiol. 8, 202-204 (2000).
    • (2000) Trends Microbiol. , vol.8 , pp. 202-204
    • Bennett, J.C.1    Hughes, C.2
  • 126
    • 0032947515 scopus 로고    scopus 로고
    • Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD
    • Neyt, C. & Cornelis, G. R. Role of SycD, the chaperone of the Yersinia Yop translocators YopB and YopD. Mol. Microbiol. 31, 143-156 (1999).
    • (1999) Mol. Microbiol. , vol.31 , pp. 143-156
    • Neyt, C.1    Cornelis, G.R.2
  • 128
    • 0035901560 scopus 로고    scopus 로고
    • Type III secretion chaperone-dependent regulation: Activation of virulence genes by SicA and InvF in Salmonella typhimurium
    • Darwin, K. H. & Miller, V. L. Type III secretion chaperone-dependent regulation: Activation of virulence genes by SicA and InvF in Salmonella typhimurium. EMBO J. 20, 1850-1862 (2001).
    • (2001) EMBO J. , vol.20 , pp. 1850-1862
    • Darwin, K.H.1    Miller, V.L.2
  • 129
    • 0036032109 scopus 로고    scopus 로고
    • Chaperones of the type III secretion pathway: Jacks of all trades
    • Page, A. L. & Parsot, C. Chaperones of the type III secretion pathway: jacks of all trades. Mol. Microbiol. 46, 1-11 (2002).
    • (2002) Mol. Microbiol. , vol.46 , pp. 1-11
    • Page, A.L.1    Parsot, C.2
  • 130
    • 0037469577 scopus 로고    scopus 로고
    • The multitalented type III chaperones: All you can do with 15 kDa
    • Feldman, M. F. & Cornelis, G. R. The multitalented type III chaperones: all you can do with 15 kDa. FEMS Microbiol. Lett. 219, 151-158 (2003).
    • (2003) FEMS Microbiol. Lett. , vol.219 , pp. 151-158
    • Feldman, M.F.1    Cornelis, G.R.2
  • 131
    • 10344249890 scopus 로고    scopus 로고
    • Process of protein transport by the type III secretion system
    • Ghosh, P. Process of protein transport by the type III secretion system. Microbiol. Mol. Biol. Rev. 68, 771-795 (2004).
    • (2004) Microbiol. Mol. Biol. Rev. , vol.68 , pp. 771-795
    • Ghosh, P.1
  • 132
    • 0345633461 scopus 로고    scopus 로고
    • The various and varying roles of specific chaperones in type III secretion systems
    • Parsot, C., Hamiaux, C. & Page, A. L. The various and varying roles of specific chaperones in type III secretion systems. Curr. Opin. Microbiol. 6, 7-14 (2003).
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 7-14
    • Parsot, C.1    Hamiaux, C.2    Page, A.L.3
  • 133
    • 0027499076 scopus 로고
    • SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE
    • Wattiau, P. & Cornelis, G. R. SycE, a chaperone-like protein of Yersinia enterocolitica involved in the secretion of YopE. Mol. Microbiol. 8, 123-131 (1993).
    • (1993) Mol. Microbiol. , vol.8 , pp. 123-131
    • Wattiau, P.1    Cornelis, G.R.2
  • 134
    • 0035180725 scopus 로고    scopus 로고
    • Structural and biochemical characterization of the type III secretion chaperones CesT and SigE
    • Luo, Y. et al. Structural and biochemical characterization of the type III secretion chaperones CesT and SigE. Nature Struct. Biol. 8, 1031-1036 (2001).
    • (2001) Nature Struct. Biol. , vol.8 , pp. 1031-1036
    • Luo, Y.1
  • 136
    • 24744442137 scopus 로고    scopus 로고
    • Crystal Structure of the Yersinia enterocolitica type III secretion chaperone SycT
    • Locher, M. et al. Crystal Structure of the Yersinia enterocolitica type III secretion chaperone SycT. J. Biol. Chem. 280, 31149-31155 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 31149-31155
    • Locher, M.1
  • 137
    • 0037321471 scopus 로고    scopus 로고
    • Structure of the Yersinia enterocolitica molecular-chaperone protein SycE
    • Trame, C. B. & McKay, D. B. Structure of the Yersinia enterocolitica molecular-chaperone protein SycE. Acta Crystallogr. D Biol. Crystallogr. 59, 389-392 (2003).
    • (2003) Acta Crystallogr. D Biol. Crystallogr. , vol.59 , pp. 389-392
    • Trame, C.B.1    McKay, D.B.2
  • 138
    • 13444295356 scopus 로고    scopus 로고
    • Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2
    • Phan, J., Tropea, J. E. & Waugh, D. S. Structure of the Yersinia pestis type III secretion chaperone SycH in complex with a stable fragment of YscM2. Acta Crystallogr. D Biol. Crystallogr. 60, 1591-1599 (2004).
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1591-1599
    • Phan, J.1    Tropea, J.E.2    Waugh, D.S.3
  • 139
    • 2942543052 scopus 로고    scopus 로고
    • Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity
    • van Eerde, A., Hamiaux, C., Perez, J., Parsot, C. & Dijkstra, B. W. Structure of Spa15, a type III secretion chaperone from Shigella flexneri with broad specificity. EMBO Rep. 5, 477-483 (2004).
    • (2004) EMBO Rep. , vol.5 , pp. 477-483
    • van Eerde, A.1    Hamiaux, C.2    Perez, J.3    Parsot, C.4    Dijkstra, B.W.5
  • 140
    • 23644461387 scopus 로고    scopus 로고
    • Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT
    • Buttner, C. R., Cornelis, G. R., Heinz, D. W. & Niemann, H. H. Crystal structure of Yersinia enterocolitica type III secretion chaperone SycT. Protein Sci. 14, 1993-2002 (2005).
    • (2005) Protein Sci. , vol.14 , pp. 1993-2002
    • Buttner, C.R.1    Cornelis, G.R.2    Heinz, D.W.3    Niemann, H.H.4
  • 141
    • 0033872740 scopus 로고    scopus 로고
    • Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE
    • Boyd, A. P., Lambermont, I. & Cornelis, G. R. Competition between the Yops of Yersinia enterocolitica for delivery into eukaryotic cells: Role of the SycE chaperone binding domain of YopE. J. Bacteriol. 182, 4811-4821 (2000).
    • (2000) J. Bacteriol. , vol.182 , pp. 4811-4821
    • Boyd, A.P.1    Lambermont, I.2    Cornelis, G.R.3
  • 142
    • 0036267949 scopus 로고    scopus 로고
    • Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway
    • Page, A. L., Sansonetti, P. & Parsot, C. Spa15 of Shigella flexneri, a third type of chaperone in the type III secretion pathway. Mol. Microbiol. 43, 1533-1542 (2002).
    • (2002) Mol. Microbiol. , vol.43 , pp. 1533-1542
    • Page, A.L.1    Sansonetti, P.2    Parsot, C.3
  • 143
    • 33746275230 scopus 로고    scopus 로고
    • The discovery of SycO highlights a new function for type III secretion effector chaperones
    • Letzelter, M. et al. The discovery of SycO highlights a new function for type III secretion effector chaperones. EMBO J.25, 3223-3233 (2006).
    • (2006) EMBO J. , vol.25 , pp. 3223-3233
    • Letzelter, M.1
  • 144
    • 4644290877 scopus 로고    scopus 로고
    • Novel protein-protein interactions of the Yersinia pestis type III secretion system elucidated with a matrix analysis by surface plasmon resonance and mass spectrometry
    • Swietnicki, W. et al. Novel protein-protein interactions of the Yersinia pestis type III secretion system elucidated with a matrix analysis by surface plasmon resonance and mass spectrometry. J. Biol. Chem. 279, 38693-38700 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 38693-38700
    • Swietnicki, W.1
  • 145
    • 1642535429 scopus 로고    scopus 로고
    • Intracellular membrane localization of pseudomonas ExoS and Yersinia YopE in mammalian cells
    • Krall, R., Zhang, Y. & Barbieri, J. T. Intracellular membrane localization of pseudomonas ExoS and Yersinia YopE in mammalian cells. J. Biol. Chem. 279, 2747-2753 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 2747-2753
    • Krall, R.1    Zhang, Y.2    Barbieri, J.T.3
  • 146
    • 1142298562 scopus 로고    scopus 로고
    • InvB is required for type III-dependent secretion of SopA in Salmonella enterica serovar Typhimurium
    • Ehrbar, K., Hapfelmeier, S., Stecher, B. & Hardt, W. D. InvB is required for type III-dependent secretion of SopA in Salmonella enterica serovar Typhimurium. J. Bacteriol. 186, 1215-1219 (2004).
    • (2004) J. Bacteriol. , vol.186 , pp. 1215-1219
    • Ehrbar, K.1    Hapfelmeier, S.2    Stecher, B.3    Hardt, W.D.4
  • 147
    • 0037219492 scopus 로고    scopus 로고
    • CesT is a bivalent enteropathogenic Escherichia coli chaperone required for translocation of both Tir and Map
    • Creasey, E. A. et al. CesT is a bivalent enteropathogenic Escherichia coli chaperone required for translocation of both Tir and Map. Mol. Microbiol. 47, 209-221 (2003).
    • (2003) Mol. Microbiol. , vol.47 , pp. 209-221
    • Creasey, E.A.1
  • 148
    • 0942279512 scopus 로고    scopus 로고
    • Salmonella type III secretion-associated chaperones confer secretion-pathway specificity
    • Lee, S. H. & Galan, J. E. Salmonella type III secretion-associated chaperones confer secretion-pathway specificity. Mol. Microbiol. 51, 483-495 (2004).
    • (2004) Mol. Microbiol. , vol.51 , pp. 483-495
    • Lee, S.H.1    Galan, J.E.2
  • 149
    • 0036170459 scopus 로고    scopus 로고
    • LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion
    • Wulff-Strobel, C. R., Williams, A. W. & Straley, S. C. LcrQ and SycH function together at the Ysc type III secretion system in Yersinia pestis to impose a hierarchy of secretion. Mol. Microbiol. 43, 411-423 (2002).
    • (2002) Mol. Microbiol. , vol.43 , pp. 411-423
    • Wulff-Strobel, C.R.1    Williams, A.W.2    Straley, S.C.3
  • 150
    • 20344407810 scopus 로고    scopus 로고
    • A secreted anti-activator, OspD1, and its chaperone, Spa15, are involved in the control of transcription by the type III secretion apparatus activity in Shigella flexneri
    • Parsot, C. et al. A secreted anti-activator, OspD1, and its chaperone, Spa15, are involved in the control of transcription by the type III secretion apparatus activity in Shigella flexneri. Mol. Microbiol. 56, 1627-1635 (2005).
    • (2005) Mol. Microbiol. , vol.56 , pp. 1627-1635
    • Parsot, C.1
  • 152
    • 11444263137 scopus 로고    scopus 로고
    • Structural characterization of a type III secretion system filament protein in complex with its chaperone
    • Yip, C.K., Finlay, B.B. & Strynadka, N.C. Structural characterization of a type III secretion system filament protein in complex with its chaperone. Nature Struct. Mol. Biol. 12, 75-81 (2005).
    • (2005) Nature Struct. Mol. Biol. , vol.12 , pp. 75-81
    • Yip, C.K.1    Finlay, B.B.2    Strynadka, N.C.3
  • 153
    • 0037350267 scopus 로고    scopus 로고
    • Targeting bacterial virulence: Inhibitors of type III secretion in Yersinia
    • Kauppi, A. M., Nordfelth, R., Uvell, H., Wolf-Watz, H. & Elofsson, M. Targeting bacterial virulence: Inhibitors of type III secretion in Yersinia. Chem. Biol. 10, 241-249 (2003).
    • (2003) Chem. Biol. , vol.10 , pp. 241-249
    • Kauppi, A.M.1    Nordfelth, R.2    Uvell, H.3    Wolf-Watz, H.4    Elofsson, M.5
  • 154
    • 33748490301 scopus 로고    scopus 로고
    • Treatment of Chlamydia trachomatis with a small molecule inhibitor of the Yersinia type III secretion system disrupts progression of the chlamydial developmental cycle
    • Wolf, K. et al. Treatment of Chlamydia trachomatis with a small molecule inhibitor of the Yersinia type III secretion system disrupts progression of the chlamydial developmental cycle. Mol. Microbiol. 61, 1543-1555 (2006).
    • (2006) Mol. Microbiol. , vol.61 , pp. 1543-1555
    • Wolf, K.1
  • 155
    • 33749259792 scopus 로고    scopus 로고
    • A small-molecule inhibitor of type III secretion inhibits different stages of the infectious cycle of Chlamydia trachomatis
    • Muschiol, S. et al. A small-molecule inhibitor of type III secretion inhibits different stages of the infectious cycle of Chlamydia trachomatis. Proc. Natl Acad. Sci. USA 103, 14566-14571 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 14566-14571
    • Muschiol, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.