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Volumn 14, Issue 19, 2004, Pages

Evasive maneuvers by secreted bacterial proteins to avoid innate immune responses

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DEFENSIN; BACTERIAL PROTEIN; CELL SURFACE RECEPTOR; MEMBRANE PROTEIN; TOLL LIKE RECEPTOR;

EID: 4644242673     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2004.09.043     Document Type: Review
Times cited : (47)

References (115)
  • 3
    • 0038557053 scopus 로고    scopus 로고
    • Phagocyte sabotage: Disruption of macrophage signalling by bacterial pathogens
    • Rosenberger C.M., Finlay B.B. Phagocyte sabotage: disruption of macrophage signalling by bacterial pathogens. Nat. Rev. Mol. Cell Biol. 4:2003;385-396
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 385-396
    • Rosenberger, C.M.1    Finlay, B.B.2
  • 4
    • 0036851306 scopus 로고    scopus 로고
    • Bacterial strategies for overcoming host innate and adaptive immune responses
    • Hornef M.W., Wick M.J., Rhen M., Normark S. Bacterial strategies for overcoming host innate and adaptive immune responses. Nat. Immunol. 3:2002;1033-1040
    • (2002) Nat. Immunol. , vol.3 , pp. 1033-1040
    • Hornef, M.W.1    Wick, M.J.2    Rhen, M.3    Normark, S.4
  • 5
    • 3142544236 scopus 로고    scopus 로고
    • Frontal and stealth attack strategies in microbial pathogenesis
    • Merrell D.S., Falkow S. Frontal and stealth attack strategies in microbial pathogenesis. Nature. 430:2004;250-256
    • (2004) Nature , vol.430 , pp. 250-256
    • Merrell, D.S.1    Falkow, S.2
  • 6
    • 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. 54:2000;735-774
    • (2000) Annu. Rev. Microbiol. , vol.54 , pp. 735-774
    • Cornelis, G.R.1    Van Gijsegem, F.2
  • 7
    • 0031864184 scopus 로고    scopus 로고
    • Type III protein secretion systems in bacterial pathogens of animals and plants
    • Hueck C.J. Type III protein secretion systems in bacterial pathogens of animals and plants. Microbiol. Mol. Biol. Rev. 62:1998;379-433
    • (1998) Microbiol. Mol. Biol. Rev. , vol.62 , pp. 379-433
    • Hueck, C.J.1
  • 8
    • 1842456892 scopus 로고    scopus 로고
    • The versatile bacterial type IV secretion systems
    • Cascales E., Christie P.J. The versatile bacterial type IV secretion systems. Nat. Rev. Microbiol. 1:2003;137-149
    • (2003) Nat. Rev. Microbiol. , vol.1 , pp. 137-149
    • Cascales, E.1    Christie, P.J.2
  • 9
    • 0038001470 scopus 로고    scopus 로고
    • Show me the substrates: Modulation of host cell function by type IV secretion systems
    • Nagai H., Roy C.R. Show me the substrates: modulation of host cell function by type IV secretion systems. Cell. Microbiol. 5:2003;373-383
    • (2003) Cell. Microbiol. , vol.5 , pp. 373-383
    • Nagai, H.1    Roy, C.R.2
  • 10
    • 0032996225 scopus 로고    scopus 로고
    • Biochemistry of type IV secretion
    • Burns D.L. Biochemistry of type IV secretion. Curr. Opin. Microbiol. 2:1999;25-29
    • (1999) Curr. Opin. Microbiol. , vol.2 , pp. 25-29
    • Burns, D.L.1
  • 11
    • 0035019730 scopus 로고    scopus 로고
    • Type II secretion and pathogenesis
    • Sandkvist M. Type II secretion and pathogenesis. Infect. Immun. 69:2001;3523-3535
    • (2001) Infect. Immun. , vol.69 , pp. 3523-3535
    • Sandkvist, M.1
  • 13
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel M. Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J. Mol. Biol. 279:1998;485-499
    • (1998) J. Mol. Biol. , vol.279 , pp. 485-499
    • Russel, M.1
  • 14
    • 0242478028 scopus 로고    scopus 로고
    • Protein secretion by Gram-negative bacterial ABC exporters - A review
    • Binet R., Letoffe S., Ghigo J.M., Delepelaire P., Wandersman C. Protein secretion by Gram-negative bacterial ABC exporters - a review. Gene. 192:1997;7-11
    • (1997) Gene , vol.192 , pp. 7-11
    • Binet, R.1    Letoffe, S.2    Ghigo, J.M.3    Delepelaire, P.4    Wandersman, C.5
  • 15
    • 0346024087 scopus 로고    scopus 로고
    • Phagocytosis, innate immunity, and host-pathogen specificity
    • Henneke P., Golenbock D.T. Phagocytosis, innate immunity, and host-pathogen specificity. J. Exp. Med. 199:2004;1-4
    • (2004) J. Exp. Med. , vol.199 , pp. 1-4
    • Henneke, P.1    Golenbock, D.T.2
  • 16
    • 0037184995 scopus 로고    scopus 로고
    • Pattern recognition receptors: Doubling up for the innate immune response
    • Gordon S. Pattern recognition receptors: doubling up for the innate immune response. Cell. 111:2002;927-930
    • (2002) Cell , vol.111 , pp. 927-930
    • Gordon, S.1
  • 17
    • 0035868908 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli mediates antiphagocytosis through the inhibition of PI 3-kinase-dependent pathways
    • Celli J., Olivier M., Finlay B.B. Enteropathogenic Escherichia coli mediates antiphagocytosis through the inhibition of PI 3-kinase-dependent pathways. EMBO J. 20:2001;1245-1258
    • (2001) EMBO J. , vol.20 , pp. 1245-1258
    • Celli, J.1    Olivier, M.2    Finlay, B.B.3
  • 18
    • 0033579479 scopus 로고    scopus 로고
    • The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases
    • Goehring U.M., Schmidt G., Pederson K.J., Aktories K., Barbieri J.T. The N-terminal domain of Pseudomonas aeruginosa exoenzyme S is a GTPase-activating protein for Rho GTPases. J. Biol. Chem. 274:1999;36369-36372
    • (1999) J. Biol. Chem. , vol.274 , pp. 36369-36372
    • Goehring, U.M.1    Schmidt, G.2    Pederson, K.J.3    Aktories, K.4    Barbieri, J.T.5
  • 19
    • 0033961448 scopus 로고    scopus 로고
    • ExoT of cytotoxic Pseudomonas aeruginosa prevents uptake by corneal epithelial cells
    • Cowell B.A., Chen D.Y., Frank D.W., Vallis A.J., Fleiszig S.M. ExoT of cytotoxic Pseudomonas aeruginosa prevents uptake by corneal epithelial cells. Infect. Immun. 68:2000;403-406
    • (2000) Infect. Immun. , vol.68 , pp. 403-406
    • Cowell, B.A.1    Chen, D.Y.2    Frank, D.W.3    Vallis, A.J.4    Fleiszig, S.M.5
  • 20
    • 0034444645 scopus 로고    scopus 로고
    • The arginine finger domain of ExoT contributes to actin cytoskeleton disruption and inhibition of internalization of Pseudomonas aeruginosa by epithelial cells and macrophages
    • Garrity-Ryan L., Kazmierczak B., Kowal R., Comolli J., Hauser A., Engel J.N. The arginine finger domain of ExoT contributes to actin cytoskeleton disruption and inhibition of internalization of Pseudomonas aeruginosa by epithelial cells and macrophages. Infect. Immun. 68:2000;7100-7113
    • (2000) Infect. Immun. , vol.68 , pp. 7100-7113
    • Garrity-Ryan, L.1    Kazmierczak, B.2    Kowal, R.3    Comolli, J.4    Hauser, A.5    Engel, J.N.6
  • 21
    • 0030978909 scopus 로고    scopus 로고
    • The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions
    • Persson C., Carballeira N., Wolf-Watz H., Fallman M. The PTPase YopH inhibits uptake of Yersinia, tyrosine phosphorylation of p130Cas and FAK, and the associated accumulation of these proteins in peripheral focal adhesions. EMBO J. 16:1997;2307-2318
    • (1997) EMBO J. , vol.16 , pp. 2307-2318
    • Persson, C.1    Carballeira, N.2    Wolf-Watz, H.3    Fallman, M.4
  • 23
    • 0037205231 scopus 로고    scopus 로고
    • A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis
    • Shao F., Merritt P.M., Bao Z., Innes R.W., Dixon J.E. A Yersinia effector and a Pseudomonas avirulence protein define a family of cysteine proteases functioning in bacterial pathogenesis. Cell. 109:2002;575-588
    • (2002) Cell , vol.109 , pp. 575-588
    • Shao, F.1    Merritt, P.M.2    Bao, Z.3    Innes, R.W.4    Dixon, J.E.5
  • 25
    • 0037452070 scopus 로고    scopus 로고
    • Microbial pathogenesis and cytoskeletal function
    • Gruenheid S., Finlay B.B. Microbial pathogenesis and cytoskeletal function. Nature. 422:2003;775-781
    • (2003) Nature , vol.422 , pp. 775-781
    • Gruenheid, S.1    Finlay, B.B.2
  • 26
    • 1842430006 scopus 로고    scopus 로고
    • Bacterial invasion: The paradigms of enteroinvasive pathogens
    • Cossart P., Sansonetti P.J. Bacterial invasion: the paradigms of enteroinvasive pathogens. Science. 304:2004;242-248
    • (2004) Science , vol.304 , pp. 242-248
    • Cossart, P.1    Sansonetti, P.J.2
  • 27
    • 0041884953 scopus 로고    scopus 로고
    • Phagosome maturation: A few bugs in the system
    • Scott C.C., Botelho R.J., Grinstein S. Phagosome maturation: a few bugs in the system. J. Membr. Biol. 193:2003;137-152
    • (2003) J. Membr. Biol. , vol.193 , pp. 137-152
    • Scott, C.C.1    Botelho, R.J.2    Grinstein, S.3
  • 28
    • 0030792813 scopus 로고    scopus 로고
    • Safe haven: The cell biology of nonfusogenic pathogen vacuoles
    • Sinai A.P., Joiner K.A. Safe haven: the cell biology of nonfusogenic pathogen vacuoles. Annu. Rev. Microbiol. 51:1997;415-462
    • (1997) Annu. Rev. Microbiol. , vol.51 , pp. 415-462
    • Sinai, A.P.1    Joiner, K.A.2
  • 29
    • 2442537071 scopus 로고    scopus 로고
    • Legionella subvert the functions of rab1 and sec22b to create a replicative organelle
    • Kagan J.C., Stein M.P., Pypaert M., Roy C.R. Legionella subvert the functions of rab1 and sec22b to create a replicative organelle. J. Exp. Med. 199:2004;1201-1211
    • (2004) J. Exp. Med. , vol.199 , pp. 1201-1211
    • Kagan, J.C.1    Stein, M.P.2    Pypaert, M.3    Roy, C.R.4
  • 30
    • 0036903907 scopus 로고    scopus 로고
    • Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites
    • Kagan J.C., Roy C.R. Legionella phagosomes intercept vesicular traffic from endoplasmic reticulum exit sites. Nat. Cell Biol. 4:2002;945-954
    • (2002) Nat. Cell Biol. , vol.4 , pp. 945-954
    • Kagan, J.C.1    Roy, C.R.2
  • 31
    • 0037169078 scopus 로고    scopus 로고
    • A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes
    • Nagai H., Kagan J.C., Zhu X., Kahn R.A., Roy C.R. A bacterial guanine nucleotide exchange factor activates ARF on Legionella phagosomes. Science. 295:2002;679-682
    • (2002) Science , vol.295 , pp. 679-682
    • Nagai, H.1    Kagan, J.C.2    Zhu, X.3    Kahn, R.A.4    Roy, C.R.5
  • 32
    • 0041920932 scopus 로고    scopus 로고
    • Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum
    • Celli J., de Chastellier C., Franchini D.M., Pizarro-Cerda J., Moreno E., Gorvel J.P. Brucella evades macrophage killing via VirB-dependent sustained interactions with the endoplasmic reticulum. J. Exp. Med. 198:2003;545-556
    • (2003) J. Exp. Med. , vol.198 , pp. 545-556
    • Celli, J.1    De Chastellier, C.2    Franchini, D.M.3    Pizarro-Cerda, J.4    Moreno, E.5    Gorvel, J.P.6
  • 33
    • 0038503985 scopus 로고    scopus 로고
    • Legionella reveal dendritic cell functions that facilitate selection of antigens for MHC class II presentation
    • Neild A.L., Roy C.R. Legionella reveal dendritic cell functions that facilitate selection of antigens for MHC class II presentation. Immunity. 18:2003;813-823
    • (2003) Immunity , vol.18 , pp. 813-823
    • Neild, A.L.1    Roy, C.R.2
  • 35
    • 0141707939 scopus 로고    scopus 로고
    • ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells
    • Guermonprez P., Saveanu L., Kleijmeer M., Davoust J., Van Endert P., Amigorena S. ER-phagosome fusion defines an MHC class I cross-presentation compartment in dendritic cells. Nature. 425:2003;397-402
    • (2003) Nature , vol.425 , pp. 397-402
    • Guermonprez, P.1    Saveanu, L.2    Kleijmeer, M.3    Davoust, J.4    Van Endert, P.5    Amigorena, S.6
  • 38
    • 0142029069 scopus 로고    scopus 로고
    • Survival perspectives from the world's most successful pathogen, Mycobacterium tuberculosis
    • Hingley-Wilson S.M., Sambandamurthy V.K., Jacobs W.R. Jr. Survival perspectives from the world's most successful pathogen, Mycobacterium tuberculosis. Nat. Immunol. 4:2003;949-955
    • (2003) Nat. Immunol. , vol.4 , pp. 949-955
    • Hingley-Wilson, S.M.1    Sambandamurthy, V.K.2    Jacobs Jr., W.R.3
  • 39
    • 0038242875 scopus 로고    scopus 로고
    • Toll-like receptor signaling pathways
    • Barton G.M., Medzhitov R. Toll-like receptor signaling pathways. Science. 300:2003;1524-1525
    • (2003) Science , vol.300 , pp. 1524-1525
    • Barton, G.M.1    Medzhitov, R.2
  • 41
  • 42
    • 0034175930 scopus 로고    scopus 로고
    • The IKK complex: An integrator of all signals that activate NF-kappaB?
    • Israel A. The IKK complex: an integrator of all signals that activate NF-kappaB? Trends Cell Biol. 10:2000;129-133
    • (2000) Trends Cell Biol. , vol.10 , pp. 129-133
    • Israel, A.1
  • 44
    • 0030831210 scopus 로고    scopus 로고
    • A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
    • Medzhitov R., Preston-Hurlburt P., Janeway C.A. Jr. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature. 388:1997;394-397
    • (1997) Nature , vol.388 , pp. 394-397
    • Medzhitov, R.1    Preston-Hurlburt, P.2    Janeway Jr., C.A.3
  • 45
    • 0030595339 scopus 로고    scopus 로고
    • The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults
    • Lemaitre B., Nicolas E., Michaut L., Reichhart J.M., Hoffmann J.A. The dorsoventral regulatory gene cassette spatzle/Toll/cactus controls the potent antifungal response in Drosophila adults. Cell. 86:1996;973-983
    • (1996) Cell , vol.86 , pp. 973-983
    • Lemaitre, B.1    Nicolas, E.2    Michaut, L.3    Reichhart, J.M.4    Hoffmann, J.A.5
  • 47
    • 0036510366 scopus 로고    scopus 로고
    • Negative regulation of toll-like receptor-mediated signaling by Tollip
    • Zhang G., Ghosh S. Negative regulation of toll-like receptor-mediated signaling by Tollip. J. Biol. Chem. 277:2002;7059-7065
    • (2002) J. Biol. Chem. , vol.277 , pp. 7059-7065
    • Zhang, G.1    Ghosh, S.2
  • 50
    • 10744226016 scopus 로고    scopus 로고
    • A common dominant TLR5 stop codon polymorphism abolishes flagellin signaling and is associated with susceptibility to legionnaires' disease
    • Hawn T.R., Verbon A., Lettinga K.D., Zhao L.P., Li S.S., Laws R.J., Skerrett S.J., Beutler B., Schroeder L., Nachman A., et al. A common dominant TLR5 stop codon polymorphism abolishes flagellin signaling and is associated with susceptibility to legionnaires' disease. J. Exp. Med. 198:2003;1563-1572
    • (2003) J. Exp. Med. , vol.198 , pp. 1563-1572
    • Hawn, T.R.1    Verbon, A.2    Lettinga, K.D.3    Zhao, L.P.4    Li, S.S.5    Laws, R.J.6    Skerrett, S.J.7    Beutler, B.8    Schroeder, L.9    Nachman, A.10
  • 51
    • 0043281537 scopus 로고    scopus 로고
    • Distinct mutations in IRAK-4 confer hyporesponsiveness to lipopolysaccharide and interleukin-1 in a patient with recurrent bacterial infections
    • Medvedev A.E., Lentschat A., Kuhns D.B., Blanco J.C., Salkowski C., Zhang S., Arditi M., Gallin J.I., Vogel S.N. Distinct mutations in IRAK-4 confer hyporesponsiveness to lipopolysaccharide and interleukin-1 in a patient with recurrent bacterial infections. J. Exp. Med. 198:2003;521-531
    • (2003) J. Exp. Med. , vol.198 , pp. 521-531
    • Medvedev, A.E.1    Lentschat, A.2    Kuhns, D.B.3    Blanco, J.C.4    Salkowski, C.5    Zhang, S.6    Arditi, M.7    Gallin, J.I.8    Vogel, S.N.9
  • 53
    • 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. 32:2002;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
  • 54
    • 0033592748 scopus 로고    scopus 로고
    • The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens
    • Underhill D.M., Ozinsky A., Hajjar A.M., Stevens A., Wilson C.B., Bassetti M., Aderem A. The Toll-like receptor 2 is recruited to macrophage phagosomes and discriminates between pathogens. Nature. 401:1999;811-815
    • (1999) Nature , vol.401 , pp. 811-815
    • Underhill, D.M.1    Ozinsky, A.2    Hajjar, A.M.3    Stevens, A.4    Wilson, C.B.5    Bassetti, M.6    Aderem, A.7
  • 55
    • 0033584935 scopus 로고    scopus 로고
    • Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa
    • Ernst R.K., Yi E.C., Guo L., Lim K.B., Burns J.L., Hackett M., Miller S.I. Specific lipopolysaccharide found in cystic fibrosis airway Pseudomonas aeruginosa. Science. 286:1999;1561-1565
    • (1999) Science , vol.286 , pp. 1561-1565
    • Ernst, R.K.1    Yi, E.C.2    Guo, L.3    Lim, K.B.4    Burns, J.L.5    Hackett, M.6    Miller, S.I.7
  • 56
    • 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. 279:2004;20044-20048
    • (2004) J. Biol. Chem. , vol.279 , pp. 20044-20048
    • Kawasaki, K.1    Ernst, R.K.2    Miller, S.I.3
  • 58
    • 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. 304:2004;1014-1018
    • (2004) Science , vol.304 , pp. 1014-1018
    • Blander, J.M.1    Medzhitov, R.2
  • 60
    • 0029021978 scopus 로고
    • Suppression of cytokines in mice by protein A-V antigen fusion peptide and restoration of synthesis by active immunization
    • Nakajima R., Motin V.L., Brubaker R.R. Suppression of cytokines in mice by protein A-V antigen fusion peptide and restoration of synthesis by active immunization. Infect. Immun. 63:1995;3021-3029
    • (1995) Infect. Immun. , vol.63 , pp. 3021-3029
    • Nakajima, R.1    Motin, V.L.2    Brubaker, R.R.3
  • 61
    • 0036467351 scopus 로고    scopus 로고
    • Yersinia enterocolitica evasion of the host innate immune response by V antigen-induced IL-10 production of macrophages is abrogated in IL-10-deficient mice
    • Sing A., Roggenkamp A., Geiger A.M., Heesemann J. Yersinia enterocolitica evasion of the host innate immune response by V antigen-induced IL-10 production of macrophages is abrogated in IL-10-deficient mice. J. Immunol. 168:2002;1315-1321
    • (2002) J. Immunol. , vol.168 , pp. 1315-1321
    • Sing, A.1    Roggenkamp, A.2    Geiger, A.M.3    Heesemann, J.4
  • 62
    • 0344562930 scopus 로고    scopus 로고
    • Suppression of T and B lymphocyte activation by a Yersinia pseudotuberculosis virulence factor, yopH
    • Yao T., Mecsas J., Healy J.I., Falkow S., Chien Y. Suppression of T and B lymphocyte activation by a Yersinia pseudotuberculosis virulence factor, yopH. J. Exp. Med. 190:1999;1343-1350
    • (1999) J. Exp. Med. , vol.190 , pp. 1343-1350
    • Yao, T.1    Mecsas, J.2    Healy, J.I.3    Falkow, S.4    Chien, Y.5
  • 63
    • 0030946572 scopus 로고    scopus 로고
    • Resistance to lipopolysaccharide mediated by the Yersinia pestis V antigen-polyhistidine fusion peptide: Amplification of interleukin-10
    • Nedialkov Y.A., Motin V.L., Brubaker R.R. Resistance to lipopolysaccharide mediated by the Yersinia pestis V antigen-polyhistidine fusion peptide: amplification of interleukin-10. Infect. Immun. 65:1997;1196-1203
    • (1997) Infect. Immun. , vol.65 , pp. 1196-1203
    • Nedialkov, Y.A.1    Motin, V.L.2    Brubaker, R.R.3
  • 64
    • 0037973623 scopus 로고    scopus 로고
    • Interleukin-10 and inhibition of innate immunity to Yersiniae: Roles of Yops and LcrV (V antigen)
    • Brubaker R.R. Interleukin-10 and inhibition of innate immunity to Yersiniae: roles of Yops and LcrV (V antigen). Infect. Immun. 71:2003;3673-3681
    • (2003) Infect. Immun. , vol.71 , pp. 3673-3681
    • Brubaker, R.R.1
  • 67
    • 3442893287 scopus 로고    scopus 로고
    • Mini-review: The role of peptidoglycan recognition in innate immunity
    • Girardin S.E., Philpott D.J. Mini-review: The role of peptidoglycan recognition in innate immunity. Eur. J. Immunol. 34:2004;1777-1782
    • (2004) Eur. J. Immunol. , vol.34 , pp. 1777-1782
    • Girardin, S.E.1    Philpott, D.J.2
  • 68
    • 0038624558 scopus 로고    scopus 로고
    • NODs: Intracellular proteins involved in inflammation and apoptosis
    • Inohara N., Nunez G. NODs: intracellular proteins involved in inflammation and apoptosis. Nat. Rev. Immunol. 3:2003;371-382
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 371-382
    • Inohara, N.1    Nunez, G.2
  • 77
    • 1342344961 scopus 로고    scopus 로고
    • Nod1 is an essential signal transducer in intestinal epithelial cells infected with bacteria that avoid recognition by toll-like receptors
    • Kim J.G., Lee S.J., Kagnoff M.F. Nod1 is an essential signal transducer in intestinal epithelial cells infected with bacteria that avoid recognition by toll-like receptors. Infect. Immun. 72:2004;1487-1495
    • (2004) Infect. Immun. , vol.72 , pp. 1487-1495
    • Kim, J.G.1    Lee, S.J.2    Kagnoff, M.F.3
  • 78
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li Q., Verma I.M. NF-kappaB regulation in the immune system. Nat. Rev. Immunol. 2:2002;725-734
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 79
    • 0036081269 scopus 로고    scopus 로고
    • Host-pathogen interactions: Subversion and utilization of the NF-kappa B pathway during infection
    • Tato C.M., Hunter C.A. Host-pathogen interactions: subversion and utilization of the NF-kappa B pathway during infection. Infect. Immun. 70:2002;3311-3317
    • (2002) Infect. Immun. , vol.70 , pp. 3311-3317
    • Tato, C.M.1    Hunter, C.A.2
  • 80
    • 0033578923 scopus 로고    scopus 로고
    • Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector
    • Orth K., Palmer L.E., Bao Z.Q., Stewart S., Rudolph A.E., Bliska J.B., Dixon J.E. Inhibition of the mitogen-activated protein kinase kinase superfamily by a Yersinia effector. Science. 285:1999;1920-1923
    • (1999) Science , vol.285 , pp. 1920-1923
    • Orth, K.1    Palmer, L.E.2    Bao, Z.Q.3    Stewart, S.4    Rudolph, A.E.5    Bliska, J.B.6    Dixon, J.E.7
  • 82
    • 0030886017 scopus 로고    scopus 로고
    • A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria
    • Hardt W.D., Galan J.E. A secreted Salmonella protein with homology to an avirulence determinant of plant pathogenic bacteria. Proc. Natl. Acad. Sci. USA. 94:1997;9887-9892
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9887-9892
    • Hardt, W.D.1    Galan, J.E.2
  • 85
    • 0142210412 scopus 로고    scopus 로고
    • An inclusion membrane protein from Chlamydia trachomatis enters the MHC class I pathway and stimulates a CD8+ T cell response
    • Starnbach M.N., Loomis W.P., Ovendale P., Regan D., Hess B., Alderson M.R., Fling S.P. An inclusion membrane protein from Chlamydia trachomatis enters the MHC class I pathway and stimulates a CD8+ T cell response. J. Immunol. 171:2003;4742-4749
    • (2003) J. Immunol. , vol.171 , pp. 4742-4749
    • Starnbach, M.N.1    Loomis, W.P.2    Ovendale, P.3    Regan, D.4    Hess, B.5    Alderson, M.R.6    Fling, S.P.7
  • 87
    • 0036137205 scopus 로고    scopus 로고
    • Chlamydia pneumoniae secretion of a protease-like activity factor for degrading host cell transcription factors required for [correction of factors is required for] major histocompatibility complex antigen expression
    • Fan P., Dong F., Huang Y., Zhong G. Chlamydia pneumoniae secretion of a protease-like activity factor for degrading host cell transcription factors required for [correction of factors is required for] major histocompatibility complex antigen expression. Infect. Immun. 70:2002;345-349
    • (2002) Infect. Immun. , vol.70 , pp. 345-349
    • Fan, P.1    Dong, F.2    Huang, Y.3    Zhong, G.4
  • 88
    • 0034193165 scopus 로고    scopus 로고
    • Degradation of transcription factor RFX5 during the inhibition of both constitutive and interferon gamma-inducible major histocompatibility complex class I expression in chlamydia-infected cells
    • Zhong G., Liu L., Fan T., Fan P., Ji H. Degradation of transcription factor RFX5 during the inhibition of both constitutive and interferon gamma-inducible major histocompatibility complex class I expression in chlamydia-infected cells. J. Exp. Med. 191:2000;1525-1534
    • (2000) J. Exp. Med. , vol.191 , pp. 1525-1534
    • Zhong, G.1    Liu, L.2    Fan, T.3    Fan, P.4    Ji, H.5
  • 89
    • 0033591635 scopus 로고    scopus 로고
    • Chlamydia inhibits interferon gamma-inducible major histocompatibility complex class II expression by degradation of upstream stimulatory factor 1
    • Zhong G., Fan T., Liu L. Chlamydia inhibits interferon gamma-inducible major histocompatibility complex class II expression by degradation of upstream stimulatory factor 1. J. Exp. Med. 189:1999;1931-1938
    • (1999) J. Exp. Med. , vol.189 , pp. 1931-1938
    • Zhong, G.1    Fan, T.2    Liu, L.3
  • 92
    • 0042932364 scopus 로고    scopus 로고
    • Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation
    • Gebert B., Fischer W., Weiss E., Hoffmann R., Haas R. Helicobacter pylori vacuolating cytotoxin inhibits T lymphocyte activation. Science. 301:2003;1099-1102
    • (2003) Science , vol.301 , pp. 1099-1102
    • Gebert, B.1    Fischer, W.2    Weiss, E.3    Hoffmann, R.4    Haas, R.5
  • 94
    • 0037057687 scopus 로고    scopus 로고
    • Antimicrobial peptides in health and disease
    • Zasloff M. Antimicrobial peptides in health and disease. N. Engl. J. Med. 347:2002;1199-1200
    • (2002) N. Engl. J. Med. , vol.347 , pp. 1199-1200
    • Zasloff, M.1
  • 95
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 415:2002;389-395
    • (2002) Nature , vol.415 , pp. 389-395
    • Zasloff, M.1
  • 96
    • 3342908873 scopus 로고    scopus 로고
    • The role of Paneth cells and their antimicrobial peptides in innate host defense
    • Ayabe T., Ashida T., Kohgo Y., Kono T. The role of Paneth cells and their antimicrobial peptides in innate host defense. Trends Microbiol. 12:2004;394-398
    • (2004) Trends Microbiol. , vol.12 , pp. 394-398
    • Ayabe, T.1    Ashida, T.2    Kohgo, Y.3    Kono, T.4
  • 97
    • 0037417311 scopus 로고    scopus 로고
    • Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin
    • Salzman N.H., Ghosh D., Huttner K.M., Paterson Y., Bevins C.L. Protection against enteric salmonellosis in transgenic mice expressing a human intestinal defensin. Nature. 422:2003;522-526
    • (2003) Nature , vol.422 , pp. 522-526
    • Salzman, N.H.1    Ghosh, D.2    Huttner, K.M.3    Paterson, Y.4    Bevins, C.L.5
  • 99
    • 0033652796 scopus 로고    scopus 로고
    • Leukocyte granule proteins mobilize innate host defenses and adaptive immune responses
    • Chertov O., Yang D., Howard O.M., Oppenheim J.J. Leukocyte granule proteins mobilize innate host defenses and adaptive immune responses. Immunol. Rev. 177:2000;68-78
    • (2000) Immunol. Rev. , vol.177 , pp. 68-78
    • Chertov, O.1    Yang, D.2    Howard, O.M.3    Oppenheim, J.J.4
  • 101
    • 0035126317 scopus 로고    scopus 로고
    • Downregulation of bactericidal peptides in enteric infections: A novel immune escape mechanism with bacterial DNA as a potential regulator
    • Islam D., Bandholtz L., Nilsson J., Wigzell H., Christensson B., Agerberth B., Gudmundsson G. Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 7:2001;180-185
    • (2001) Nat. Med. , vol.7 , pp. 180-185
    • Islam, D.1    Bandholtz, L.2    Nilsson, J.3    Wigzell, H.4    Christensson, B.5    Agerberth, B.6    Gudmundsson, G.7
  • 102
    • 0037372643 scopus 로고    scopus 로고
    • Enteric salmonella infection inhibits Paneth cell antimicrobial peptide expression
    • Salzman N.H., Chou M.M., de Jong H., Liu L., Porter E.M., Paterson Y. Enteric salmonella infection inhibits Paneth cell antimicrobial peptide expression. Infect. Immun. 71:2003;1109-1115
    • (2003) Infect. Immun. , vol.71 , pp. 1109-1115
    • Salzman, N.H.1    Chou, M.M.2    De Jong, H.3    Liu, L.4    Porter, E.M.5    Paterson, Y.6
  • 103
    • 1642454704 scopus 로고    scopus 로고
    • Staphylococcus aureus resists human defensins by production of staphylokinase, a novel bacterial evasion mechanism
    • Jin T., Bokarewa M., Foster T., Mitchell J., Higgins J., Tarkowski A. Staphylococcus aureus resists human defensins by production of staphylokinase, a novel bacterial evasion mechanism. J. Immunol. 172:2004;1169-1176
    • (2004) J. Immunol. , vol.172 , pp. 1169-1176
    • Jin, T.1    Bokarewa, M.2    Foster, T.3    Mitchell, J.4    Higgins, J.5    Tarkowski, A.6
  • 105
    • 2342464290 scopus 로고    scopus 로고
    • Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system
    • Perrin A.J., Jiang X., Birmingham C.L., So N.S., Brumell J.H. Recognition of bacteria in the cytosol of mammalian cells by the ubiquitin system. Curr. Biol. 14:2004;806-811
    • (2004) Curr. Biol. , vol.14 , pp. 806-811
    • Perrin, A.J.1    Jiang, X.2    Birmingham, C.L.3    So, N.S.4    Brumell, J.H.5
  • 106
    • 0036685429 scopus 로고    scopus 로고
    • The host cytosol: Front-line or home front?
    • O'Riordan M., Portnoy D.A. The host cytosol: front-line or home front? Trends Microbiol. 10:2002;361-364
    • (2002) Trends Microbiol. , vol.10 , pp. 361-364
    • O'Riordan, M.1    Portnoy, D.A.2
  • 107
    • 0036259995 scopus 로고    scopus 로고
    • Disruption of the Salmonella-containing vacuole leads to increased replication of Salmonella enterica serovar typhimurium in the cytosol of epithelial cells
    • Brumell J.H., Tang P., Zaharik M.L., Finlay B.B. Disruption of the Salmonella-containing vacuole leads to increased replication of Salmonella enterica serovar typhimurium in the cytosol of epithelial cells. Infect. Immun. 70:2002;3264-3270
    • (2002) Infect. Immun. , vol.70 , pp. 3264-3270
    • Brumell, J.H.1    Tang, P.2    Zaharik, M.L.3    Finlay, B.B.4
  • 108
    • 0036736564 scopus 로고    scopus 로고
    • Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines
    • Beuzon C.R., Salcedo S.P., Holden D.W. Growth and killing of a Salmonella enterica serovar Typhimurium sifA mutant strain in the cytosol of different host cell lines. Microbiology. 148:2002;2705-2715
    • (2002) Microbiology , vol.148 , pp. 2705-2715
    • Beuzon, C.R.1    Salcedo, S.P.2    Holden, D.W.3
  • 110
    • 0030610785 scopus 로고    scopus 로고
    • Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt G., Sehr P., Wilm M., Selzer J., Mann M., Aktories K. Gln 63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature. 387:1997;725-729
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1    Sehr, P.2    Wilm, M.3    Selzer, J.4    Mann, M.5    Aktories, K.6
  • 112
    • 4143129048 scopus 로고    scopus 로고
    • Activation and proteasomal degradation of Rho GTPases by CNF1 elicit a controlled inflammatory response
    • Munro P., Flatau G., Doye A., Boyer L., Oregioni O., Mege J.L., Landraud L., Lemichez E. Activation and proteasomal degradation of Rho GTPases by CNF1 elicit a controlled inflammatory response. J. Biol. Chem. 279:2004;35849-35857
    • (2004) J. Biol. Chem. , vol.279 , pp. 35849-35857
    • Munro, P.1    Flatau, G.2    Doye, A.3    Boyer, L.4    Oregioni, O.5    Mege, J.L.6    Landraud, L.7    Lemichez, E.8
  • 113
    • 1942486364 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K7 protein targets a ubiquitin-like/ubiquitin-associated domain-containing protein to promote protein degradation
    • Feng P., Scott C.W., Cho N.H., Nakamura H., Chung Y.H., Monteiro M.J., Jung J.U. Kaposi's sarcoma-associated herpesvirus K7 protein targets a ubiquitin-like/ubiquitin-associated domain-containing protein to promote protein degradation. Mol. Cell Biol. 24:2004;3938-3948
    • (2004) Mol. Cell Biol. , vol.24 , pp. 3938-3948
    • Feng, P.1    Scott, C.W.2    Cho, N.H.3    Nakamura, H.4    Chung, Y.H.5    Monteiro, M.J.6    Jung, J.U.7
  • 114
    • 0038679208 scopus 로고    scopus 로고
    • Hepatitis B virus core protein stimulates the proteasome-mediated degradation of viral X protein
    • Kim J.H., Kang S., Kim J., Ahn B.Y. Hepatitis B virus core protein stimulates the proteasome-mediated degradation of viral X protein. J. Virol. 77:2003;7166-7173
    • (2003) J. Virol. , vol.77 , pp. 7166-7173
    • Kim, J.H.1    Kang, S.2    Kim, J.3    Ahn, B.Y.4
  • 115
    • 2942670459 scopus 로고    scopus 로고
    • Can innate immunity be enhanced to treat microbial infections?
    • Finlay B.B., Hancock R.E. Can innate immunity be enhanced to treat microbial infections? Nat. Rev. Microbiol. 2:2004;497-504
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 497-504
    • Finlay, B.B.1    Hancock, R.E.2


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