메뉴 건너뛰기




Volumn 16, Issue 1, 2013, Pages 17-22

The impact of Toll-like receptors on bacterial virulence strategies

Author keywords

[No Author keywords available]

Indexed keywords

BETA DEFENSIN; INTERFERON REGULATORY FACTOR 3; LIPID A; MYELOID DIFFERENTIATION FACTOR 88; STRESS ACTIVATED PROTEIN KINASE; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 3; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 5; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6;

EID: 84875808989     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2012.11.004     Document Type: Review
Times cited : (18)

References (70)
  • 1
    • 77951260924 scopus 로고    scopus 로고
    • The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors
    • Kawai T., Akira S. The role of pattern-recognition receptors in innate immunity: update on Toll-like receptors. Nat Immunol 2010, 11:373-384.
    • (2010) Nat Immunol , vol.11 , pp. 373-384
    • Kawai, T.1    Akira, S.2
  • 2
    • 74549167783 scopus 로고    scopus 로고
    • Regulation of adaptive immunity by the innate immune system
    • Iwasaki A., Medzhitov R. Regulation of adaptive immunity by the innate immune system. Science 2010, 327:291-295.
    • (2010) Science , vol.327 , pp. 291-295
    • Iwasaki, A.1    Medzhitov, R.2
  • 6
    • 33748455338 scopus 로고    scopus 로고
    • Type I interferons in host defense
    • Stetson D.B., Medzhitov R. Type I interferons in host defense. Immunity 2006, 25:373-381.
    • (2006) Immunity , vol.25 , pp. 373-381
    • Stetson, D.B.1    Medzhitov, R.2
  • 7
    • 0030300136 scopus 로고    scopus 로고
    • CD80, CD86 and CD40 provide accessory signals in a multiple-step T-cell activation model
    • Van Gool S.W., Vandenberghe P., de Boer M., Ceuppens J.L. CD80, CD86 and CD40 provide accessory signals in a multiple-step T-cell activation model. Immunol Rev 1996, 153:47-83.
    • (1996) Immunol Rev , vol.153 , pp. 47-83
    • Van Gool, S.W.1    Vandenberghe, P.2    de Boer, M.3    Ceuppens, J.L.4
  • 8
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes: complexity in action
    • Underhill D.M., Ozinsky A. Phagocytosis of microbes: complexity in action. Annu Rev Immunol 2002, 20:825-852.
    • (2002) Annu Rev Immunol , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 9
    • 1542406446 scopus 로고    scopus 로고
    • NOX enzymes and the biology of reactive oxygen
    • Lambeth J.D. NOX enzymes and the biology of reactive oxygen. Nat Rev Immunol 2004, 4:181-189.
    • (2004) Nat Rev Immunol , vol.4 , pp. 181-189
    • Lambeth, J.D.1
  • 11
    • 2342525996 scopus 로고    scopus 로고
    • Regulation of phagosome maturation by signals from toll-like receptors
    • Blander J.M., Medzhitov R. Regulation of phagosome maturation by signals from toll-like receptors. Science 2004, 304:1014-1018.
    • (2004) Science , vol.304 , pp. 1014-1018
    • Blander, J.M.1    Medzhitov, R.2
  • 13
    • 33645734929 scopus 로고    scopus 로고
    • Toll-dependent selection of microbial antigens for presentation by dendritic cells
    • Blander J.M., Medzhitov R. Toll-dependent selection of microbial antigens for presentation by dendritic cells. Nature 2006, 440:808-812.
    • (2006) Nature , vol.440 , pp. 808-812
    • Blander, J.M.1    Medzhitov, R.2
  • 14
    • 0037470438 scopus 로고    scopus 로고
    • Activation of lysosomal function during dendritic cell maturation
    • Trombetta E.S., Ebersold M., Garrett W., Pypaert M., Mellman I. Activation of lysosomal function during dendritic cell maturation. Science 2003, 299:1400-1403.
    • (2003) Science , vol.299 , pp. 1400-1403
    • Trombetta, E.S.1    Ebersold, M.2    Garrett, W.3    Pypaert, M.4    Mellman, I.5
  • 15
    • 33644648533 scopus 로고    scopus 로고
    • Expression of CRAMP via PGN-TLR-2 and of alpha-defensin-3 via CpG-ODN-TLR-9 in corneal fibroblasts
    • Rodriguez-Martinez S., Cancino-Diaz M.E., Cancino-Diaz J.C. Expression of CRAMP via PGN-TLR-2 and of alpha-defensin-3 via CpG-ODN-TLR-9 in corneal fibroblasts. Br J Ophthalmol 2006, 90:378-382.
    • (2006) Br J Ophthalmol , vol.90 , pp. 378-382
    • Rodriguez-Martinez, S.1    Cancino-Diaz, M.E.2    Cancino-Diaz, J.C.3
  • 16
    • 79952106615 scopus 로고    scopus 로고
    • Toll-like receptor activation modulates antimicrobial peptide expression by ocular surface cells
    • Redfern R.L., Reins R.Y., McDermott A.M. Toll-like receptor activation modulates antimicrobial peptide expression by ocular surface cells. Exp Eye Res 2011, 92:209-220.
    • (2011) Exp Eye Res , vol.92 , pp. 209-220
    • Redfern, R.L.1    Reins, R.Y.2    McDermott, A.M.3
  • 17
    • 0034641738 scopus 로고    scopus 로고
    • Toll-related receptors and the control of antimicrobial peptide expression in Drosophila
    • Tauszig S., Jouanguy E., Hoffmann J.A., Imler J.L. Toll-related receptors and the control of antimicrobial peptide expression in Drosophila. Proc Natl Acad Sci U S A 2000, 97:10520-10525.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10520-10525
    • Tauszig, S.1    Jouanguy, E.2    Hoffmann, J.A.3    Imler, J.L.4
  • 18
    • 0033783756 scopus 로고    scopus 로고
    • Bacterial inhibition of phagocytosis
    • Ernst J.D. Bacterial inhibition of phagocytosis. Cell Microbiol 2000, 2:379-386.
    • (2000) Cell Microbiol , vol.2 , pp. 379-386
    • Ernst, J.D.1
  • 19
    • 0029073803 scopus 로고
    • Role of Yops in inhibition of phagocytosis and killing of opsonized Yersinia enterocolitica by human granulocytes
    • Visser L.G., Annema A., van Furth R. Role of Yops in inhibition of phagocytosis and killing of opsonized Yersinia enterocolitica by human granulocytes. Infect Immun 1995, 63:2570-2575.
    • (1995) Infect Immun , vol.63 , pp. 2570-2575
    • Visser, L.G.1    Annema, A.2    van Furth, R.3
  • 20
    • 0023711836 scopus 로고
    • Inhibition of phagocytosis in Yersinia pseudotuberculosis: a virulence plasmid-encoded ability involving the Yop2b protein
    • Rosqvist R., Bolin I., Wolf-Watz H. Inhibition of phagocytosis in Yersinia pseudotuberculosis: a virulence plasmid-encoded ability involving the Yop2b protein. Infect Immun 1988, 56:2139-2143.
    • (1988) Infect Immun , vol.56 , pp. 2139-2143
    • Rosqvist, R.1    Bolin, I.2    Wolf-Watz, H.3
  • 21
    • 0033973827 scopus 로고    scopus 로고
    • Bacterial replication in the host cell cytosol
    • Goebel W., Kuhn M. Bacterial replication in the host cell cytosol. Curr Opin Microbiol 2000, 3:49-53.
    • (2000) Curr Opin Microbiol , vol.3 , pp. 49-53
    • Goebel, W.1    Kuhn, M.2
  • 25
    • 0035889228 scopus 로고    scopus 로고
    • Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes
    • Kawai T., Takeuchi O., Fujita T., Inoue J., Muhlradt P.F., Sato S., Hoshino K., Akira S. Lipopolysaccharide stimulates the MyD88-independent pathway and results in activation of IFN-regulatory factor 3 and the expression of a subset of lipopolysaccharide-inducible genes. J Immunol 2001, 167:5887-5894.
    • (2001) J Immunol , vol.167 , pp. 5887-5894
    • Kawai, T.1    Takeuchi, O.2    Fujita, T.3    Inoue, J.4    Muhlradt, P.F.5    Sato, S.6    Hoshino, K.7    Akira, S.8
  • 26
    • 0036318851 scopus 로고    scopus 로고
    • Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments
    • Ahmad-Nejad P., Hacker H., Rutz M., Bauer S., Vabulas R.M., Wagner H. Bacterial CpG-DNA and lipopolysaccharides activate Toll-like receptors at distinct cellular compartments. Eur J Immunol 2002, 32:1958-1968.
    • (2002) Eur J Immunol , vol.32 , pp. 1958-1968
    • Ahmad-Nejad, P.1    Hacker, H.2    Rutz, M.3    Bauer, S.4    Vabulas, R.M.5    Wagner, H.6
  • 27
    • 0037852065 scopus 로고    scopus 로고
    • Stimulation of Toll-like receptor 4 by lipopolysaccharide during cellular invasion by live Salmonella typhimurium is a critical but not exclusive event leading to macrophage responses
    • Royle M.C., Tötemeyer S., Alldridge L.C., Maskell D.J., Bryant C.E. Stimulation of Toll-like receptor 4 by lipopolysaccharide during cellular invasion by live Salmonella typhimurium is a critical but not exclusive event leading to macrophage responses. J Immunol 2003, 170:5445-5454.
    • (2003) J Immunol , vol.170 , pp. 5445-5454
    • Royle, M.C.1    Tötemeyer, S.2    Alldridge, L.C.3    Maskell, D.J.4    Bryant, C.E.5
  • 30
    • 3042546218 scopus 로고    scopus 로고
    • Flagella and chemotaxis are required for efficient induction of Salmonella enterica serovar Typhimurium colitis in streptomycin-pretreated mice
    • Stecher B., Hapfelmeier S., Müller C., Kremer M., Stallmach T., Hardt W-D. Flagella and chemotaxis are required for efficient induction of Salmonella enterica serovar Typhimurium colitis in streptomycin-pretreated mice. Infect Immun 2004, 72:4138-4150.
    • (2004) Infect Immun , vol.72 , pp. 4138-4150
    • Stecher, B.1    Hapfelmeier, S.2    Müller, C.3    Kremer, M.4    Stallmach, T.5    Hardt, W.-D.6
  • 31
    • 0030984298 scopus 로고    scopus 로고
    • Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ
    • Guo L., Lim K.B., Gunn J.S., Bainbridge B., Darveau R.P., Hackett M., Miller S.I. Regulation of lipid A modifications by Salmonella typhimurium virulence genes phoP-phoQ. Science 1997, 276:250-253.
    • (1997) Science , vol.276 , pp. 250-253
    • Guo, L.1    Lim, K.B.2    Gunn, J.S.3    Bainbridge, B.4    Darveau, R.P.5    Hackett, M.6    Miller, S.I.7
  • 32
    • 0032538292 scopus 로고    scopus 로고
    • Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides
    • Guo L., Lim K.B., Poduje C.M., Daniel M., Gunn J.S., Hackett M., Miller S.I. Lipid A acylation and bacterial resistance against vertebrate antimicrobial peptides. Cell 1998, 95:189-198.
    • (1998) Cell , vol.95 , pp. 189-198
    • Guo, L.1    Lim, K.B.2    Poduje, C.M.3    Daniel, M.4    Gunn, J.S.5    Hackett, M.6    Miller, S.I.7
  • 33
    • 10744224023 scopus 로고    scopus 로고
    • Relationship between structures and biological activities of mycoplasmal diacylated lipopeptides and their recognition by toll-like receptors 2 and 6
    • Okusawa T., Fujita M., Nakamura J., Into T., Yasuda M., Yoshimura A., Hara Y., Hasebe A., Golenbock D.T., Morita M., et al. Relationship between structures and biological activities of mycoplasmal diacylated lipopeptides and their recognition by toll-like receptors 2 and 6. Infect Immun 2004, 72:1657-1665.
    • (2004) Infect Immun , vol.72 , pp. 1657-1665
    • Okusawa, T.1    Fujita, M.2    Nakamura, J.3    Into, T.4    Yasuda, M.5    Yoshimura, A.6    Hara, Y.7    Hasebe, A.8    Golenbock, D.T.9    Morita, M.10
  • 34
    • 25444476973 scopus 로고    scopus 로고
    • SseJ deacylase activity by Salmonella enterica serovar Typhimurium promotes virulence in mice
    • Ohlson M.B., Fluhr K., Birmingham C.L., Brumell J.H., Miller S.I. SseJ deacylase activity by Salmonella enterica serovar Typhimurium promotes virulence in mice. Infect Immun 2005, 73:6249-6259.
    • (2005) Infect Immun , vol.73 , pp. 6249-6259
    • Ohlson, M.B.1    Fluhr, K.2    Birmingham, C.L.3    Brumell, J.H.4    Miller, S.I.5
  • 35
    • 23644461233 scopus 로고    scopus 로고
    • Remodeling of Helicobacter pylori lipopolysaccharide
    • Tran A.X., Stead C.M., Trent M.S. Remodeling of Helicobacter pylori lipopolysaccharide. J Endotoxin Res 2005, 11:161-166.
    • (2005) J Endotoxin Res , vol.11 , pp. 161-166
    • Tran, A.X.1    Stead, C.M.2    Trent, M.S.3
  • 36
    • 54049094370 scopus 로고    scopus 로고
    • Yersinia pestis evades TLR4-dependent induction of IL-12(p40)2 by dendritic cells and subsequent cell migration
    • Robinson R.T., Khader S.A., Locksley R.M., Lien E., Smiley S.T., Cooper A.M. Yersinia pestis evades TLR4-dependent induction of IL-12(p40)2 by dendritic cells and subsequent cell migration. J Immunol 2008, 181:5560-5567.
    • (2008) J Immunol , vol.181 , pp. 5560-5567
    • Robinson, R.T.1    Khader, S.A.2    Locksley, R.M.3    Lien, E.4    Smiley, S.T.5    Cooper, A.M.6
  • 37
    • 2442544458 scopus 로고    scopus 로고
    • 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4
    • Kawasaki K., Ernst R.K., Miller S.I. 3-O-deacylation of lipid A by PagL, a PhoP/PhoQ-regulated deacylase of Salmonella typhimurium, modulates signaling through Toll-like receptor 4. J Biol Chem 2004, 279:20044-20048.
    • (2004) J Biol Chem , vol.279 , pp. 20044-20048
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 39
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway C.A. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 1989, 54(Pt 1):1-13.
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PT 1 , pp. 1-13
    • Janeway, C.A.1
  • 40
    • 45549093413 scopus 로고    scopus 로고
    • In vitro signaling by MAPK and NFkappaB pathways inhibited by Yersinia YopJ
    • Mukherjee S., Orth K. In vitro signaling by MAPK and NFkappaB pathways inhibited by Yersinia YopJ. Methods Enzymol 2008, 438:343-353.
    • (2008) Methods Enzymol , vol.438 , pp. 343-353
    • Mukherjee, S.1    Orth, K.2
  • 41
    • 34848831208 scopus 로고    scopus 로고
    • YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction
    • Sweet C.R., Conlon J., Golenbock D.T., Goguen J., Silverman N. YopJ targets TRAF proteins to inhibit TLR-mediated NF-kappaB, MAPK and IRF3 signal transduction. Cell Microbiol 2007, 9:2700-2715.
    • (2007) Cell Microbiol , vol.9 , pp. 2700-2715
    • Sweet, C.R.1    Conlon, J.2    Golenbock, D.T.3    Goguen, J.4    Silverman, N.5
  • 42
    • 0037462764 scopus 로고    scopus 로고
    • Yersinia effector YopJ inhibits yeast MAPK signaling pathways by an evolutionarily conserved mechanism
    • Yoon S., Liu Z., Eyobo Y., Orth K. Yersinia effector YopJ inhibits yeast MAPK signaling pathways by an evolutionarily conserved mechanism. J Biol Chem 2003, 278:2131-2135.
    • (2003) J Biol Chem , vol.278 , pp. 2131-2135
    • Yoon, S.1    Liu, Z.2    Eyobo, Y.3    Orth, K.4
  • 43
    • 79953046297 scopus 로고    scopus 로고
    • Proteasome-independent degradation of canonical NFkappaB complex components by the NleC protein of pathogenic Escherichia coli
    • Muhlen S., Ruchaud-Sparagano M.H., Kenny B. Proteasome-independent degradation of canonical NFkappaB complex components by the NleC protein of pathogenic Escherichia coli. J Biol Chem 2011, 286:5100-5107.
    • (2011) J Biol Chem , vol.286 , pp. 5100-5107
    • Muhlen, S.1    Ruchaud-Sparagano, M.H.2    Kenny, B.3
  • 44
    • 79953057642 scopus 로고    scopus 로고
    • A type III effector protease NleC from enteropathogenic Escherichia coli targets NF-kappaB for degradation
    • Pearson J.S., Riedmaier P., Marches O., Frankel G., Hartland E.L. A type III effector protease NleC from enteropathogenic Escherichia coli targets NF-kappaB for degradation. Mol Microbiol 2011, 80:219-230.
    • (2011) Mol Microbiol , vol.80 , pp. 219-230
    • Pearson, J.S.1    Riedmaier, P.2    Marches, O.3    Frankel, G.4    Hartland, E.L.5
  • 45
    • 80052305157 scopus 로고    scopus 로고
    • Attaching and effacing bacterial effector NleC suppresses epithelial inflammatory responses by inhibiting NF-kappaB and p38 mitogen-activated protein kinase activation
    • Sham H.P., Shames S.R., Croxen M.A., Ma C., Chan J.M., Khan M.A., Wickham M.E., Deng W., Finlay B.B., Vallance B.A. Attaching and effacing bacterial effector NleC suppresses epithelial inflammatory responses by inhibiting NF-kappaB and p38 mitogen-activated protein kinase activation. Infect Immun 2011, 79:3552-3562.
    • (2011) Infect Immun , vol.79 , pp. 3552-3562
    • Sham, H.P.1    Shames, S.R.2    Croxen, M.A.3    Ma, C.4    Chan, J.M.5    Khan, M.A.6    Wickham, M.E.7    Deng, W.8    Finlay, B.B.9    Vallance, B.A.10
  • 46
    • 78651257387 scopus 로고    scopus 로고
    • NleC, a type III secretion protease, compromises NF-kappaB activation by targeting p65/RelA
    • Yen H., Ooka T., Iguchi A., Hayashi T., Sugimoto N., Tobe T. NleC, a type III secretion protease, compromises NF-kappaB activation by targeting p65/RelA. PLoS Pathog 2010, 6:e1001231.
    • (2010) PLoS Pathog , vol.6
    • Yen, H.1    Ooka, T.2    Iguchi, A.3    Hayashi, T.4    Sugimoto, N.5    Tobe, T.6
  • 47
    • 77955109451 scopus 로고    scopus 로고
    • A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response
    • 66-73, sup 1-9
    • Ashida H., Kim M., Schmidt-Supprian M., Ma A., Ogawa M., Sasakawa C. A bacterial E3 ubiquitin ligase IpaH9.8 targets NEMO/IKKgamma to dampen the host NF-kappaB-mediated inflammatory response. Nat Cell Biol 2010, 12. 66-73, sup 1-9.
    • (2010) Nat Cell Biol , vol.12
    • Ashida, H.1    Kim, M.2    Schmidt-Supprian, M.3    Ma, A.4    Ogawa, M.5    Sasakawa, C.6
  • 48
    • 25444461419 scopus 로고    scopus 로고
    • The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes
    • Kim D.W., Lenzen G., Page A.L., Legrain P., Sansonetti P.J., Parsot C. The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Proc Natl Acad Sci U S A 2005, 102:14046-14051.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14046-14051
    • Kim, D.W.1    Lenzen, G.2    Page, A.L.3    Legrain, P.4    Sansonetti, P.J.5    Parsot, C.6
  • 49
    • 84856785397 scopus 로고    scopus 로고
    • Manipulation of kinase signaling by bacterial pathogens
    • Krachler A.M., Woolery A.R., Orth K. Manipulation of kinase signaling by bacterial pathogens. J Cell Biol 2011, 195:1083-1092.
    • (2011) J Cell Biol , vol.195 , pp. 1083-1092
    • Krachler, A.M.1    Woolery, A.R.2    Orth, K.3
  • 50
    • 65649148280 scopus 로고    scopus 로고
    • Brucella TIR domain-containing protein mimics properties of the toll-like receptor adaptor protein TIRAP
    • Radhakrishnan G.K., Yu Q., Harms J.S., Splitter G.A. Brucella TIR domain-containing protein mimics properties of the toll-like receptor adaptor protein TIRAP. J Biol Chem 2009, 284:9892-9898.
    • (2009) J Biol Chem , vol.284 , pp. 9892-9898
    • Radhakrishnan, G.K.1    Yu, Q.2    Harms, J.S.3    Splitter, G.A.4
  • 51
    • 29644438009 scopus 로고    scopus 로고
    • Identification and characterization of a novel bacterial virulence factor that shares homology with mammalian Toll/interleukin-1 receptor family proteins
    • Newman R.M., Salunkhe P., Godzik A., Reed J.C. Identification and characterization of a novel bacterial virulence factor that shares homology with mammalian Toll/interleukin-1 receptor family proteins. Infect Immun 2006, 74:594-601.
    • (2006) Infect Immun , vol.74 , pp. 594-601
    • Newman, R.M.1    Salunkhe, P.2    Godzik, A.3    Reed, J.C.4
  • 52
    • 68849085894 scopus 로고    scopus 로고
    • A cell biological view of Toll-like receptor function: regulation through compartmentalization
    • Barton G.M., Kagan J.C. A cell biological view of Toll-like receptor function: regulation through compartmentalization. Nat Rev Immunol 2009, 9:535-542.
    • (2009) Nat Rev Immunol , vol.9 , pp. 535-542
    • Barton, G.M.1    Kagan, J.C.2
  • 53
    • 40949134086 scopus 로고    scopus 로고
    • TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta
    • Kagan J.C., Su T., Horng T., Chow A., Akira S., Medzhitov R. TRAM couples endocytosis of Toll-like receptor 4 to the induction of interferon-beta. Nat Immunol 2008, 9:361-368.
    • (2008) Nat Immunol , vol.9 , pp. 361-368
    • Kagan, J.C.1    Su, T.2    Horng, T.3    Chow, A.4    Akira, S.5    Medzhitov, R.6
  • 54
    • 16244399792 scopus 로고    scopus 로고
    • Human fibrinogen bound to Streptococcus pyogenes M protein inhibits complement deposition via the classical pathway
    • Carlsson F., Sandin C., Lindahl G. Human fibrinogen bound to Streptococcus pyogenes M protein inhibits complement deposition via the classical pathway. Mol Microbiol 2005, 56:28-39.
    • (2005) Mol Microbiol , vol.56 , pp. 28-39
    • Carlsson, F.1    Sandin, C.2    Lindahl, G.3
  • 55
    • 77958121661 scopus 로고    scopus 로고
    • Contribution of coagulases towards Staphylococcus aureus disease and protective immunity
    • Cheng A.G., McAdow M., Kim H.K., Bae T., Missiakas D.M., Schneewind O. Contribution of coagulases towards Staphylococcus aureus disease and protective immunity. PLoS Pathog 2010, 6:e1001036.
    • (2010) PLoS Pathog , vol.6
    • Cheng, A.G.1    McAdow, M.2    Kim, H.K.3    Bae, T.4    Missiakas, D.M.5    Schneewind, O.6
  • 56
    • 64749104915 scopus 로고    scopus 로고
    • Life on the inside: the intracellular lifestyle of cytosolic bacteria
    • Ray K., Marteyn B., Sansonetti P.J., Tang C.M. Life on the inside: the intracellular lifestyle of cytosolic bacteria. Nat Rev Microbiol 2009, 7:333-340.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 333-340
    • Ray, K.1    Marteyn, B.2    Sansonetti, P.J.3    Tang, C.M.4
  • 58
    • 0037305123 scopus 로고    scopus 로고
    • Restricted fusion of Chlamydia trachomatis vesicles with endocytic compartments during the initial stages of infection
    • Scidmore M.A., Fischer E.R., Hackstadt T. Restricted fusion of Chlamydia trachomatis vesicles with endocytic compartments during the initial stages of infection. Infect Immun 2003, 71:973-984.
    • (2003) Infect Immun , vol.71 , pp. 973-984
    • Scidmore, M.A.1    Fischer, E.R.2    Hackstadt, T.3
  • 59
    • 0016742008 scopus 로고
    • Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival
    • Armstrong J.A., Hart P.D. Phagosome-lysosome interactions in cultured macrophages infected with virulent tubercle bacilli. Reversal of the usual nonfusion pattern and observations on bacterial survival. J Exp Med 1975, 142:1-16.
    • (1975) J Exp Med , vol.142 , pp. 1-16
    • Armstrong, J.A.1    Hart, P.D.2
  • 60
    • 17644362734 scopus 로고    scopus 로고
    • The Brucella abortus Cu, Zn superoxide dismutase is required for optimal resistance to oxidative killing by murine macrophages and wild-type virulence in experimentally infected mice
    • Gee J.M., Valderas M.W., Kovach M.E., Grippe V.K., Robertson G.T., Ng W.L., Richardson J.M., Winkler M.E., Roop R.M. The Brucella abortus Cu, Zn superoxide dismutase is required for optimal resistance to oxidative killing by murine macrophages and wild-type virulence in experimentally infected mice. Infect Immun 2005, 73:2873-2880.
    • (2005) Infect Immun , vol.73 , pp. 2873-2880
    • Gee, J.M.1    Valderas, M.W.2    Kovach, M.E.3    Grippe, V.K.4    Robertson, G.T.5    Ng, W.L.6    Richardson, J.M.7    Winkler, M.E.8    Roop, R.M.9
  • 61
    • 51849101917 scopus 로고    scopus 로고
    • Intracellular survival of Staphylococcus aureus: correlating production of catalase and superoxide dismutase with levels of inflammatory cytokines
    • Das D., Saha S.S., Bishayi B. Intracellular survival of Staphylococcus aureus: correlating production of catalase and superoxide dismutase with levels of inflammatory cytokines. Inflamm Res 2008, 57:340-349.
    • (2008) Inflamm Res , vol.57 , pp. 340-349
    • Das, D.1    Saha, S.S.2    Bishayi, B.3
  • 63
    • 13444259757 scopus 로고    scopus 로고
    • Mig-14 is an inner membrane-associated protein that promotes Salmonella typhimurium resistance to CRAMP, survival within activated macrophages and persistent infection
    • Brodsky I.E., Ghori N., Falkow S., Monack D. Mig-14 is an inner membrane-associated protein that promotes Salmonella typhimurium resistance to CRAMP, survival within activated macrophages and persistent infection. Mol Microbiol 2005, 55:954-972.
    • (2005) Mol Microbiol , vol.55 , pp. 954-972
    • Brodsky, I.E.1    Ghori, N.2    Falkow, S.3    Monack, D.4
  • 65
    • 0029809576 scopus 로고    scopus 로고
    • PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance
    • Gunn J.S., Miller S.I. PhoP-PhoQ activates transcription of pmrAB, encoding a two-component regulatory system involved in Salmonella typhimurium antimicrobial peptide resistance. J Bacteriol 1996, 178:6857-6864.
    • (1996) J Bacteriol , vol.178 , pp. 6857-6864
    • Gunn, J.S.1    Miller, S.I.2
  • 66
    • 38849124779 scopus 로고    scopus 로고
    • The Salmonellae PhoQ sensor: mechanisms of detection of phagosome signals
    • Prost L., Miller S. The Salmonellae PhoQ sensor: mechanisms of detection of phagosome signals. Cell Microbiol 2008, 10:576-582.
    • (2008) Cell Microbiol , vol.10 , pp. 576-582
    • Prost, L.1    Miller, S.2
  • 69
    • 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 2003, 5:501-511.
    • (2003) Cell Microbiol , vol.5 , pp. 501-511
    • Waterman, S.R.1    Holden, D.W.2
  • 70
    • 0030031402 scopus 로고    scopus 로고
    • The lpf fimbrial operon mediates adhesion of Salmonella typhimurium to murine Peyer's patches
    • Bäumler A.J., Tsolis R.M., Heffron F. The lpf fimbrial operon mediates adhesion of Salmonella typhimurium to murine Peyer's patches. Proc Natl Acad Sci U S A 1996, 93:279-283.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 279-283
    • Bäumler, A.J.1    Tsolis, R.M.2    Heffron, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.