메뉴 건너뛰기




Volumn 5, Issue 6, 2009, Pages 580-592

Bacterial Adhesins in Host-Microbe Interactions

Author keywords

CELLBIO; MICROBIO

Indexed keywords

ADHESIN; BACTERIAL POLYSACCHARIDE; BACTERIAL PROTEIN; CELL RECEPTOR; CHAPERONE; SORTASE;

EID: 67649408960     PISSN: 19313128     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chom.2009.05.011     Document Type: Review
Times cited : (472)

References (130)
  • 2
    • 65249162778 scopus 로고    scopus 로고
    • Pivotal advance: toll-like receptor regulation of scavenger receptor-A-mediated phagocytosis
    • Amiel E., Alonso A., Uematsu S., Akira S., Poynter M.E., and Berwin B. Pivotal advance: toll-like receptor regulation of scavenger receptor-A-mediated phagocytosis. J. Leukoc. Biol. 85 (2009) 595-605
    • (2009) J. Leukoc. Biol. , vol.85 , pp. 595-605
    • Amiel, E.1    Alonso, A.2    Uematsu, S.3    Akira, S.4    Poynter, M.E.5    Berwin, B.6
  • 4
    • 49449114197 scopus 로고    scopus 로고
    • Pattern recognition receptors and their role in innate immunity: focus on microbial protein ligands
    • Areschoug T., and Gordon S. Pattern recognition receptors and their role in innate immunity: focus on microbial protein ligands. Contrib. Microbiol. 15 (2008) 45-60
    • (2008) Contrib. Microbiol. , vol.15 , pp. 45-60
    • Areschoug, T.1    Gordon, S.2
  • 5
    • 58149337016 scopus 로고    scopus 로고
    • Evasion of macrophage scavenger receptor A-mediated recognition by pathogenic streptococci
    • Areschoug T., Waldemarsson J., and Gordon S. Evasion of macrophage scavenger receptor A-mediated recognition by pathogenic streptococci. Eur. J. Immunol. 38 (2008) 3068-3079
    • (2008) Eur. J. Immunol. , vol.38 , pp. 3068-3079
    • Areschoug, T.1    Waldemarsson, J.2    Gordon, S.3
  • 9
    • 7044249443 scopus 로고    scopus 로고
    • The Streptococcus gordonii surface proteins GspB and Hsa mediate binding to sialylated carbohydrate epitopes on the platelet membrane glycoprotein Ibalpha
    • Bensing B.A., Lopez J.A., and Sullam P.M. The Streptococcus gordonii surface proteins GspB and Hsa mediate binding to sialylated carbohydrate epitopes on the platelet membrane glycoprotein Ibalpha. Infect. Immun. 72 (2004) 6528-6537
    • (2004) Infect. Immun. , vol.72 , pp. 6528-6537
    • Bensing, B.A.1    Lopez, J.A.2    Sullam, P.M.3
  • 11
    • 43249101994 scopus 로고    scopus 로고
    • Cooperative retraction of bundled type IV pili enables nanonewton force generation
    • Biais N., Ladoux B., Higashi D., So M., and Sheetz M. Cooperative retraction of bundled type IV pili enables nanonewton force generation. PLoS Biol. 6 (2008) e87
    • (2008) PLoS Biol. , vol.6
    • Biais, N.1    Ladoux, B.2    Higashi, D.3    So, M.4    Sheetz, M.5
  • 12
    • 0034006823 scopus 로고    scopus 로고
    • Expression of and cytokine activation by Escherichia coli curli fibers in human sepsis
    • Bian Z., Brauner A., Li Y., and Normark S. Expression of and cytokine activation by Escherichia coli curli fibers in human sepsis. J. Infect. Dis. 181 (2000) 602-612
    • (2000) J. Infect. Dis. , vol.181 , pp. 602-612
    • Bian, Z.1    Brauner, A.2    Li, Y.3    Normark, S.4
  • 13
    • 0035865827 scopus 로고    scopus 로고
    • Activation of inducible nitric oxide synthase/nitric oxide by curli fibers leads to a fall in blood pressure during systemic Escherichia coli infection in mice
    • Bian Z., Yan Z.Q., Hansson G.K., Thoren P., and Normark S. Activation of inducible nitric oxide synthase/nitric oxide by curli fibers leads to a fall in blood pressure during systemic Escherichia coli infection in mice. J. Infect. Dis. 183 (2001) 612-619
    • (2001) J. Infect. Dis. , vol.183 , pp. 612-619
    • Bian, Z.1    Yan, Z.Q.2    Hansson, G.K.3    Thoren, P.4    Normark, S.5
  • 14
    • 34249670657 scopus 로고    scopus 로고
    • Cyclic AMP-regulated exocytosis of Escherichia coli from infected bladder epithelial cells
    • Bishop B.L., Duncan M.J., Song J., Li G., Zaas D., and Abraham S.N. Cyclic AMP-regulated exocytosis of Escherichia coli from infected bladder epithelial cells. Nat. Med. 13 (2007) 625-630
    • (2007) Nat. Med. , vol.13 , pp. 625-630
    • Bishop, B.L.1    Duncan, M.J.2    Song, J.3    Li, G.4    Zaas, D.5    Abraham, S.N.6
  • 17
    • 3042681606 scopus 로고    scopus 로고
    • Mucosal vaccination against serogroup B meningococci: induction of bactericidal antibodies and cellular immunity following intranasal immunization with NadA of Neisseria meningitidis and mutants of Escherichia coli heat-labile enterotoxin
    • Bowe F., Lavelle E.C., McNeela E.A., Hale C., Clare S., Arico B., Giuliani M.M., Rae A., Huett A., Rappuoli R., et al. Mucosal vaccination against serogroup B meningococci: induction of bactericidal antibodies and cellular immunity following intranasal immunization with NadA of Neisseria meningitidis and mutants of Escherichia coli heat-labile enterotoxin. Infect. Immun. 72 (2004) 4052-4060
    • (2004) Infect. Immun. , vol.72 , pp. 4052-4060
    • Bowe, F.1    Lavelle, E.C.2    McNeela, E.A.3    Hale, C.4    Clare, S.5    Arico, B.6    Giuliani, M.M.7    Rae, A.8    Huett, A.9    Rappuoli, R.10
  • 19
    • 12344272637 scopus 로고    scopus 로고
    • Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function
    • Carbonnelle E., Helaine S., Prouvensier L., Nassif X., and Pelicic V. Type IV pilus biogenesis in Neisseria meningitidis: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function. Mol. Microbiol. 55 (2005) 54-64
    • (2005) Mol. Microbiol. , vol.55 , pp. 54-64
    • Carbonnelle, E.1    Helaine, S.2    Prouvensier, L.3    Nassif, X.4    Pelicic, V.5
  • 20
    • 33748484296 scopus 로고    scopus 로고
    • A systematic genetic analysis in Neisseria meningitidis defines the Pil proteins required for assembly, functionality, stabilization and export of type IV pili
    • Carbonnelle E., Helaine S., Nassif X., and Pelicic V. A systematic genetic analysis in Neisseria meningitidis defines the Pil proteins required for assembly, functionality, stabilization and export of type IV pili. Mol. Microbiol. 61 (2006) 1510-1522
    • (2006) Mol. Microbiol. , vol.61 , pp. 1510-1522
    • Carbonnelle, E.1    Helaine, S.2    Nassif, X.3    Pelicic, V.4
  • 22
    • 3843151668 scopus 로고    scopus 로고
    • Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213
    • Chen Q., Wu H., and Fives-Taylor P.M. Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213. Mol. Microbiol. 53 (2004) 843-856
    • (2004) Mol. Microbiol. , vol.53 , pp. 843-856
    • Chen, Q.1    Wu, H.2    Fives-Taylor, P.M.3
  • 23
    • 23944519950 scopus 로고    scopus 로고
    • The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats
    • Cherny I., Rockah L., Levy-Nissenbaum O., Gophna U., Ron E.Z., and Gazit E. The formation of Escherichia coli curli amyloid fibrils is mediated by prion-like peptide repeats. J. Mol. Biol. 352 (2005) 245-252
    • (2005) J. Mol. Biol. , vol.352 , pp. 245-252
    • Cherny, I.1    Rockah, L.2    Levy-Nissenbaum, O.3    Gophna, U.4    Ron, E.Z.5    Gazit, E.6
  • 25
    • 18044363515 scopus 로고    scopus 로고
    • Trimeric autotransporters: a distinct subfamily of autotransporter proteins
    • Cotter S.E., Surana N.K., and St Geme III J.W. Trimeric autotransporters: a distinct subfamily of autotransporter proteins. Trends Microbiol. 13 (2005) 199-205
    • (2005) Trends Microbiol. , vol.13 , pp. 199-205
    • Cotter, S.E.1    Surana, N.K.2    St Geme III, J.W.3
  • 26
    • 12244313428 scopus 로고    scopus 로고
    • A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A
    • Deivanayagam C.C., Wann E.R., Chen W., Carson M., Rajashankar K.R., Hook M., and Narayana S.V. A novel variant of the immunoglobulin fold in surface adhesins of Staphylococcus aureus: crystal structure of the fibrinogen-binding MSCRAMM, clumping factor A. EMBO J. 21 (2002) 6660-6672
    • (2002) EMBO J. , vol.21 , pp. 6660-6672
    • Deivanayagam, C.C.1    Wann, E.R.2    Chen, W.3    Carson, M.4    Rajashankar, K.R.5    Hook, M.6    Narayana, S.V.7
  • 28
    • 22744449495 scopus 로고    scopus 로고
    • I-domain-containing integrins serve as pilus receptors for Neisseria gonorrhoeae adherence to human epithelial cells
    • Edwards J.L., and Apicella M.A. I-domain-containing integrins serve as pilus receptors for Neisseria gonorrhoeae adherence to human epithelial cells. Cell. Microbiol. 7 (2005) 1197-1211
    • (2005) Cell. Microbiol. , vol.7 , pp. 1197-1211
    • Edwards, J.L.1    Apicella, M.A.2
  • 30
    • 33845977041 scopus 로고    scopus 로고
    • Biological Trojan horse: antigen 43 provides specific bacterial uptake and survival in human neutrophils
    • Fexby S., Bjarnsholt T., Jensen P.O., Roos V., Hoiby N., Givskov M., and Klemm P. Biological Trojan horse: antigen 43 provides specific bacterial uptake and survival in human neutrophils. Infect. Immun. 75 (2007) 30-34
    • (2007) Infect. Immun. , vol.75 , pp. 30-34
    • Fexby, S.1    Bjarnsholt, T.2    Jensen, P.O.3    Roos, V.4    Hoiby, N.5    Givskov, M.6    Klemm, P.7
  • 32
    • 58849133793 scopus 로고    scopus 로고
    • Factor H binding as a complement evasion mechanism for an anaerobic pathogen, Fusobacterium necrophorum
    • Friberg N., Carlson P., Kentala E., Mattila P.S., Kuusela P., Meri S., and Jarva H. Factor H binding as a complement evasion mechanism for an anaerobic pathogen, Fusobacterium necrophorum. J. Immunol. 181 (2008) 8624-8632
    • (2008) J. Immunol. , vol.181 , pp. 8624-8632
    • Friberg, N.1    Carlson, P.2    Kentala, E.3    Mattila, P.S.4    Kuusela, P.5    Meri, S.6    Jarva, H.7
  • 33
  • 34
    • 57149093798 scopus 로고    scopus 로고
    • A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics
    • Ganesh V.K., Rivera J.J., Smeds E., Ko Y.P., Bowden M.G., Wann E.R., Gurusiddappa S., Fitzgerald J.R., and Hook M. A structural model of the Staphylococcus aureus ClfA-fibrinogen interaction opens new avenues for the design of anti-staphylococcal therapeutics. PLoS Pathog. 4 (2008) e1000226
    • (2008) PLoS Pathog. , vol.4
    • Ganesh, V.K.1    Rivera, J.J.2    Smeds, E.3    Ko, Y.P.4    Bowden, M.G.5    Wann, E.R.6    Gurusiddappa, S.7    Fitzgerald, J.R.8    Hook, M.9
  • 36
    • 4444299763 scopus 로고    scopus 로고
    • CD46 in Neisseria pathogenesis
    • Gill D.B., and Atkinson J.P. CD46 in Neisseria pathogenesis. Trends Mol. Med. 10 (2004) 459-465
    • (2004) Trends Mol. Med. , vol.10 , pp. 459-465
    • Gill, D.B.1    Atkinson, J.P.2
  • 37
    • 33744519083 scopus 로고    scopus 로고
    • Adhesion mediated by autotransporters of Gram-negative bacteria: structural and functional features
    • Girard V., and Mourez M. Adhesion mediated by autotransporters of Gram-negative bacteria: structural and functional features. Res. Microbiol. 157 (2006) 407-416
    • (2006) Res. Microbiol. , vol.157 , pp. 407-416
    • Girard, V.1    Mourez, M.2
  • 38
    • 11144331374 scopus 로고    scopus 로고
    • Vaccination with purified Dr Fimbriae reduces mortality associated with chronic urinary tract infection due to Escherichia coli bearing Dr adhesin
    • Goluszko P., Goluszko E., Nowicki B., Nowicki S., Popov V., and Wang H.Q. Vaccination with purified Dr Fimbriae reduces mortality associated with chronic urinary tract infection due to Escherichia coli bearing Dr adhesin. Infect. Immun. 73 (2005) 627-631
    • (2005) Infect. Immun. , vol.73 , pp. 627-631
    • Goluszko, P.1    Goluszko, E.2    Nowicki, B.3    Nowicki, S.4    Popov, V.5    Wang, H.Q.6
  • 41
    • 33749258758 scopus 로고    scopus 로고
    • Porphyromonas gingivalis fimbriae proactively modulate beta2 integrin adhesive activity and promote binding to and internalization by macrophages
    • Hajishengallis G., Wang M., Harokopakis E., Triantafilou M., and Triantafilou K. Porphyromonas gingivalis fimbriae proactively modulate beta2 integrin adhesive activity and promote binding to and internalization by macrophages. Infect. Immun. 74 (2006) 5658-5666
    • (2006) Infect. Immun. , vol.74 , pp. 5658-5666
    • Hajishengallis, G.1    Wang, M.2    Harokopakis, E.3    Triantafilou, M.4    Triantafilou, K.5
  • 43
    • 33748773323 scopus 로고    scopus 로고
    • Type IV pilin structures: insights on shared architecture, fiber assembly, receptor binding and type II secretion
    • Hansen J.K., and Forest K.T. Type IV pilin structures: insights on shared architecture, fiber assembly, receptor binding and type II secretion. J. Mol. Microbiol. Biotechnol. 11 (2006) 192-207
    • (2006) J. Mol. Microbiol. Biotechnol. , vol.11 , pp. 192-207
    • Hansen, J.K.1    Forest, K.T.2
  • 44
    • 33744903384 scopus 로고    scopus 로고
    • TLR2 transmodulates monocyte adhesion and transmigration via Rac1- and PI3K-mediated inside-out signaling in response to Porphyromonas gingivalis fimbriae
    • Harokopakis E., Albzreh M.H., Martin M.H., and Hajishengallis G. TLR2 transmodulates monocyte adhesion and transmigration via Rac1- and PI3K-mediated inside-out signaling in response to Porphyromonas gingivalis fimbriae. J. Immunol. 176 (2006) 7645-7656
    • (2006) J. Immunol. , vol.176 , pp. 7645-7656
    • Harokopakis, E.1    Albzreh, M.H.2    Martin, M.H.3    Hajishengallis, G.4
  • 45
    • 2642635843 scopus 로고    scopus 로고
    • Activation of the contact-phase system on bacterial surfaces-a clue to serious complications in infectious diseases
    • Herwald H., Morgelin M., Olsen A., Rhen M., Dahlback B., Muller-Esterl W., and Bjorck L. Activation of the contact-phase system on bacterial surfaces-a clue to serious complications in infectious diseases. Nat. Med. 4 (1998) 298-302
    • (1998) Nat. Med. , vol.4 , pp. 298-302
    • Herwald, H.1    Morgelin, M.2    Olsen, A.3    Rhen, M.4    Dahlback, B.5    Muller-Esterl, W.6    Bjorck, L.7
  • 46
    • 34848820894 scopus 로고    scopus 로고
    • Dynamics of Neisseria gonorrhoeae attachment: microcolony development, cortical plaque formation, and cytoprotection
    • Higashi D.L., Lee S.W., Snyder A., Weyand N.J., Bakke A., and So M. Dynamics of Neisseria gonorrhoeae attachment: microcolony development, cortical plaque formation, and cytoprotection. Infect. Immun. 75 (2007) 4743-4753
    • (2007) Infect. Immun. , vol.75 , pp. 4743-4753
    • Higashi, D.L.1    Lee, S.W.2    Snyder, A.3    Weyand, N.J.4    Bakke, A.5    So, M.6
  • 47
    • 0034669051 scopus 로고    scopus 로고
    • Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins
    • Hoiczyk E., Roggenkamp A., Reichenbecher M., Lupas A., and Heesemann J. Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesins. EMBO J. 19 (2000) 5989-5999
    • (2000) EMBO J. , vol.19 , pp. 5989-5999
    • Hoiczyk, E.1    Roggenkamp, A.2    Reichenbecher, M.3    Lupas, A.4    Heesemann, J.5
  • 48
    • 46249115222 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activation by Neisseria gonorrhoeae downregulates epithelial cell proapoptotic proteins Bad and Bim
    • Howie H.L., Shiflett S.L., and So M. Extracellular signal-regulated kinase activation by Neisseria gonorrhoeae downregulates epithelial cell proapoptotic proteins Bad and Bim. Infect. Immun. 76 (2008) 2715-2721
    • (2008) Infect. Immun. , vol.76 , pp. 2715-2721
    • Howie, H.L.1    Shiflett, S.L.2    So, M.3
  • 49
    • 0345586153 scopus 로고
    • The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus
    • Hultgren S.J., Lindberg F., Magnusson G., Kihlberg J., Tennent J.M., and Normark S. The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus. Proc. Natl. Acad. Sci. USA 86 (1989) 4357-4361
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4357-4361
    • Hultgren, S.J.1    Lindberg, F.2    Magnusson, G.3    Kihlberg, J.4    Tennent, J.M.5    Normark, S.6
  • 51
    • 0028001464 scopus 로고
    • Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18)
    • Ishibashi Y., Claus S., and Relman D.A. Bordetella pertussis filamentous hemagglutinin interacts with a leukocyte signal transduction complex and stimulates bacterial adherence to monocyte CR3 (CD11b/CD18). J. Exp. Med. 180 (1994) 1225-1233
    • (1994) J. Exp. Med. , vol.180 , pp. 1225-1233
    • Ishibashi, Y.1    Claus, S.2    Relman, D.A.3
  • 52
    • 33845933694 scopus 로고    scopus 로고
    • Filamentation by Escherichia coli subverts innate defenses during urinary tract infection
    • Justice S.S., Hunstad D.A., Seed P.C., and Hultgren S.J. Filamentation by Escherichia coli subverts innate defenses during urinary tract infection. Proc. Natl. Acad. Sci. USA 103 (2006) 19884-19889
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 19884-19889
    • Justice, S.S.1    Hunstad, D.A.2    Seed, P.C.3    Hultgren, S.J.4
  • 53
    • 0019481791 scopus 로고
    • Structure of carbohydrate part of receptor on human uroepithelial cells for pyelonephritogenic Escherichia coli
    • Kallenius G., Svenson S., Mollby R., Cedergren B., Hultberg H., and Winberg J. Structure of carbohydrate part of receptor on human uroepithelial cells for pyelonephritogenic Escherichia coli. Lancet 2 (1981) 604-606
    • (1981) Lancet , vol.2 , pp. 604-606
    • Kallenius, G.1    Svenson, S.2    Mollby, R.3    Cedergren, B.4    Hultberg, H.5    Winberg, J.6
  • 54
    • 33646005763 scopus 로고    scopus 로고
    • A dominant complement fixation pathway for pneumococcal polysaccharides initiated by SIGN-R1 interacting with C1q
    • Kang Y.S., Do Y., Lee H.K., Park S.H., Cheong C., Lynch R.M., Loeffler J.M., Steinman R.M., and Park C.G. A dominant complement fixation pathway for pneumococcal polysaccharides initiated by SIGN-R1 interacting with C1q. Cell 125 (2006) 47-58
    • (2006) Cell , vol.125 , pp. 47-58
    • Kang, Y.S.1    Do, Y.2    Lee, H.K.3    Park, S.H.4    Cheong, C.5    Lynch, R.M.6    Loeffler, J.M.7    Steinman, R.M.8    Park, C.G.9
  • 55
    • 35548963800 scopus 로고    scopus 로고
    • Animal protection and structural studies of a consensus sequence vaccine targeting the receptor binding domain of the type IV pilus of Pseudomonas aeruginosa
    • Kao D.J., Churchill M.E., Irvin R.T., and Hodges R.S. Animal protection and structural studies of a consensus sequence vaccine targeting the receptor binding domain of the type IV pilus of Pseudomonas aeruginosa. J. Mol. Biol. 374 (2007) 426-442
    • (2007) J. Mol. Biol. , vol.374 , pp. 426-442
    • Kao, D.J.1    Churchill, M.E.2    Irvin, R.T.3    Hodges, R.S.4
  • 56
    • 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., and Elofsson M. Targeting bacterial virulence: inhibitors of type III secretion in Yersinia. Chem. Biol. 10 (2003) 241-249
    • (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
  • 57
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny B., DeVinney R., Stein M., Reinscheid D.J., Frey E.A., and Finlay B.B. Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91 (1997) 511-520
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 58
    • 18444380597 scopus 로고    scopus 로고
    • The PilC adhesin of the Neisseria type IV pilus-binding specificities and new insights into the nature of the host cell receptor
    • Kirchner M., and Meyer T.F. The PilC adhesin of the Neisseria type IV pilus-binding specificities and new insights into the nature of the host cell receptor. Mol. Microbiol. 56 (2005) 945-957
    • (2005) Mol. Microbiol. , vol.56 , pp. 945-957
    • Kirchner, M.1    Meyer, T.F.2
  • 59
    • 17644417153 scopus 로고    scopus 로고
    • CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells
    • Kirchner M., Heuer D., and Meyer T.F. CD46-independent binding of neisserial type IV pili and the major pilus adhesin, PilC, to human epithelial cells. Infect. Immun. 73 (2005) 3072-3082
    • (2005) Infect. Immun. , vol.73 , pp. 3072-3082
    • Kirchner, M.1    Heuer, D.2    Meyer, T.F.3
  • 60
    • 50849105103 scopus 로고    scopus 로고
    • Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein
    • Kirjavainen V., Jarva H., Biedzka-Sarek M., Blom A.M., Skurnik M., and Meri S. Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein. PLoS Pathog. 4 (2008) e1000140
    • (2008) PLoS Pathog. , vol.4
    • Kirjavainen, V.1    Jarva, H.2    Biedzka-Sarek, M.3    Blom, A.M.4    Skurnik, M.5    Meri, S.6
  • 62
    • 51949106120 scopus 로고    scopus 로고
    • Escherichia coli DraE adhesin-associated bacterial internalization by epithelial cells is promoted independently by decay-accelerating factor and carcinoembryonic antigen-related cell adhesion molecule binding and does not require the DraD invasin
    • Korotkova N., Yarova-Yarovaya Y., Tchesnokova V., Yazvenko N., Carl M.A., Stapleton A.E., and Moseley S.L. Escherichia coli DraE adhesin-associated bacterial internalization by epithelial cells is promoted independently by decay-accelerating factor and carcinoembryonic antigen-related cell adhesion molecule binding and does not require the DraD invasin. Infect. Immun. 76 (2008) 3869-3880
    • (2008) Infect. Immun. , vol.76 , pp. 3869-3880
    • Korotkova, N.1    Yarova-Yarovaya, Y.2    Tchesnokova, V.3    Yazvenko, N.4    Carl, M.A.5    Stapleton, A.E.6    Moseley, S.L.7
  • 66
    • 33750723428 scopus 로고    scopus 로고
    • Meningococcal biofilm formation: structure, development and phenotypes in a standardized continuous flow system
    • Lappann M., Haagensen J.A., Claus H., Vogel U., and Molin S. Meningococcal biofilm formation: structure, development and phenotypes in a standardized continuous flow system. Mol. Microbiol. 62 (2006) 1292-1309
    • (2006) Mol. Microbiol. , vol.62 , pp. 1292-1309
    • Lappann, M.1    Haagensen, J.A.2    Claus, H.3    Vogel, U.4    Molin, S.5
  • 67
    • 0019852815 scopus 로고
    • Glycolipid receptors for uropathogenic Escherichia coli on human erythrocytes and uroepithelial cells
    • Leffler H., and Svanborg-Eden C. Glycolipid receptors for uropathogenic Escherichia coli on human erythrocytes and uroepithelial cells. Infect. Immun. 34 (1981) 920-929
    • (1981) Infect. Immun. , vol.34 , pp. 920-929
    • Leffler, H.1    Svanborg-Eden, C.2
  • 68
    • 33744728321 scopus 로고    scopus 로고
    • Trimeric autotransporter adhesins: variable structure, common function
    • Linke D., Riess T., Autenrieth I.B., Lupas A., and Kempf V.A. Trimeric autotransporter adhesins: variable structure, common function. Trends Microbiol. 14 (2006) 264-270
    • (2006) Trends Microbiol. , vol.14 , pp. 264-270
    • Linke, D.1    Riess, T.2    Autenrieth, I.B.3    Lupas, A.4    Kempf, V.A.5
  • 71
    • 33846910750 scopus 로고    scopus 로고
    • Group B streptococcal pilus proteins contribute to adherence to and invasion of brain microvascular endothelial cells
    • Maisey H.C., Hensler M., Nizet V., and Doran K.S. Group B streptococcal pilus proteins contribute to adherence to and invasion of brain microvascular endothelial cells. J. Bacteriol. 189 (2007) 1464-1467
    • (2007) J. Bacteriol. , vol.189 , pp. 1464-1467
    • Maisey, H.C.1    Hensler, M.2    Nizet, V.3    Doran, K.S.4
  • 72
    • 52949117534 scopus 로고    scopus 로고
    • The molecular switch that activates the cell wall anchoring step of pilus assembly in gram-positive bacteria
    • Mandlik A., Das A., and Ton-That H. The molecular switch that activates the cell wall anchoring step of pilus assembly in gram-positive bacteria. Proc. Natl. Acad. Sci. USA 105 (2008) 14147-14152
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 14147-14152
    • Mandlik, A.1    Das, A.2    Ton-That, H.3
  • 73
    • 37749043209 scopus 로고    scopus 로고
    • Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development
    • Mandlik A., Swierczynski A., Das A., and Ton-That H. Pili in Gram-positive bacteria: assembly, involvement in colonization and biofilm development. Trends Microbiol. 16 (2008) 33-40
    • (2008) Trends Microbiol. , vol.16 , pp. 33-40
    • Mandlik, A.1    Swierczynski, A.2    Das, A.3    Ton-That, H.4
  • 77
    • 0034518454 scopus 로고    scopus 로고
    • Interactions of pathogenic neisseriae with epithelial cell membranes
    • Merz A.J., and So M. Interactions of pathogenic neisseriae with epithelial cell membranes. Annu. Rev. Cell Dev. Biol. 16 (2000) 423-457
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 423-457
    • Merz, A.J.1    So, M.2
  • 83
    • 0021961909 scopus 로고
    • Molecular basis of Escherichia coli colonization of the upper urinary tract in BALB/c mice. Gal-Gal pili immunization prevents Escherichia coli pyelonephritis in the BALB/c mouse model of human pyelonephritis
    • O'Hanley P., Lark D., Falkow S., and Schoolnik G. Molecular basis of Escherichia coli colonization of the upper urinary tract in BALB/c mice. Gal-Gal pili immunization prevents Escherichia coli pyelonephritis in the BALB/c mouse model of human pyelonephritis. J. Clin. Invest. 75 (1985) 347-360
    • (1985) J. Clin. Invest. , vol.75 , pp. 347-360
    • O'Hanley, P.1    Lark, D.2    Falkow, S.3    Schoolnik, G.4
  • 85
    • 11144281811 scopus 로고    scopus 로고
    • Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: characterization of DraB-DraE complexes
    • Piatek R., Zalewska B., Kolaj O., Ferens M., Nowicki B., and Kur J. Molecular aspects of biogenesis of Escherichia coli Dr Fimbriae: characterization of DraB-DraE complexes. Infect. Immun. 73 (2005) 135-145
    • (2005) Infect. Immun. , vol.73 , pp. 135-145
    • Piatek, R.1    Zalewska, B.2    Kolaj, O.3    Ferens, M.4    Nowicki, B.5    Kur, J.6
  • 87
    • 67649394036 scopus 로고    scopus 로고
    • SR-A, MARCO and TLRs differentially recognise selected surface proteins from Neisseria meningitidis: an example of fine specificity in microbial ligand recognition by innate immune receptors
    • Plüddemann A., Mukhopadhyay S., Sankala M., Savino S., Pizza M., Rappuoli R., Tryggvason K., and Gordon S. SR-A, MARCO and TLRs differentially recognise selected surface proteins from Neisseria meningitidis: an example of fine specificity in microbial ligand recognition by innate immune receptors. J. Innate Immun. 1 (2009) 153-163
    • (2009) J. Innate Immun. , vol.1 , pp. 153-163
    • Plüddemann, A.1    Mukhopadhyay, S.2    Sankala, M.3    Savino, S.4    Pizza, M.5    Rappuoli, R.6    Tryggvason, K.7    Gordon, S.8
  • 89
    • 60149111839 scopus 로고    scopus 로고
    • Pili in Gram-negative and Gram-positive bacteria-structure, assembly and their role in disease
    • Proft T., and Baker E.N. Pili in Gram-negative and Gram-positive bacteria-structure, assembly and their role in disease. Cell. Mol. Life Sci. 66 (2009) 613-635
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 613-635
    • Proft, T.1    Baker, E.N.2
  • 90
    • 33745195658 scopus 로고    scopus 로고
    • Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism
    • Remaut H., Rose R.J., Hannan T.J., Hultgren S.J., Radford S.E., Ashcroft A.E., and Waksman G. Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted beta strand displacement mechanism. Mol. Cell 22 (2006) 831-842
    • (2006) Mol. Cell , vol.22 , pp. 831-842
    • Remaut, H.1    Rose, R.J.2    Hannan, T.J.3    Hultgren, S.J.4    Radford, S.E.5    Ashcroft, A.E.6    Waksman, G.7
  • 93
    • 48749094614 scopus 로고    scopus 로고
    • Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge
    • Rose L., Shivshankar P., Hinojosa E., Rodriguez A., Sanchez C.J., and Orihuela C.J. Antibodies against PsrP, a novel Streptococcus pneumoniae adhesin, block adhesion and protect mice against pneumococcal challenge. J. Infect. Dis. 198 (2008) 375-383
    • (2008) J. Infect. Dis. , vol.198 , pp. 375-383
    • Rose, L.1    Shivshankar, P.2    Hinojosa, E.3    Rodriguez, A.4    Sanchez, C.J.5    Orihuela, C.J.6
  • 95
    • 59049093883 scopus 로고    scopus 로고
    • Enterotoxigenic Escherichia coli EtpA mediates adhesion between flagella and host cells
    • Roy K., Hilliard G.M., Hamilton D.J., Luo J., Ostmann M.M., and Fleckenstein J.M. Enterotoxigenic Escherichia coli EtpA mediates adhesion between flagella and host cells. Nature 457 (2009) 594-598
    • (2009) Nature , vol.457 , pp. 594-598
    • Roy, K.1    Hilliard, G.M.2    Hamilton, D.J.3    Luo, J.4    Ostmann, M.M.5    Fleckenstein, J.M.6
  • 96
    • 0028795092 scopus 로고
    • Neisseria PilC protein identified as type-4 pilus tip-located adhesin
    • Rudel T., Scheurerpflug I., and Meyer T.F. Neisseria PilC protein identified as type-4 pilus tip-located adhesin. Nature 373 (1995) 357-359
    • (1995) Nature , vol.373 , pp. 357-359
    • Rudel, T.1    Scheurerpflug, I.2    Meyer, T.F.3
  • 97
    • 66149090368 scopus 로고    scopus 로고
    • The Escherichia coli common pilus and the bundle-forming pilus act in concert during the formation of localized adherence by enteropathogenic E. coli
    • Saldana Z., Erdem A.L., Schuller S., Okeke I.N., Lucas M., Sivananthan A., Phillips A.D., Kaper J.B., Puente J.L., and Giron J.A. The Escherichia coli common pilus and the bundle-forming pilus act in concert during the formation of localized adherence by enteropathogenic E. coli. J. Bacteriol. 191 (2009) 3451-3461
    • (2009) J. Bacteriol. , vol.191 , pp. 3451-3461
    • Saldana, Z.1    Erdem, A.L.2    Schuller, S.3    Okeke, I.N.4    Lucas, M.5    Sivananthan, A.6    Phillips, A.D.7    Kaper, J.B.8    Puente, J.L.9    Giron, J.A.10
  • 98
    • 63849126614 scopus 로고    scopus 로고
    • Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli
    • Saldana Z., Xicohtencatl-Cortes J., Avelino F., Phillips A.D., Kaper J.B., Puente J.L., and Giron J.A. Synergistic role of curli and cellulose in cell adherence and biofilm formation of attaching and effacing Escherichia coli and identification of Fis as a negative regulator of curli. Environ. Microbiol. 11 (2009) 992-1006
    • (2009) Environ. Microbiol. , vol.11 , pp. 992-1006
    • Saldana, Z.1    Xicohtencatl-Cortes, J.2    Avelino, F.3    Phillips, A.D.4    Kaper, J.B.5    Puente, J.L.6    Giron, J.A.7
  • 99
    • 34548125418 scopus 로고    scopus 로고
    • Inhibition of P-fimbriated Escherichia coli adhesion by multivalent galabiose derivatives studied by a live-bacteria application of surface plasmon resonance
    • Salminen A., Loimaranta V., Joosten J.A., Khan A.S., Hacker J., Pieters R.J., and Finne J. Inhibition of P-fimbriated Escherichia coli adhesion by multivalent galabiose derivatives studied by a live-bacteria application of surface plasmon resonance. J. Antimicrob. Chemother. 60 (2007) 495-501
    • (2007) J. Antimicrob. Chemother. , vol.60 , pp. 495-501
    • Salminen, A.1    Loimaranta, V.2    Joosten, J.A.3    Khan, A.S.4    Hacker, J.5    Pieters, R.J.6    Finne, J.7
  • 101
    • 0035283006 scopus 로고    scopus 로고
    • Structure and function of Escherichia coli type 1 pili: new insight into the pathogenesis of urinary tract infections
    • Schilling J.D., Mulvey M.A., and Hultgren S.J. Structure and function of Escherichia coli type 1 pili: new insight into the pathogenesis of urinary tract infections. J. Infect. Dis. 183 Suppl 1 (2001) S36-S40
    • (2001) J. Infect. Dis. , vol.183 , Issue.SUPPL. 1
    • Schilling, J.D.1    Mulvey, M.A.2    Hultgren, S.J.3
  • 102
    • 0037388307 scopus 로고    scopus 로고
    • Toll-like receptor 4 on stromal and hematopoietic cells mediates innate resistance to uropathogenic Escherichia coli
    • Schilling J.D., Martin S.M., Hung C.S., Lorenz R.G., and Hultgren S.J. Toll-like receptor 4 on stromal and hematopoietic cells mediates innate resistance to uropathogenic Escherichia coli. Proc. Natl. Acad. Sci. USA 100 (2003) 4203-4208
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4203-4208
    • Schilling, J.D.1    Martin, S.M.2    Hung, C.S.3    Lorenz, R.G.4    Hultgren, S.J.5
  • 104
    • 33749184817 scopus 로고    scopus 로고
    • Pili with strong attachments: Gram-positive bacteria do it differently
    • Scott J.R., and Zahner D. Pili with strong attachments: Gram-positive bacteria do it differently. Mol. Microbiol. 62 (2006) 320-330
    • (2006) Mol. Microbiol. , vol.62 , pp. 320-330
    • Scott, J.R.1    Zahner, D.2
  • 105
    • 0037106334 scopus 로고    scopus 로고
    • Irreversible inhibition of the bacterial cysteine protease-transpeptidase sortase (SrtA) by substrate-derived affinity labels
    • Scott C.J., McDowell A., Martin S.L., Lynas J.F., Vandenbroeck K., and Walker B. Irreversible inhibition of the bacterial cysteine protease-transpeptidase sortase (SrtA) by substrate-derived affinity labels. Biochem. J. 366 (2002) 953-958
    • (2002) Biochem. J. , vol.366 , pp. 953-958
    • Scott, C.J.1    McDowell, A.2    Martin, S.L.3    Lynas, J.F.4    Vandenbroeck, K.5    Walker, B.6
  • 106
    • 66749138696 scopus 로고    scopus 로고
    • HadA is an atypical new multifunctional trimeric coiled-coil adhesin of Haemophilus influenzae biogroup aegyptius, which promotes entry into host cells
    • 10.1111/j.1462-5822.2009.01306.x in press. Published online March 26, 2009
    • Serruto D., Spadafina T., Scarselli M., Bambini S., Comanducci M., Hohle S., Kilian M., Veiga E., Cossart P., Oggioni M.R., et al. HadA is an atypical new multifunctional trimeric coiled-coil adhesin of Haemophilus influenzae biogroup aegyptius, which promotes entry into host cells. Cell. Microbiol. (2009) 10.1111/j.1462-5822.2009.01306.x in press. Published online March 26, 2009
    • (2009) Cell. Microbiol.
    • Serruto, D.1    Spadafina, T.2    Scarselli, M.3    Bambini, S.4    Comanducci, M.5    Hohle, S.6    Kilian, M.7    Veiga, E.8    Cossart, P.9    Oggioni, M.R.10
  • 108
    • 16244372364 scopus 로고    scopus 로고
    • Role of SraP, a serine-rich surface protein of Staphylococcus aureus, in binding to human platelets
    • Siboo I.R., Chambers H.F., and Sullam P.M. Role of SraP, a serine-rich surface protein of Staphylococcus aureus, in binding to human platelets. Infect. Immun. 73 (2005) 2273-2280
    • (2005) Infect. Immun. , vol.73 , pp. 2273-2280
    • Siboo, I.R.1    Chambers, H.F.2    Sullam, P.M.3
  • 109
    • 34249079398 scopus 로고    scopus 로고
    • Importance of the ebp (endocarditis- and biofilm-associated pilus) locus in the pathogenesis of Enterococcus faecalis ascending urinary tract infection
    • Singh K.V., Nallapareddy S.R., and Murray B.E. Importance of the ebp (endocarditis- and biofilm-associated pilus) locus in the pathogenesis of Enterococcus faecalis ascending urinary tract infection. J. Infect. Dis. 195 (2007) 1671-1677
    • (2007) J. Infect. Dis. , vol.195 , pp. 1671-1677
    • Singh, K.V.1    Nallapareddy, S.R.2    Murray, B.E.3
  • 110
    • 55849083867 scopus 로고    scopus 로고
    • Meningococcal outer membrane protein NhhA is essential for colonization and disease by preventing phagocytosis and complement attack
    • Sjolinder H., Eriksson J., Maudsdotter L., Aro H., and Jonsson A.B. Meningococcal outer membrane protein NhhA is essential for colonization and disease by preventing phagocytosis and complement attack. Infect. Immun. 76 (2008) 5412-5420
    • (2008) Infect. Immun. , vol.76 , pp. 5412-5420
    • Sjolinder, H.1    Eriksson, J.2    Maudsdotter, L.3    Aro, H.4    Jonsson, A.B.5
  • 112
    • 34249886044 scopus 로고    scopus 로고
    • TLR4-initiated and cAMP-mediated abrogation of bacterial invasion of the bladder
    • Song J., Bishop B.L., Li G., Duncan M.J., and Abraham S.N. TLR4-initiated and cAMP-mediated abrogation of bacterial invasion of the bladder. Cell Host Microbe 1 (2007) 287-298
    • (2007) Cell Host Microbe , vol.1 , pp. 287-298
    • Song, J.1    Bishop, B.L.2    Li, G.3    Duncan, M.J.4    Abraham, S.N.5
  • 113
    • 1842456935 scopus 로고    scopus 로고
    • Immunogenic properties of the Salmonella atypical fimbriae in BALB/c mice
    • Strindelius L., Folkesson A., Normark S., and Sjoholm I. Immunogenic properties of the Salmonella atypical fimbriae in BALB/c mice. Vaccine 22 (2004) 1448-1456
    • (2004) Vaccine , vol.22 , pp. 1448-1456
    • Strindelius, L.1    Folkesson, A.2    Normark, S.3    Sjoholm, I.4
  • 114
    • 0031724534 scopus 로고    scopus 로고
    • Type I Helicobacter pylori shows Lewis(b)-independent adherence to gastric cells requiring de novo protein synthesis in both host and bacteria
    • Su B., Hellstrom P.M., Rubio C., Celik J., Granstrom M., and Normark S. Type I Helicobacter pylori shows Lewis(b)-independent adherence to gastric cells requiring de novo protein synthesis in both host and bacteria. J. Infect. Dis. 178 (1998) 1379-1390
    • (1998) J. Infect. Dis. , vol.178 , pp. 1379-1390
    • Su, B.1    Hellstrom, P.M.2    Rubio, C.3    Celik, J.4    Granstrom, M.5    Normark, S.6
  • 115
    • 0025336528 scopus 로고
    • Antibodies directed against the toxin-coregulated pilus isolated from Vibrio cholerae provide protection in the infant mouse experimental cholera model
    • Sun D.X., Mekalanos J.J., and Taylor R.K. Antibodies directed against the toxin-coregulated pilus isolated from Vibrio cholerae provide protection in the infant mouse experimental cholera model. J. Infect. Dis. 161 (1990) 1231-1236
    • (1990) J. Infect. Dis. , vol.161 , pp. 1231-1236
    • Sun, D.X.1    Mekalanos, J.J.2    Taylor, R.K.3
  • 116
    • 49449093139 scopus 로고    scopus 로고
    • Vaccines against enterotoxigenic Escherichia coli
    • Svennerholm A.M., and Tobias J. Vaccines against enterotoxigenic Escherichia coli. Expert Rev. Vaccines 7 (2008) 795-804
    • (2008) Expert Rev. Vaccines , vol.7 , pp. 795-804
    • Svennerholm, A.M.1    Tobias, J.2
  • 119
    • 0027180060 scopus 로고
    • Role of plasmid-encoded antigens of Yersinia enterocolitica in humoral immunity against secondary Y. enterocolitica infection in mice
    • Vogel U., Autenrieth I.B., Berner R., and Heesemann J. Role of plasmid-encoded antigens of Yersinia enterocolitica in humoral immunity against secondary Y. enterocolitica infection in mice. Microb. Pathog. 15 (1993) 23-36
    • (1993) Microb. Pathog. , vol.15 , pp. 23-36
    • Vogel, U.1    Autenrieth, I.B.2    Berner, R.3    Heesemann, J.4
  • 120
    • 34848908962 scopus 로고    scopus 로고
    • Fimbrial proteins of porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and complement receptor 3 to persist in macrophages
    • Wang M., Shakhatreh M.A., James D., Liang S., Nishiyama S., Yoshimura F., Demuth D.R., and Hajishengallis G. Fimbrial proteins of porphyromonas gingivalis mediate in vivo virulence and exploit TLR2 and complement receptor 3 to persist in macrophages. J. Immunol. 179 (2007) 2349-2358
    • (2007) J. Immunol. , vol.179 , pp. 2349-2358
    • Wang, M.1    Shakhatreh, M.A.2    James, D.3    Liang, S.4    Nishiyama, S.5    Yoshimura, F.6    Demuth, D.R.7    Hajishengallis, G.8
  • 122
    • 18444401131 scopus 로고    scopus 로고
    • A conserved set of pilin-like molecules controls type IV pilus dynamics and organelle-associated functions in Neisseria gonorrhoeae
    • Winther-Larsen H.C., Wolfgang M., Dunham S., van Putten J.P., Dorward D., Lovold C., Aas F.E., and Koomey M. A conserved set of pilin-like molecules controls type IV pilus dynamics and organelle-associated functions in Neisseria gonorrhoeae. Mol. Microbiol. 56 (2005) 903-917
    • (2005) Mol. Microbiol. , vol.56 , pp. 903-917
    • Winther-Larsen, H.C.1    Wolfgang, M.2    Dunham, S.3    van Putten, J.P.4    Dorward, D.5    Lovold, C.6    Aas, F.E.7    Koomey, M.8
  • 123
    • 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. Components and dynamics of fiber formation define a ubiquitous biogenesis pathway for bacterial pili. EMBO J. 19 (2000) 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
  • 124
    • 34547909227 scopus 로고    scopus 로고
    • Development of intracellular bacterial communities of uropathogenic Escherichia coli depends on type 1 pili
    • Wright K.J., Seed P.C., and Hultgren S.J. Development of intracellular bacterial communities of uropathogenic Escherichia coli depends on type 1 pili. Cell. Microbiol. 9 (2007) 2230-2241
    • (2007) Cell. Microbiol. , vol.9 , pp. 2230-2241
    • Wright, K.J.1    Seed, P.C.2    Hultgren, S.J.3
  • 125
    • 0035022986 scopus 로고    scopus 로고
    • Molecular strategies for fimbrial expression and assembly
    • Wu H., and Fives-Taylor P.M. Molecular strategies for fimbrial expression and assembly. Crit. Rev. Oral Biol. Med. 12 (2001) 101-115
    • (2001) Crit. Rev. Oral Biol. Med. , vol.12 , pp. 101-115
    • Wu, H.1    Fives-Taylor, P.M.2
  • 127
    • 0014255292 scopus 로고
    • Electron microscopy of fine structure of Corynebacterium renale with special reference to pili
    • Yanagawa R., Otsuki K., and Tokui T. Electron microscopy of fine structure of Corynebacterium renale with special reference to pili. Jpn. J. Vet. Res. 16 (1968) 31-37
    • (1968) Jpn. J. Vet. Res. , vol.16 , pp. 31-37
    • Yanagawa, R.1    Otsuki, K.2    Tokui, T.3
  • 128
    • 0005143931 scopus 로고    scopus 로고
    • Actinomyces: surface macromolecules and bacteria-host interactions
    • Fischetti V.A., Novick R.P., Feretti J.J., Portnoy D.A., and Rood J.I. (Eds), American Society for Microbiology, Washington, DC
    • Yeung M.K. Actinomyces: surface macromolecules and bacteria-host interactions. In: Fischetti V.A., Novick R.P., Feretti J.J., Portnoy D.A., and Rood J.I. (Eds). Gram-Positive Pathogens (2000), American Society for Microbiology, Washington, DC 583-593
    • (2000) Gram-Positive Pathogens , pp. 583-593
    • Yeung, M.K.1
  • 129
    • 42949155298 scopus 로고    scopus 로고
    • Human dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells
    • Zhang P., Skurnik M., Zhang S.S., Schwartz O., Kalyanasundaram R., Bulgheresi S., He J.J., Klena J.D., Hinnebusch B.J., and Chen T. Human dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells. Infect. Immun. 76 (2008) 2070-2079
    • (2008) Infect. Immun. , vol.76 , pp. 2070-2079
    • Zhang, P.1    Skurnik, M.2    Zhang, S.S.3    Schwartz, O.4    Kalyanasundaram, R.5    Bulgheresi, S.6    He, J.J.7    Klena, J.D.8    Hinnebusch, B.J.9    Chen, T.10
  • 130
    • 0035065254 scopus 로고    scopus 로고
    • The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix
    • Zogaj X., Nimtz M., Rohde M., Bokranz W., and Romling U. The multicellular morphotypes of Salmonella typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix. Mol. Microbiol. 39 (2001) 1452-1463
    • (2001) Mol. Microbiol. , vol.39 , pp. 1452-1463
    • Zogaj, X.1    Nimtz, M.2    Rohde, M.3    Bokranz, W.4    Romling, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.