메뉴 건너뛰기




Volumn 13, Issue 1, 2010, Pages 59-66

Anaplasma phagocytophilum and Ehrlichia chaffeensis type IV secretion and Ank proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; CELL NUCLEUS DNA; DNA FRAGMENT; PROTEIN ANKA; PROTEIN TYROSINE PHOSPHATASE SHP 1; PROTEIN VIRD4; UNCLASSIFIED DRUG;

EID: 75249092539     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2009.12.008     Document Type: Review
Times cited : (70)

References (50)
  • 1
    • 0029294739 scopus 로고
    • Experimental transmission of Ehrlichia chaffeensis (Rickettsiales: Ehrlichieae) among white-tailed deer by Amblyomma americanum (Acari: Ixodidae)
    • Ewing S.A., Dawson J.E., Kocan A.A., Barker R.W., Warner C.K., Panciera R.J., Fox J.C., Kocan K.M., and Blouin E.F. Experimental transmission of Ehrlichia chaffeensis (Rickettsiales: Ehrlichieae) among white-tailed deer by Amblyomma americanum (Acari: Ixodidae). J Med Entomol 32 (1995) 368-374
    • (1995) J Med Entomol , vol.32 , pp. 368-374
    • Ewing, S.A.1    Dawson, J.E.2    Kocan, A.A.3    Barker, R.W.4    Warner, C.K.5    Panciera, R.J.6    Fox, J.C.7    Kocan, K.M.8    Blouin, E.F.9
  • 3
    • 0037240533 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis: a prototypical emerging pathogen
    • Paddock C.D., and Childs J.E. Ehrlichia chaffeensis: a prototypical emerging pathogen. Clin Microbiol Rev 16 (2003) 37-64
    • (2003) Clin Microbiol Rev , vol.16 , pp. 37-64
    • Paddock, C.D.1    Childs, J.E.2
  • 4
    • 49849084354 scopus 로고    scopus 로고
    • Human granulocytic anaplasmosis
    • viii
    • Bakken J.S., and Dumler S. Human granulocytic anaplasmosis. Infect Dis Clin North Am 22 (2008) 433-448 viii
    • (2008) Infect Dis Clin North Am , vol.22 , pp. 433-448
    • Bakken, J.S.1    Dumler, S.2
  • 5
    • 70350468702 scopus 로고    scopus 로고
    • Current management of human granulocytic anaplasmosis, human monocytic ehrlichiosis and Ehrlichia ewingii ehrlichiosis
    • Thomas R.J., Dumler J.S., and Carlyon J.A. Current management of human granulocytic anaplasmosis, human monocytic ehrlichiosis and Ehrlichia ewingii ehrlichiosis. Expert Rev Anti Infect Ther 7 (2009) 709-722
    • (2009) Expert Rev Anti Infect Ther , vol.7 , pp. 709-722
    • Thomas, R.J.1    Dumler, J.S.2    Carlyon, J.A.3
  • 7
    • 71449116162 scopus 로고    scopus 로고
    • Biological diversities of prokaryotic Type IV secretion systems
    • This is a comprehensive and updated review of comparative Type IV secretion systems.
    • Alvarez-Marinez C.E., and Christie P.J. Biological diversities of prokaryotic Type IV secretion systems. Microbiol Mol Biol Rev 73 (2009) 775-808. This is a comprehensive and updated review of comparative Type IV secretion systems.
    • (2009) Microbiol Mol Biol Rev , vol.73 , pp. 775-808
    • Alvarez-Marinez, C.E.1    Christie, P.J.2
  • 9
    • 34848862803 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection
    • This study demonstrated a tyrosine-phosphorylated protein throughout infection, is A. phagocytophilum AnkA. AnkA is shown to be secreted in a VirB/D4-dependent manner. AnkA binds to Abl-interactor 1 that interacts with Abl-1 tyrosine kinase, thus mediating AnkA phosphorylation. Infection was inhibited upon host cytoplasmic delivery of anti-AnkA antibody, Abl-1 knockdown with targeted siRNA, or treatment with a specific pharmacological inhibitor of Abl-1.
    • Lin M., den Dulk-Ras A., Hooykaas P.J., and Rikihisa Y. Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection. Cell Microbiol 9 (2007) 2644-2657. This study demonstrated a tyrosine-phosphorylated protein throughout infection, is A. phagocytophilum AnkA. AnkA is shown to be secreted in a VirB/D4-dependent manner. AnkA binds to Abl-interactor 1 that interacts with Abl-1 tyrosine kinase, thus mediating AnkA phosphorylation. Infection was inhibited upon host cytoplasmic delivery of anti-AnkA antibody, Abl-1 knockdown with targeted siRNA, or treatment with a specific pharmacological inhibitor of Abl-1.
    • (2007) Cell Microbiol , vol.9 , pp. 2644-2657
    • Lin, M.1    den Dulk-Ras, A.2    Hooykaas, P.J.3    Rikihisa, Y.4
  • 10
    • 0035899360 scopus 로고    scopus 로고
    • Structural mimicry in bacterial virulence
    • Stebbins C.E., and Galan J.E. Structural mimicry in bacterial virulence. Nature 412 (2001) 701-705
    • (2001) Nature , vol.412 , pp. 701-705
    • Stebbins, C.E.1    Galan, J.E.2
  • 11
    • 67649397592 scopus 로고    scopus 로고
    • The Coxiella burnetii ankyrin repeat domain-containing protein family is heterogeneous with C-terminal truncations that influence Dot/Icm-mediated secretion
    • Using Legionella pneumophila as surrogate host, the authors identified 10 Anks from Coxiella burnetii Dugway and one Ank specific to the G and K endocarditis isolates are translocated into the host cytosol in a Dot/Icm-dependent fashion. A 10 amino acid C-terminal region is necessary for translocation with some Anks also requiring the chaperone IcmS for secretion. Ectopically expressed Anks localized to a variety of subcellular regions in mammalian cells including microtubules, mitochondria, and the PV membrane.
    • Voth D.E., Howe D., Beare P.A., Vogel J.P., Unsworth N., Samuel J.E., and Heinzen R.A. The Coxiella burnetii ankyrin repeat domain-containing protein family is heterogeneous with C-terminal truncations that influence Dot/Icm-mediated secretion. J Bacteriol 191 (2009) 4232-4242. Using Legionella pneumophila as surrogate host, the authors identified 10 Anks from Coxiella burnetii Dugway and one Ank specific to the G and K endocarditis isolates are translocated into the host cytosol in a Dot/Icm-dependent fashion. A 10 amino acid C-terminal region is necessary for translocation with some Anks also requiring the chaperone IcmS for secretion. Ectopically expressed Anks localized to a variety of subcellular regions in mammalian cells including microtubules, mitochondria, and the PV membrane.
    • (2009) J Bacteriol , vol.191 , pp. 4232-4242
    • Voth, D.E.1    Howe, D.2    Beare, P.A.3    Vogel, J.P.4    Unsworth, N.5    Samuel, J.E.6    Heinzen, R.A.7
  • 13
    • 67649718305 scopus 로고    scopus 로고
    • Type IV secretion system of Anaplasma phagocytophilum and Ehrlichia chaffeensis
    • Rikihisa Y., Lin M., Niu H., and Cheng Z. Type IV secretion system of Anaplasma phagocytophilum and Ehrlichia chaffeensis. Ann N Y Acad Sci 1166 (2009) 106-111
    • (2009) Ann N Y Acad Sci , vol.1166 , pp. 106-111
    • Rikihisa, Y.1    Lin, M.2    Niu, H.3    Cheng, Z.4
  • 14
    • 31844445394 scopus 로고    scopus 로고
    • Ehrlichia subversion of host innate responses
    • Rikihisa Y. Ehrlichia subversion of host innate responses. Curr Opin Microbiol 9 (2006) 95-101
    • (2006) Curr Opin Microbiol , vol.9 , pp. 95-101
    • Rikihisa, Y.1
  • 15
    • 33746921665 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum delays spontaneous human neutrophil apoptosis by modulation of multiple apoptotic pathways
    • Ge Y., and Rikihisa Y. Anaplasma phagocytophilum delays spontaneous human neutrophil apoptosis by modulation of multiple apoptotic pathways. Cell Microbiol 8 (2006) 1406-1416
    • (2006) Cell Microbiol , vol.8 , pp. 1406-1416
    • Ge, Y.1    Rikihisa, Y.2
  • 16
    • 12444278282 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum inhibits human neutrophil apoptosis via upregulation of bfl-1, maintenance of mitochondrial membrane potential and prevention of caspase 3 activation
    • Ge Y., Yoshiie K., Kuribayashi F., Lin M., and Rikihisa Y. Anaplasma phagocytophilum inhibits human neutrophil apoptosis via upregulation of bfl-1, maintenance of mitochondrial membrane potential and prevention of caspase 3 activation. Cell Microbiol 7 (2005) 29-38
    • (2005) Cell Microbiol , vol.7 , pp. 29-38
    • Ge, Y.1    Yoshiie, K.2    Kuribayashi, F.3    Lin, M.4    Rikihisa, Y.5
  • 17
    • 34248142208 scopus 로고    scopus 로고
    • High-cholesterol diet facilitates Anaplasma phagocytophilum infection and up-regulates macrophage inflammatory protein-2 and CXCR2 expression in apolipoprotein E-deficient mice
    • Xiong Q., Wang X., and Rikihisa Y. High-cholesterol diet facilitates Anaplasma phagocytophilum infection and up-regulates macrophage inflammatory protein-2 and CXCR2 expression in apolipoprotein E-deficient mice. J Infect Dis 195 (2007) 1497-1503
    • (2007) J Infect Dis , vol.195 , pp. 1497-1503
    • Xiong, Q.1    Wang, X.2    Rikihisa, Y.3
  • 18
    • 84891032102 scopus 로고    scopus 로고
    • Intracellular niches of Ehrlichia and Anaplasma
    • Schaible U., and Haas A. (Eds), Wiley-VCH Verlag GmbH & Co, KGaA, Weinheim
    • Rikihisa Y. Intracellular niches of Ehrlichia and Anaplasma. In: Schaible U., and Haas A. (Eds). Intracellular Niches of Microbes. A Pathogens Guide Through the Host Cell (2009), Wiley-VCH Verlag GmbH & Co, KGaA, Weinheim 301-314
    • (2009) Intracellular Niches of Microbes. A Pathogens Guide Through the Host Cell , pp. 301-314
    • Rikihisa, Y.1
  • 19
    • 38849200959 scopus 로고    scopus 로고
    • Subversion of cellular autophagy by Anaplasma phagocytophilum
    • Niu H., Yamaguchi M., and Rikihisa Y. Subversion of cellular autophagy by Anaplasma phagocytophilum. Cell Microbiol 10 (2008) 593-605
    • (2008) Cell Microbiol , vol.10 , pp. 593-605
    • Niu, H.1    Yamaguchi, M.2    Rikihisa, Y.3
  • 20
    • 0042825338 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival
    • Lin M., and Rikihisa Y. Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival. Infect Immun 71 (2003) 5324-5331
    • (2003) Infect Immun , vol.71 , pp. 5324-5331
    • Lin, M.1    Rikihisa, Y.2
  • 21
    • 63549109967 scopus 로고    scopus 로고
    • Cholesterol-dependent Anaplasma phagocytophilum exploits the low-density lipoprotein uptake pathway
    • Xiong Q., Lin M., and Rikihisa Y. Cholesterol-dependent Anaplasma phagocytophilum exploits the low-density lipoprotein uptake pathway. PLoS Pathog 5 (2009) e1000329
    • (2009) PLoS Pathog , vol.5
    • Xiong, Q.1    Lin, M.2    Rikihisa, Y.3
  • 22
    • 40449139085 scopus 로고    scopus 로고
    • Regulation of type IV secretion apparatus genes during Ehrlichia chaffeensis intracellular development by a previously unidentified protein
    • This study showed that transcription of all five virB/D loci is down-regulated before the release of E. chaffeensis from host THP-1 cells and is up-regulated at the initiation of exponential growth. An E. chaffeensis 12.3-kDa hypothetical protein (EcxR) binds to the promoter regions of these individual virB/D loci, and activates transcription of all five virB/D loci in LacZ reporter constructs.
    • Cheng Z., Wang X., and Rikihisa Y. Regulation of type IV secretion apparatus genes during Ehrlichia chaffeensis intracellular development by a previously unidentified protein. J Bacteriol 190 (2008) 2096-2105. This study showed that transcription of all five virB/D loci is down-regulated before the release of E. chaffeensis from host THP-1 cells and is up-regulated at the initiation of exponential growth. An E. chaffeensis 12.3-kDa hypothetical protein (EcxR) binds to the promoter regions of these individual virB/D loci, and activates transcription of all five virB/D loci in LacZ reporter constructs.
    • (2008) J Bacteriol , vol.190 , pp. 2096-2105
    • Cheng, Z.1    Wang, X.2    Rikihisa, Y.3
  • 23
    • 33644821065 scopus 로고    scopus 로고
    • Differential expression of VirB9 and VirB6 during the life cycle of Anaplasma phagocytophilum in human leucocytes is associated with differential binding and avoidance of lysosome pathway
    • Niu H., Rikihisa Y., Yamaguchi M., and Ohashi N. Differential expression of VirB9 and VirB6 during the life cycle of Anaplasma phagocytophilum in human leucocytes is associated with differential binding and avoidance of lysosome pathway. Cell Microbiol 8 (2006) 523-534
    • (2006) Cell Microbiol , vol.8 , pp. 523-534
    • Niu, H.1    Rikihisa, Y.2    Yamaguchi, M.3    Ohashi, N.4
  • 24
    • 0141446033 scopus 로고    scopus 로고
    • Sequence and expression analysis of virB9 of the type IV secretion system of Ehrlichia canis strains in ticks, dogs, and cultured cells
    • Felek S., Huang H., and Rikihisa Y. Sequence and expression analysis of virB9 of the type IV secretion system of Ehrlichia canis strains in ticks, dogs, and cultured cells. Infect Immun 71 (2003) 6063-6067
    • (2003) Infect Immun , vol.71 , pp. 6063-6067
    • Felek, S.1    Huang, H.2    Rikihisa, Y.3
  • 25
    • 58149490639 scopus 로고    scopus 로고
    • Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles
    • This study showed that all four virB6 paralogs (virB6-1, virB6-2, virB6-3, and virB6-4) that are 3-10-fold larger than A. tumefaciens virB6 are cotranscribed in THP-1 human leukemia and ISE6 tick cell cultures. VirB9 interacts with VirB6-1 and VirB6-2; VirB6-4 interacts with VirB6-1, VirB6-2, and VirB6-3; and VirB6-2 80-kDa fragment interacts with VirB6-3 and VirB6-4.
    • Bao W., Kumagai Y., Niu H., Yamaguchi M., Miura K., and Rikihisa Y. Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles. J Bacteriol 191 (2009) 278-286. This study showed that all four virB6 paralogs (virB6-1, virB6-2, virB6-3, and virB6-4) that are 3-10-fold larger than A. tumefaciens virB6 are cotranscribed in THP-1 human leukemia and ISE6 tick cell cultures. VirB9 interacts with VirB6-1 and VirB6-2; VirB6-4 interacts with VirB6-1, VirB6-2, and VirB6-3; and VirB6-2 80-kDa fragment interacts with VirB6-3 and VirB6-4.
    • (2009) J Bacteriol , vol.191 , pp. 278-286
    • Bao, W.1    Kumagai, Y.2    Niu, H.3    Yamaguchi, M.4    Miura, K.5    Rikihisa, Y.6
  • 27
    • 70350653834 scopus 로고    scopus 로고
    • Analysis of complete genome sequence of Neorickettsia risticii: causative agent of Potomac horse fever
    • Lin M., Zhang C., Gibson K., and Rikihisa Y. Analysis of complete genome sequence of Neorickettsia risticii: causative agent of Potomac horse fever. Nucleic Acids Res 37 (2009) 6076-6091
    • (2009) Nucleic Acids Res , vol.37 , pp. 6076-6091
    • Lin, M.1    Zhang, C.2    Gibson, K.3    Rikihisa, Y.4
  • 28
    • 34547640142 scopus 로고    scopus 로고
    • Surface-exposed proteins of Ehrlichia chaffeensis
    • Ge Y., and Rikihisa Y. Surface-exposed proteins of Ehrlichia chaffeensis. Infect Immun 75 (2007) 3833-3841
    • (2007) Infect Immun , vol.75 , pp. 3833-3841
    • Ge, Y.1    Rikihisa, Y.2
  • 29
    • 70350716934 scopus 로고    scopus 로고
    • The perplexing functions and surprising origins of Legionella pneumophila type IV secretion effectors
    • Franco I.S., Shuman H.A., and Charpentier X. The perplexing functions and surprising origins of Legionella pneumophila type IV secretion effectors. Cell Microbiol 11 (2009) 1435-1443
    • (2009) Cell Microbiol , vol.11 , pp. 1435-1443
    • Franco, I.S.1    Shuman, H.A.2    Charpentier, X.3
  • 30
    • 65549131958 scopus 로고    scopus 로고
    • Distinct activities of Bartonella henselae type IV secretion effector proteins modulate capillary-like sprout formation
    • Scheidegger F., Ellner Y., Guye P., Rhomberg T.A., Weber H., Augustin H.G., and Dehio C. Distinct activities of Bartonella henselae type IV secretion effector proteins modulate capillary-like sprout formation. Cell Microbiol 11 (2009) 1088-1101
    • (2009) Cell Microbiol , vol.11 , pp. 1088-1101
    • Scheidegger, F.1    Ellner, Y.2    Guye, P.3    Rhomberg, T.A.4    Weber, H.5    Augustin, H.G.6    Dehio, C.7
  • 31
    • 17344379177 scopus 로고    scopus 로고
    • Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion
    • Odenbreit S., Puls J., Sedlmaier B., Gerland E., Fischer W., and Haas R. Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion. Science 287 (2000) 1497-1500
    • (2000) Science , vol.287 , pp. 1497-1500
    • Odenbreit, S.1    Puls, J.2    Sedlmaier, B.3    Gerland, E.4    Fischer, W.5    Haas, R.6
  • 32
    • 0029113743 scopus 로고
    • Localization of the promoter for the ptl genes of Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin
    • Kotob S.I., Hausman S.Z., and Burns D.L. Localization of the promoter for the ptl genes of Bordetella pertussis, which encode proteins essential for secretion of pertussis toxin. Infect Immun 63 (1995) 3227-3230
    • (1995) Infect Immun , vol.63 , pp. 3227-3230
    • Kotob, S.I.1    Hausman, S.Z.2    Burns, D.L.3
  • 33
    • 67649836366 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens VirC2 enhances T-DNA transfer and virulence through its C-terminal ribbon-helix-helix DNA-binding fold
    • Lu J., den Dulk-Ras A., Hooykaas P.J., and Glover J.N. Agrobacterium tumefaciens VirC2 enhances T-DNA transfer and virulence through its C-terminal ribbon-helix-helix DNA-binding fold. Proc Natl Acad Sci U S A 106 (2009) 9643-9648
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 9643-9648
    • Lu, J.1    den Dulk-Ras, A.2    Hooykaas, P.J.3    Glover, J.N.4
  • 34
    • 33645865541 scopus 로고    scopus 로고
    • Type IV secretion systems and their effectors in bacterial pathogenesis
    • Backert S., and Meyer T.F. Type IV secretion systems and their effectors in bacterial pathogenesis. Curr Opin Microbiol 9 (2006) 207-217
    • (2006) Curr Opin Microbiol , vol.9 , pp. 207-217
    • Backert, S.1    Meyer, T.F.2
  • 35
    • 34547217380 scopus 로고    scopus 로고
    • Effector proteins translocated by Legionella pneumophila: strength in numbers
    • Ninio S., and Roy C.R. Effector proteins translocated by Legionella pneumophila: strength in numbers. Trends Microbiol 15 (2007) 372-380
    • (2007) Trends Microbiol , vol.15 , pp. 372-380
    • Ninio, S.1    Roy, C.R.2
  • 37
    • 14144249589 scopus 로고    scopus 로고
    • A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells
    • Nagai H., Cambronne E.D., Kagan J.C., Amor J.C., Kahn R.A., and Roy C.R. A C-terminal translocation signal required for Dot/Icm-dependent delivery of the Legionella RalF protein to host cells. Proc Natl Acad Sci U S A 102 (2005) 826-831
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 826-831
    • Nagai, H.1    Cambronne, E.D.2    Kagan, J.C.3    Amor, J.C.4    Kahn, R.A.5    Roy, C.R.6
  • 40
    • 34147154867 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection
    • The authors showed that a 190-kDa protein, AnkA, is increasingly tyrosine-phosphorylated in infected host cell. Recombinant AnkA can be phosphorylated by Src in vitro and AnkA expressed in COS-7 cells is tyrosine phosphorylation by Src in EPIYA motifs and AnkA binds to the host-cell phosphatase SHP-1 during early infection.
    • IJdo J., Carlson A.C., and Kennedy E.L. Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection. Cell Microbiol 9 (2007) 1284-1296. The authors showed that a 190-kDa protein, AnkA, is increasingly tyrosine-phosphorylated in infected host cell. Recombinant AnkA can be phosphorylated by Src in vitro and AnkA expressed in COS-7 cells is tyrosine phosphorylation by Src in EPIYA motifs and AnkA binds to the host-cell phosphatase SHP-1 during early infection.
    • (2007) Cell Microbiol , vol.9 , pp. 1284-1296
    • IJdo, J.1    Carlson, A.C.2    Kennedy, E.L.3
  • 41
    • 4143085008 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins
    • Park J., Kim K.J., Choi K.S., Grab D.J., and Dumler J.S. Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins. Cell Microbiol 6 (2004) 743-751
    • (2004) Cell Microbiol , vol.6 , pp. 743-751
    • Park, J.1    Kim, K.J.2    Choi, K.S.3    Grab, D.J.4    Dumler, J.S.5
  • 42
    • 66549089938 scopus 로고    scopus 로고
    • Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum
    • The authors reported that AnkA accumulates in nuclei of infected cells and interacts with transcriptional regulatory regions of the CYBB locus. AnkA binds to regions with high AT content. Histone H3 acetylation decreased at the CYBB locus during A. phagocytophilum infection. Transcription of CYBB and other defense genes is significantly decreased in AnkA-transfected HL-60 cells.
    • Garcia-Garcia J.C., Rennoll-Bankert K.E., Pelly S., Milstone A.M., and Dumler J.S. Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum. Infect Immun 77 (2009) 2385-2391. The authors reported that AnkA accumulates in nuclei of infected cells and interacts with transcriptional regulatory regions of the CYBB locus. AnkA binds to regions with high AT content. Histone H3 acetylation decreased at the CYBB locus during A. phagocytophilum infection. Transcription of CYBB and other defense genes is significantly decreased in AnkA-transfected HL-60 cells.
    • (2009) Infect Immun , vol.77 , pp. 2385-2391
    • Garcia-Garcia, J.C.1    Rennoll-Bankert, K.E.2    Pelly, S.3    Milstone, A.M.4    Dumler, J.S.5
  • 43
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L.K., Cammett T.J., Desrosiers D.C., and Peng Z.Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci 13 (2004) 1435-1448
    • (2004) Protein Sci , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 44
    • 27744546297 scopus 로고    scopus 로고
    • Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer
    • de Felipe K.S., Pampou S., Jovanovic O.S., Pericone C.D., Ye S.F., Kalachikov S., and Shuman H.A. Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. J Bacteriol 187 (2005) 7716-7726
    • (2005) J Bacteriol , vol.187 , pp. 7716-7726
    • de Felipe, K.S.1    Pampou, S.2    Jovanovic, O.S.3    Pericone, C.D.4    Ye, S.F.5    Kalachikov, S.6    Shuman, H.A.7
  • 45
    • 34249944112 scopus 로고    scopus 로고
    • The Orientia tsutsugamushi genome reveals massive proliferation of conjugative type IV secretion system and host-cell interaction genes
    • Cho N.H., Kim H.R., Lee J.H., Kim S.Y., Kim J., Cha S., Darby A.C., Fuxelius H.H., Yin J., Kim J.H., et al. The Orientia tsutsugamushi genome reveals massive proliferation of conjugative type IV secretion system and host-cell interaction genes. Proc Natl Acad Sci U S A 104 (2007) 7981-7986
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 7981-7986
    • Cho, N.H.1    Kim, H.R.2    Lee, J.H.3    Kim, S.Y.4    Kim, J.5    Cha, S.6    Darby, A.C.7    Fuxelius, H.H.8    Yin, J.9    Kim, J.H.10
  • 46
    • 21844441807 scopus 로고    scopus 로고
    • Distribution, expression, and motif variability of ankyrin domain genes in Wolbachia pipientis
    • Iturbe-Ormaetxe I., Burke G.R., Riegler M., and O'Neill S.L. Distribution, expression, and motif variability of ankyrin domain genes in Wolbachia pipientis. J Bacteriol 187 (2005) 5136-5145
    • (2005) J Bacteriol , vol.187 , pp. 5136-5145
    • Iturbe-Ormaetxe, I.1    Burke, G.R.2    Riegler, M.3    O'Neill, S.L.4
  • 49
    • 46249111623 scopus 로고    scopus 로고
    • Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors
    • Authors showed that Legionella pneumophila AnkX protein is secreted by T4S system and prevents microtubule-dependent vesicular transport to interfere with fusion of the L. pneumophila-containing vacuole with late endosomes after infection of macrophages.
    • Pan X., Luhrmann A., Satoh A., Laskowski-Arce M.A., and Roy C.R. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320 (2008) 1651-1654. Authors showed that Legionella pneumophila AnkX protein is secreted by T4S system and prevents microtubule-dependent vesicular transport to interfere with fusion of the L. pneumophila-containing vacuole with late endosomes after infection of macrophages.
    • (2008) Science , vol.320 , pp. 1651-1654
    • Pan, X.1    Luhrmann, A.2    Satoh, A.3    Laskowski-Arce, M.A.4    Roy, C.R.5
  • 50
    • 70349417835 scopus 로고    scopus 로고
    • Nuclear translocated Ehrlichia chaffeensis ankyrin protein interacts with a specific adenine-rich motif of host promoter and intronic Alu elements
    • This study reported that a 200-kDa AnkA of E. chaffeensis is detected in the nuclei of Ehrlichia-infected THP-1 cells. AnkA interacts host promoter and intronic Alu-Sx elements; a specific adenine-rich (mid A-stretch) motif. Genes (n = 456) with promoter Alu elements primarily related to transcription, apoptosis, ATPase activity and structural proteins associated with the nucleus and membrane-bound organelles are the targets of p200.
    • Zhu B., Nethery K.A., Kuriakose J.A., Wakeel A., Zhang X., and McBride J.W. Nuclear translocated Ehrlichia chaffeensis ankyrin protein interacts with a specific adenine-rich motif of host promoter and intronic Alu elements. Infect Immun 77 (2009) 4243-4255. This study reported that a 200-kDa AnkA of E. chaffeensis is detected in the nuclei of Ehrlichia-infected THP-1 cells. AnkA interacts host promoter and intronic Alu-Sx elements; a specific adenine-rich (mid A-stretch) motif. Genes (n = 456) with promoter Alu elements primarily related to transcription, apoptosis, ATPase activity and structural proteins associated with the nucleus and membrane-bound organelles are the targets of p200.
    • (2009) Infect Immun , vol.77 , pp. 4243-4255
    • Zhu, B.1    Nethery, K.A.2    Kuriakose, J.A.3    Wakeel, A.4    Zhang, X.5    McBride, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.