Abstract
Enterohemorrhagic Escherichia coli (EHEC) is a significant foodborne attaching and effacing (A/E) pathogen that causes diarrhea, hemorrhagic colitis and the hemolytic-uremic syndrome (HUS) in humans. EHEC is closely related to enteropathogenic E. coli (EPEC) and both induce characteristic A/E lesions on the gut mucosal surface. During EHEC and EPEC infection, host innate immune responses, such as inflammation and cell death are rapidly activated, upon the detection of bacterial components and virulence factor activity. To promote A/E lesion formation and dissemination of the pathogen in the body, EHEC and EPEC deliver a repertoire of effector proteins, including Tir, NleA/EspI and NleB to -H, to the host cell cytosol via a type III secretion system (T3SS). These interfere with a range of host cell processes, including host defense mechanisms. Several T3SS effector proteins specifically modify or cleave host proteins involved in inflammation and cell death, thereby inactivating these pathways. The identification of the host targets and the characterization of the biochemical function of T3SS effectors have greatly contributed to understanding the pathogenesis of EHEC and EPEC infections.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Abbreviations
- A/E pathogen:
-
Attaching/effacing pathogen
- AP-1:
-
Activation protein-1
- BI-1:
-
Bax inhibitor-1
- CLR:
-
C-type lection receptor
- CRL:
-
Cullin Ring E3 ligases
- DC:
-
Dendritic cell
- DD:
-
Death domains
- DISC:
-
Death-inducing signaling complex
- EHEC:
-
Enterohemorrhagic Escherichia coli
- FA:
-
Focal adhesion
- GlcNAc:
-
N-acetylglucosamine
- HUS:
-
Hemolytic uremic syndrome
- IE:
-
Integrative element
- ILK:
-
Integrin-linked kinase
- ITIM:
-
Immunoreceptor tyrosine-based inhibitory motifs
- LEE:
-
Locus of enterocyte effacement
- LPS:
-
Lipopolysaccharide
- MAPK:
-
Mitogen-activated protein kinase
- MTS:
-
Mitochondrial targeting sequence
- NF-κB:
-
Nuclear-factor κB
- NLR:
-
NOD-like receptor
- NZF:
-
Npl4 Zinc figure
- OI:
-
O-island
- PAMPs:
-
Pathogen-associated molecular patterns
- PKC:
-
Protein kinase C
- PRRs:
-
Pattern recognition receptors
- RLR:
-
RIG-I-like receptor
- SAM:
-
S-adenosyl-L-methionine
- Stx:
-
Shiga toxins
- T3SS:
-
Type III secretion system
- TAB2 and TAB3:
-
TAK1-binding proteins 2 and 3
- TAD:
-
Transcription activation domain
- TIM17b:
-
Translocase of inner mitochondrial membrane 17b
- Tir:
-
Translocated intimin receptor
- TLR:
-
Toll-like receptor
- TNFR1:
-
Tumor necrosis factor receptor 1
- TRAIL:
-
TNF-associated apoptosis-inducing ligand
References
Akira, S., Uematsu, S., & Takeuchi, O. (2006). Pathogen recognition and innate immunity. Cell, 124(4), 783–801.
Barnett Foster, D., et al. (2000). Enterohemorrhagic Escherichia coli induces apoptosis which augments bacterial binding and phosphatidylethanolamine exposure on the plasma membrane outer leaflet. Infection and Immunity, 68(6), 3108–3115.
Baruch, K., et al. (2011). Metalloprotease type III effectors that specifically cleave JNK and NF-kappaB. The EMBO Journal, 30(1), 221–231.
Berger, C. N., et al. (2012). EspZ of enteropathogenic and enterohemorrhagic Escherichia coli regulates type III secretion system protein translocation. MBio, 3(5), e00317–e00312.
Berin, M. C., et al. (2002). Role of EHEC O157:H7 virulence factors in the activation of intestinal epithelial cell NF-kappaB and MAP kinase pathways and the upregulated expression of interleukin 8. Cellular Microbiology, 4(10), 635–648.
Blasche, S., et al. (2013). The E. coli effector protein NleF is a caspase inhibitor. PloS One, 8(3), e58937.
Boyce, T. G., Swerdlow, D. L., & Griffin, P. M. (1995). Escherichia coli O157:H7 and the hemolytic-uremic syndrome. The New England Journal of Medicine, 333(6), 364–368.
Callaway, T. R., et al. (2009). Diet, Escherichia coli O157:H7, and cattle: A review after 10 years. Current Issues in Molecular Biology, 11(2), 67–79.
Crow, A., et al. (2012). The molecular basis of ubiquitin-like protein NEDD8 deamidation by the bacterial effector protein Cif. Proceedings of the National Academy of Sciences of the United States of America, 109(27), E1830–E1838.
Cui, J., et al. (2010). Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Science, 329(5996), 1215–1218.
Dean, P., et al. (2010). The enteropathogenic E. coli effector EspF targets and disrupts the nucleolus by a process regulated by mitochondrial dysfunction. PLoS Pathogens, 6(6), e1000961.
Deng, W., et al. (2004). Dissecting virulence: Systematic and functional analyses of a pathogenicity island. Proceedings of the National Academy of Sciences of the United States of America, 101(10), 3597–3602.
Durso, L. M., et al. (2005). Shiga-toxigenic Escherichia coli O157:H7 infections among livestock exhibitors and visitors at a Texas County fair. Vector Borne and Zoonotic Diseases, 5(2), 193–201.
Elliott, S. J., et al. (2000). The locus of enterocyte effacement (LEE)-encoded regulator controls expression of both LEE- and non-LEE-encoded virulence factors in enteropathogenic and enterohemorrhagic Escherichia coli. Infection and Immunity, 68(11), 6115–6126.
Endo, Y., et al. (1988). Site of action of a Vero toxin (VT2) from Escherichia coli O157:H7 and of Shiga toxin on eukaryotic ribosomes. RNA N-glycosidase activity of the toxins. European Journal of Biochemistry, 171(1–2), 45–50.
Feng, P. C., & Reddy, S. (2013). Prevalences of Shiga toxin subtypes and selected other virulence factors among Shiga-toxigenic Escherichia coli strains isolated from fresh produce. Applied and Environmental Microbiology, 79(22), 6917–6923.
Feuerbacher, L. A., & Hardwidge, P. R. (2014). Influence of NleH effector expression, host genetics, and inflammation on Citrobacter rodentium colonization of mice. Microbes and Infection, 16(5), 429–433.
Frankel, G., et al. (1998). Enteropathogenic and enterohaemorrhagic Escherichia coli: More subversive elements. Molecular Microbiology, 30(5), 911–921.
From the Centers for Disease Control and Prevention. (1995). Escherichia coli O157:H7 outbreak linked to commercially distributed dry-cured salami – Washington and California, 1994. JAMA, 273(13), 985–986.
Gao, X., et al. (2009). Bacterial effector binding to ribosomal protein s3 subverts NF-kappaB function. PLoS Pathogens, 5(12), e1000708.
Gao, X., et al. (2013). NleB, a bacterial effector with glycosyltransferase activity, targets GAPDH function to inhibit NF-kappaB activation. Cell Host & Microbe, 13(1), 87–99.
Ghosh, S., May, M. J., & Kopp, E. B. (1998). NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses. Annual Review of Immunology, 16, 225–260.
Giogha, C., et al. (2015). Substrate recognition by the zinc metalloprotease effector NleC from enteropathogenic Escherichia coli. Cellular Microbiology, 17, 1766–1778.
Hayden, M. S., & Ghosh, S. (2008). Shared principles in NF-kappaB signaling. Cell, 132(3), 344–362.
Hemrajani, C., et al. (2008). Role of NleH, a type III secreted effector from attaching and effacing pathogens, in colonization of the bovine, ovine, and murine gut. Infection and Immunity, 76(11), 4804–4813.
Hemrajani, C., et al. (2010). NleH effectors interact with Bax inhibitor-1 to block apoptosis during enteropathogenic Escherichia coli infection. Proceedings of the National Academy of Sciences of the United States of America, 107(7), 3129–3134.
Hurley, B. P., Thorpe, C. M., & Acheson, D. W. (2001). Shiga toxin translocation across intestinal epithelial cells is enhanced by neutrophil transmigration. Infection and Immunity, 69(10), 6148–6155.
Iguchi, A., et al. (2009). Complete genome sequence and comparative genome analysis of enteropathogenic Escherichia coli O127:H6 strain E2348/69. Journal of Bacteriology, 191(1), 347–354.
Imtiyaz, H. Z., Zhang, Y., & Zhang, J. (2005). Structural requirements for signal-induced target binding of FADD determined by functional reconstitution of FADD deficiency. The Journal of Biological Chemistry, 280(36), 31360–31367.
Johnson, G. L., & Lapadat, R. (2002). Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science, 298(5600), 1911–1912.
Kanack, K. J., et al. (2005). SepZ/EspZ is secreted and translocated into HeLa cells by the enteropathogenic Escherichia coli type III secretion system. Infection and Immunity, 73(7), 4327–4337.
Kaper, J. B., Nataro, J. P., & Mobley, H. L. (2004). Pathogenic Escherichia coli. Nature Reviews. Microbiology, 2(2), 123–140.
Karmali, M. A., et al. (1983). Sporadic cases of haemolytic-uraemic syndrome associated with faecal cytotoxin and cytotoxin-producing Escherichia coli in stools. Lancet, 1(8325), 619–620.
Karmali, M. A., Gannon, V., & Sargeant, J. M. (2010). Verocytotoxin-producing Escherichia coli (VTEC). Veterinary Microbiology, 140(3–4), 360–370.
Kashiwamura, M., et al. (2009). Shiga toxin kills epithelial cells isolated from distal but not proximal part of mouse colon. Biological & Pharmaceutical Bulletin, 32(9), 1614–1617.
Kelly, M., et al. (2006). Essential role of the type III secretion system effector NleB in colonization of mice by Citrobacter rodentium. Infection and Immunity, 74(4), 2328–2337.
Kenny, B., & Jepson, M. (2000). Targeting of an enteropathogenic Escherichia coli (EPEC) effector protein to host mitochondria. Cellular Microbiology, 2(6), 579–590.
Khan, M. A., et al. (2006). Toll-like receptor 4 contributes to colitis development but not to host defense during Citrobacter rodentium infection in mice. Infection and Immunity, 74(5), 2522–2536.
Kim, D. W., et al. (2005). The Shigella flexneri effector OspG interferes with innate immune responses by targeting ubiquitin-conjugating enzymes. Proceedings of the National Academy of Sciences of the United States of America, 102(39), 14046–14051.
Kim, M., et al. (2009). Bacteria hijack integrin-linked kinase to stabilize focal adhesions and block cell detachment. Nature, 459(7246), 578–582.
Li, S., et al. (2013). Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains. Nature, 501(7466), 242–246.
Liu, S., & Chen, Z. J. (2011). Expanding role of ubiquitination in NF-kappaB signaling. Cell Research, 21(1), 6–21.
Lupfer, C. R., et al. (2014). Reactive oxygen species regulate caspase-11 expression and activation of the non-canonical NLRP3 inflammasome during enteric pathogen infection. PLoS Pathogens, 10(9), e1004410.
Ma, C., et al. (2006). Citrobacter rodentium infection causes both mitochondrial dysfunction and intestinal epithelial barrier disruption in vivo: Role of mitochondrial associated protein (Map). Cellular Microbiology, 8(10), 1669–1686.
Manning, S. D., et al. (2008). Variation in virulence among clades of Escherichia coli O157:H7 associated with disease outbreaks. Proceedings of the National Academy of Sciences of the United States of America, 105(12), 4868–4873.
Marches, O., et al. (2003). Enteropathogenic and enterohaemorrhagic Escherichia coli deliver a novel effector called Cif, which blocks cell cycle G2/M transition. Molecular Microbiology, 50(5), 1553–1567.
Marches, O., et al. (2005). Characterization of two non-locus of enterocyte effacement-encoded type III-translocated effectors, NleC and NleD, in attaching and effacing pathogens. Infection and Immunity, 73(12), 8411–8417.
McCormack, R. M., et al. (2015). Enteric pathogens deploy cell cycle inhibiting factors to block the bactericidal activity of Perforin-2. eLife, 4, e06505.
McDaniel, T. K., et al. (1995). A genetic locus of enterocyte effacement conserved among diverse enterobacterial pathogens. Proceedings of the National Academy of Sciences of the United States of America, 92(5), 1664–1668.
Mead, P. S., & Griffin, P. M. (1998). Escherichia coli O157:H7. Lancet, 352(9135), 1207–1212.
Miyamoto, Y., et al. (2006). Role of Shiga toxin versus H7 flagellin in enterohaemorrhagic Escherichia coli signalling of human colon epithelium in vivo. Cellular Microbiology, 8(5), 869–879.
Morita-Ishihara, T., et al. (2013). EspO1-2 regulates EspM2-mediated RhoA activity to s(43): p. 30101-13. Tabilize formation of focal adhesions in enterohemorrhagic Escherichia coli-infected host cells. PloS One, 8(2), e55960.
Muhlen, S., Ruchaud-Sparagano, M. H., & Kenny, B. (2011). Proteasome-independent degradation of canonical NFkappaB complex components by the NleC protein of pathogenic Escherichia coli. The Journal of Biological Chemistry, 286(7), 5100–5107.
Mukaida, N., Mahe, Y., & Matsushima, K. (1990). Cooperative interaction of nuclear factor-kappa B- and cis-regulatory enhancer binding protein-like factor binding elements in activating the interleukin-8 gene by pro-inflammatory cytokines. The Journal of Biological Chemistry, 265(34), 21128–21133.
Mukaida, N., et al. (1994). Molecular mechanism of interleukin-8 gene expression. Journal of Leukocyte Biology, 56(5), 554–558.
Muthing, J., et al. (2009). Shiga toxins, glycosphingolipid diversity, and endothelial cell injury. Thrombosis and Haemostasis, 101(2), 252–264.
Nadler, C., et al. (2010). The type III secretion effector NleE inhibits NF-kappaB activation. PLoS Pathogens, 6(1), e1000743.
Neel, B. G., Gu, H., & Pao, L. (2003). The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling. Trends in Biochemical Sciences, 28(6), 284–293.
Newton, H. J., et al. (2010). The type III effectors NleE and NleB from enteropathogenic E. coli and OspZ from Shigella block nuclear translocation of NF-kappaB p65. PLoS Pathogens, 6(5), e1000898.
Nordlander, S., Pott, J., & Maloy, K. J. (2014). NLRC4 expression in intestinal epithelial cells mediates protection against an enteric pathogen. Mucosal Immunology, 7(4), 775–785.
Nougayrede, J. P., Foster, G. H., & Donnenberg, M. S. (2007). Enteropathogenic Escherichia coli effector EspF interacts with host protein Abcf2. Cellular Microbiology, 9(3), 680–693.
Orchard, R. C., et al. (2012). Identification of F-actin as the dynamic hub in a microbial-induced GTPase polarity circuit. Cell, 148(4), 803–815.
Pallett, M. A., et al. (2014). The type III secretion effector NleF of enteropathogenic Escherichia coli activates NF-kappaB early during infection. Infection and Immunity, 82(11), 4878–4888.
Park, H. H., et al. (2007). The death domain superfamily in intracellular signaling of apoptosis and inflammation. Annual Review of Immunology, 25, 561–586.
Pearson, J. S., & Hartland, E. L. (2014). The inflammatory response during Enterohemorrhagic Escherichia coli infection. Microbiology Spectrum, 2(4), 321–339.
Pearson, J. S., et al. (2011). A type III effector protease NleC from enteropathogenic Escherichia coli targets NF-kappaB for degradation. Molecular Microbiology, 80(1), 219–230.
Pearson, J. S., et al. (2013). A type III effector antagonizes death receptor signalling during bacterial gut infection. Nature, 501(7466), 247–251.
Perna, N. T., et al. (2001). Genome sequence of enterohaemorrhagic Escherichia coli O157:H7. Nature, 409(6819), 529–533.
Pham, T. H., et al. (2012). Functional differences and interactions between the Escherichia coli type III secretion system effectors NleH1 and NleH2. Infection and Immunity, 80(6), 2133–2140.
Raymond, B., et al. (2011). The WxxxE effector EspT triggers expression of immune mediators in an Erk/JNK and NF-kappaB-dependent manner. Cellular Microbiology, 13(12), 1881–1893.
Riley, L. W., et al. (1983). Hemorrhagic colitis associated with a rare Escherichia coli serotype. The New England Journal of Medicine, 308(12), 681–685.
Robinson, K. S., et al. (2010). The enteropathogenic Escherichia coli effector NleH inhibits apoptosis induced by Clostridium difficile toxin B. Microbiology, 156(Pt 6), 1815–1823.
Ruchaud-Sparagano, M. H., et al. (2011). The enteropathogenic E. coli (EPEC) Tir effector inhibits NF-kappaB activity by targeting TNFalpha receptor-associated factors. PLoS Pathogens, 7(12), e1002414.
Samba-Louaka, A., et al. (2008). Bacterial cyclomodulin Cif blocks the host cell cycle by stabilizing the cyclin-dependent kinase inhibitors p21 and p27. Cellular Microbiology, 10(12), 2496–2508.
Samba-Louaka, A., et al. (2009). The enteropathogenic Escherichia coli effector Cif induces delayed apoptosis in epithelial cells. Infection and Immunity, 77(12), 5471–5477.
Sato, Y., et al. (2009). Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by NZF domains of TAB2 and TAB3. The EMBO Journal, 28(24), 3903–3909.
Schuller, S., Frankel, G., & Phillips, A. D. (2004). Interaction of Shiga toxin from Escherichia coli with human intestinal epithelial cell lines and explants: Stx2 induces epithelial damage in organ culture. Cellular Microbiology, 6(3), 289–301.
Sellin, M. E., et al. (2015). Inflammasomes of the intestinal epithelium. Trends in Immunology, 36(8), 442–450.
Sham, H. P., et al. (2011). Attaching and effacing bacterial effector NleC suppresses epithelial inflammatory responses by inhibiting NF-kappaB and p38 mitogen-activated protein kinase activation. Infection and Immunity, 79(9), 3552–3562.
Shames, S. R., et al. (2010). The pathogenic E. coli type III effector EspZ interacts with host CD98 and facilitates host cell prosurvival signalling. Cellular Microbiology, 12(9), 1322–1339.
Shames, S. R., et al. (2011a). The pathogenic Escherichia coli type III secreted protease NleC degrades the host acetyltransferase p300. Cellular Microbiology, 13(10), 1542–1557.
Shames, S. R., et al. (2011b). The type III system-secreted effector EspZ localizes to host mitochondria and interacts with the translocase of inner mitochondrial membrane 17b. Infection and Immunity, 79(12), 4784–4790.
Shaulian, E., & Karin, M. (2001). AP-1 in cell proliferation and survival. Oncogene, 20(19), 2390–2400.
Smith, W. E., et al. (2003). Shiga toxin 1 triggers a ribotoxic stress response leading to p38 and JNK activation and induction of apoptosis in intestinal epithelial cells. Infection and Immunity, 71(3), 1497–1504.
Spika, J. S., et al. (1986). Hemolytic uremic syndrome and diarrhea associated with Escherichia coli O157:H7 in a day care center. The Journal of Pediatrics, 109(2), 287–291.
Stahl, A. L., et al. (2006). Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome. Blood, 108(1), 167–176.
Taieb, F., et al. (2006). Escherichia coli Cyclomodulin Cif induces G2 arrest of the host cell cycle without activation of the DNA-damage checkpoint-signalling pathway. Cellular Microbiology, 8(12), 1910–1921.
Takaesu, G., et al. (2000). TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway. Molecular Cell, 5(4), 649–658.
Takeuchi, O., & Akira, S. (2010). Pattern recognition receptors and inflammation. Cell, 140(6), 805–820.
Thorpe, C. M., et al. (1999). Shiga toxins stimulate secretion of interleukin-8 from intestinal epithelial cells. Infection and Immunity, 67(11), 5985–5993.
Thorpe, C. M., et al. (2001). Shiga toxins induce, superinduce, and stabilize a variety of C-X-C chemokine mRNAs in intestinal epithelial cells, resulting in increased chemokine expression. Infection and Immunity, 69(10), 6140–6147.
Toro, T. B., Toth, J. I., & Petroski, M. D. (2013). The cyclomodulin cycle inhibiting factor (CIF) alters cullin neddylation dynamics. The Journal of Biological Chemistry, 288(21), 14716–14726.
Tzipori, S., et al. (1985). Enteropathogenic Escherichia coli enteritis: Evaluation of the gnotobiotic piglet as a model of human infection. Gut, 26(6), 570–578.
Tzipori, S., Gibson, R., & Montanaro, J. (1989). Nature and distribution of mucosal lesions associated with enteropathogenic and enterohemorrhagic Escherichia coli in piglets and the role of plasmid-mediated factors. Infection and Immunity, 57(4), 1142–1150.
van Setten, P. A., et al. (1996). Effects of verocytotoxin-1 on nonadherent human monocytes: Binding characteristics, protein synthesis, and induction of cytokine release. Blood, 88(1), 174–183.
Vallabhapurapu, S., & Karin, M. (2009). Regulation and function of NF-kappaB transcription factors in the immune system. Annual Review of Immunology, 27, 693–733.
Varma, J. K., et al. (2003). An outbreak of Escherichia coli O157 infection following exposure to a contaminated building. JAMA, 290(20), 2709–2712.
Vossenkamper, A., et al. (2010). Inhibition of NF-kappaB signaling in human dendritic cells by the enteropathogenic Escherichia coli effector protein NleE. Journal of Immunology, 185(7), 4118–4127.
Walters, M. D., et al. (1989). The polymorphonuclear leucocyte count in childhood haemolytic uraemic syndrome. Pediatric Nephrology, 3(2), 130–134.
Wan, F., et al. (2011). IKKbeta phosphorylation regulates RPS3 nuclear translocation and NF-kappaB function during infection with Escherichia coli strain O157:H7. Nature Immunology, 12(4), 335–343.
Wang, L., et al. (2010). The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nature Structural & Molecular Biology, 17(11), 1324–1329.
Wilbur, J. S., et al. (2015). The secreted effector protein EspZ is essential for virulence of rabbit enteropathogenic Escherichia coli. Infection and Immunity, 83(3), 1139–1149.
Wong Fok Lung, T., et al. (2014). The cell death response to enteropathogenic Escherichia coli infection. Cellular Microbiology, 16(12), 1736–1745.
Wong, A. R., et al. (2011). Enteropathogenic and enterohaemorrhagic Escherichia coli: Even more subversive elements. Molecular Microbiology, 80(6), 1420–1438.
Yan, D., et al. (2012). Inhibition of TLR signaling by a bacterial protein containing immunoreceptor tyrosine-based inhibitory motifs. Nature Immunology, 13(11), 1063–1071.
Yan, D., et al. (2013). Enteropathogenic Escherichia coli Tir recruits cellular SHP-2 through ITIM motifs to suppress host immune response. Cellular Signalling, 25(9), 1887–1894.
Yao, Q., et al. (2014). Structure and specificity of the bacterial cysteine methyltransferase effector NleE suggests a novel substrate in human DNA repair pathway. PLoS Pathogens, 10(11), e1004522.
Yen, H., et al. (2010). NleC, a type III secretion protease, compromises NF-kappaB activation by targeting p65/RelA. PLoS Pathogens, 6(12), e1001231.
Yen, H., Sugimoto, N., & Tobe, T. (2015). Enteropathogenic Escherichia coli uses NleA to inhibit NLRP3 inflammasome activation. PLoS Pathogens, 11(9), e1005121.
Yi, C. R., et al. (2014). Systematic analysis of bacterial effector-postsynaptic density 95/disc large/zonula occludens-1 (PDZ) domain interactions demonstrates Shigella OspE protein promotes protein kinase C activation via PDLIM proteins. The Journal of Biological Chemistry, 289, 30101–30113.
Zhang, Q., et al. (2000). Lack of phosphotyrosine phosphatase SHP-1 expression in malignant T-cell lymphoma cells results from methylation of the SHP-1 promoter. The American Journal of Pathology, 157(4), 1137–1146.
Zhang, L., et al. (2012). Cysteine methylation disrupts ubiquitin-chain sensing in NF-kappaB activation. Nature, 481(7380), 204–208.
Zhou, X., et al. (2003). Flagellin of enteropathogenic Escherichia coli stimulates interleukin-8 production in T84 cells. Infection and Immunity, 71(4), 2120–2129.
Zurawski, D. V., et al. (2008). The NleE/OspZ family of effector proteins is required for polymorphonuclear transepithelial migration, a characteristic shared by enteropathogenic Escherichia coli and Shigella flexneri infections. Infection and Immunity, 76(1), 369–379.
Acknowledgements
This work was supported by grants to ELH from the Australian National Health and Medical Research Council (APP1044061). JSP is the recipient of an NHMRC Early Career Fellowship. YZ is the recipient of a University of Melbourne International Research Scholarship (MIRS).
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2017 Springer International Publishing AG
About this chapter
Cite this chapter
Zhang, Y., Pearson, J.S., Hartland, E.L. (2017). Host Innate Immune Factors Influencing Enterohemorrhagic Escherichia coli Pathogenicity. In: Gurtler, J., Doyle, M., Kornacki, J. (eds) Foodborne Pathogens. Food Microbiology and Food Safety(). Springer, Cham. https://doi.org/10.1007/978-3-319-56836-2_12
Download citation
DOI: https://doi.org/10.1007/978-3-319-56836-2_12
Published:
Publisher Name: Springer, Cham
Print ISBN: 978-3-319-56834-8
Online ISBN: 978-3-319-56836-2
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)