메뉴 건너뛰기




Volumn 8, Issue 5, 2010, Pages 328-339

Anaplasma phagocytophilum and Ehrlichia chaffeensis: Subversive manipulators of host cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1,3 FUCOSYLTRANSFERASE; BACTERIAL PROTEIN; DOXYCYCLINE; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE P38; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN F; OUTER SURFACE PROTEIN A; P SELECTIN GLYCOPROTEIN LIGAND 1; PEPTIDOGLYCAN; PROTEIN P28; PROTEIN P44; RNA 16S; X LINKED INHIBITOR OF APOPTOSIS;

EID: 77951097433     PISSN: 17401526     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrmicro2318     Document Type: Review
Times cited : (168)

References (150)
  • 1
    • 0011386679 scopus 로고
    • Anaplasma marginale (gen. and spec. nov.) the marginal points in the blood of cattle suffering from specific disease
    • Dept. Agr.
    • Theiler, A. Anaplasma marginale (gen. and spec. nov.) The marginal points in the blood of cattle suffering from specific disease. Transvaal S. Afr. Rep.Vet. Bacteriol. Dept. Agr. 1908-1909, 7-64 (1910).
    • (1910) Transvaal S. Afr. Rep.Vet. Bacteriol , vol.7 , Issue.64 , pp. 1908-1909
    • Theiler, A.1
  • 2
    • 70350468702 scopus 로고    scopus 로고
    • Current management of human granulocytic anaplasmosis, human monocytic ehrlichiosis and Ehrlichia ewingii ehrlichiosis
    • Thomas, R. J., Dumler, J. S. & Carlyon, J. A. Current management of human granulocytic anaplasmosis, human monocytic ehrlichiosis and Ehrlichia ewingii ehrlichiosis. Expert Rev. Anti Infect. Ther. 7, 709-722 (2009).
    • (2009) Expert Rev. Anti Infect. Ther. , vol.7 , pp. 709-722
    • Thomas, R.J.1    Dumler, J.S.2    Carlyon, J.A.3
  • 3
    • 0037240533 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis: A prototypical emerging pathogen
    • Paddock, C. D. & Childs, J. E. Ehrlichia chaffeensis: a prototypical emerging pathogen. Clin. Microbiol. Rev. 16, 37-64 (2003).
    • (2003) Clin. Microbiol. Rev. , vol.16 , pp. 37-64
    • Paddock, C.D.1    Childs, J.E.2
  • 6
    • 0038649210 scopus 로고    scopus 로고
    • National surveillance for the human ehrlichioses United States 1997-2001 and proposed methods for evaluation of data quality
    • Gardner, S. L., Holman, R. C., Krebs, J. W., Berkelman, R. & Childs, J. E. National surveillance for the human ehrlichioses in the United States, 1997-2001, and proposed methods for evaluation of data quality. Ann. N.Y. Acad. Sci. 990, 80-89 (2003).
    • (2003) Ann. N.Y. Acad. Sci. , vol.990 , pp. 80-89
    • Gardner, S.L.1    Holman, R.C.2    Krebs, J.W.3    Berkelman, R.4    Childs, J.E.5
  • 7
    • 68549139017 scopus 로고    scopus 로고
    • Sennetsu neorickettsiosis: A probable fish-borne cause of fever rediscovered in Laos
    • Newton, P. N. et al. Sennetsu neorickettsiosis: a probable fish-borne cause of fever rediscovered in Laos. Am. J. Trop. Med. Hyg. 81, 190-194 (2009).
    • (2009) Am. J. Trop. Med. Hyg. , vol.81 , pp. 190-194
    • Newton, P.N.1
  • 8
    • 33845738723 scopus 로고    scopus 로고
    • Human infection with Ehrlichia canis accompanied by clinical signs in Venezuela.
    • Perez, M., Bodor, M., Zhang, C., Xiong, Q. & Rikihisa, Y. Human infection with Ehrlichia canis accompanied by clinical signs in Venezuela. Ann. N.Y. Acad. Sci. 107 8, 110-117 (2006).
    • (2006) Ann. N.Y. Acad. Sci. , vol.107 , Issue.8 , pp. 110-117
    • Perez, M.1    Bodor, M.2    Zhang, C.3    Xiong, Q.4    Rikihisa, Y.5
  • 9
    • 0029740665 scopus 로고    scopus 로고
    • Ehrlichia canis-like agent isolated from a man in Venezuela: Antigenic and genetic characterization
    • Perez, M., Rikihisa, Y. & Wen, B. Ehrlichia canis-like agent isolated from a man in Venezuela: antigenic and genetic characterization. J. Clin. Microbiol. 34, 2133-2139 (1996).
    • (1996) J. Clin. Microbiol. , vol.34 , pp. 2133-2139
    • Perez, M.1    Rikihisa, Y.2    Wen, B.3
  • 10
    • 33745727549 scopus 로고    scopus 로고
    • Ehrlichia ruminantium: An emerging human pathogen?
    • Allsopp, M. T., Louw, M. & Meyer, E. C. Ehrlichia ruminantium: an emerging human pathogen? Ann. N.Y. Acad. Sci. 1063, 358-360 (2005).
    • (2005) Ann. N.Y. Acad. Sci. , vol.1063 , pp. 358-360
    • Allsopp, M.T.1    Louw, M.2    Meyer, E.C.3
  • 11
    • 31844445394 scopus 로고    scopus 로고
    • Ehrlichia subversion of host innate responses
    • Rikihisa, Y. Ehrlichia subversion of host innate responses. Curr. Opin. Microbiol. 9, 95-101 (2006).
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 95-101
    • Rikihisa, Y.1
  • 12
    • 74449083802 scopus 로고    scopus 로고
    • Molecular events involved in cellular invasion by Ehrlichia chaffeensis and Anaplasma phagocytophilum
    • Rikihisa, Y. Molecular events involved in cellular invasion by Ehrlichia chaffeensis and Anaplasma phagocytophilum. Vet. Parasitol. 167, 155-166 (2010).
    • (2010) Vet. Parasitol. , vol.167 , pp. 155-166
    • Rikihisa, Y.1
  • 13
    • 20144370399 scopus 로고    scopus 로고
    • Immunity to the ehrlichiae: New tools and recent developments
    • Winslow, G. M. & Bitsaktsis, C. Immunity to the ehrlichiae: new tools and recent developments. Curr. Opin. Infect. Dis. 18, 217-221 (2005).
    • (2005) Curr. Opin. Infect. Dis. , vol.18 , pp. 217-221
    • Winslow, G.M.1    Bitsaktsis, C.2
  • 14
    • 33644836708 scopus 로고    scopus 로고
    • Mechanisms of evasion of neutrophil killing by Anaplasma phagocytophilum
    • Carlyon, J. A. & Fikrig, E. Mechanisms of evasion of neutrophil killing by Anaplasma phagocytophilum. Curr. Opin. Hematol. 13, 28-33 (2006).
    • (2006) Curr. Opin. Hematol. , vol.13 , pp. 28-33
    • Carlyon, J.A.1    Fikrig, E.2
  • 15
    • 77951113461 scopus 로고    scopus 로고
    • Intracellular niches of microbes
    • eds Schaible, U. & Haas, A. Wiley-VCH, Weinheim
    • Rikihisa, Y. in Intracellular Niches of Microbes. A Pathogen's Guide Through the Host Cell (eds Schaible, U. & Haas, A.)
    • (2009) A Pathogen's Guide Through the Host Cell , pp. 301-314
    • Rikihisa, Y.1
  • 16
    • 0029294739 scopus 로고
    • Experimental transmission of Ehrlichia chaffeensis (Rickettsiales: Ehrlichieae) among white-tailed deer by Amblyomma americanum (Acari: Ixodidae)
    • Ewing, S. A. et al. Experimental transmission of Ehrlichia chaffeensis (Rickettsiales: Ehrlichieae) among white-tailed deer by Amblyomma americanum (Acari: Ixodidae). J. Med. Entomol. 32, 368-374 (1995).
    • (1995) J. Med. Entomol. , vol.32 , pp. 368-374
    • Ewing, S.A.1
  • 17
    • 0030003084 scopus 로고    scopus 로고
    • Perpetuation of the agent of human granulocytic ehrlichiosis in a deer tick-rodent cycle
    • 3rd et al
    • Telford, S. R. 3rd et al. Perpetuation of the agent of human granulocytic ehrlichiosis in a deer tick-rodent cycle. Proc. Natl Acad. Sci. USA 93, 6209-6214 (1996).
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 6209-6214
    • Telford, S.R.1
  • 18
    • 70350731142 scopus 로고    scopus 로고
    • Diagnosis of Ehrlichia ewingii infection by PCR in a puppy from Ohio
    • Gieg, J., Rikihisa, Y. & Wellman, M. Diagnosis of Ehrlichia ewingii infection by PCR in a puppy from Ohio. Vet. Clin. Pathol. 38, 406-410 (2009).
    • (2009) Vet. Clin. Pathol. , vol.38 , pp. 406-410
    • Gieg, J.1    Rikihisa, Y.2    Wellman, M.3
  • 19
    • 0033565959 scopus 로고    scopus 로고
    • Ehrlichia ewingii, a newly recognized agent of human ehrlichiosis
    • Buller, R. S. et al. Ehrlichia ewingii, a newly recognized agent of human ehrlichiosis. N. Engl. J. Med. 341, 148-155 (1999).
    • (1999) N. Engl. J. Med. , vol.341 , pp. 148-155
    • Buller, R.S.1
  • 20
    • 0036627626 scopus 로고    scopus 로고
    • Infection rates of Amblyomma americanum and Dermacentor variabilis by Ehrlichia chaffeensis and Ehrlichia ewingii in southwest Missouri
    • Steiert, J. G. & Gilfoy, F. Infection rates of Amblyomma americanum and Dermacentor variabilis by Ehrlichia chaffeensis and Ehrlichia ewingii in southwest Missouri. Vector Borne Zoonotic Dis. 2, 53-60 (2002).
    • (2002) Vector Borne Zoonotic Dis. , vol.2 , pp. 53-60
    • Steiert, J.G.1    Gilfoy, F.2
  • 21
    • 0025439243 scopus 로고
    • Experimental transmission of a granulocytic form of the tribe Ehrlichieae by Dermacentor variabilis and Amblyomma americanum to dogs
    • Anziani, O. S., Ewing, S. A. & Barker, R. W. Experimental transmission of a granulocytic form of the tribe Ehrlichieae by Dermacentor variabilis and Amblyomma americanum to dogs. Am. J. Vet. Res. 51, 929-931 (1990).
    • (1990) Am. J. Vet. Res. , vol.51 , pp. 929-931
    • Anziani, O.S.1    Ewing, S.A.2    Barker, R.W.3
  • 22
    • 56649117358 scopus 로고    scopus 로고
    • Nosocomial transmission of human granulocytic anaplasmosis in China
    • Zhang, L. et al. Nosocomial transmission of human granulocytic anaplasmosis in China. JAMA 300, 2263-2270 (2008).
    • (2008) JAMA , vol.300 , pp. 2263-2270
    • Zhang, L.1
  • 23
    • 56649088049 scopus 로고    scopus 로고
    • Nosocomial transmission of human granulocytic anaplasmosis?
    • Krause, P. J. & Wormser, G. P. Nosocomial transmission of human granulocytic anaplasmosis? JAMA 300, 2308-2309 (2008).
    • (2008) JAMA , vol.300 , pp. 2308-2309
    • Krause, P.J.1    Wormser, G.P.2
  • 24
    • 0042825338 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival
    • Lin, M. & Rikihisa, Y. Ehrlichia chaffeensis and Anaplasma phagocytophilum lack genes for lipid A biosynthesis and incorporate cholesterol for their survival. Infect. Immun. 71, 5324-5331 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 5324-5331
    • Lin, M.1    Rikihisa, Y.2
  • 25
    • 0034595997 scopus 로고    scopus 로고
    • Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand PSGL-1
    • Herron, M. J. et al. Intracellular parasitism by the human granulocytic ehrlichiosis bacterium through the P-selectin ligand, PSGL-1. Science 288, 1653-1656 (2000).
    • (2000) Science , vol.288 , pp. 1653-1656
    • Herron, M.J.1
  • 26
    • 33750621550 scopus 로고    scopus 로고
    • Characterization of a sialic acid-and P-selectin glycoprotein ligand-1-independent adhesin activity in the granulocytotropic bacterium Anaplasma phagocytophilum
    • Reneer, D. V. et al. Characterization of a sialic acid-and P-selectin glycoprotein ligand-1-independent adhesin activity in the granulocytotropic bacterium Anaplasma phagocytophilum. Cell. Microbiol. 8, 1972-1984 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 1972-1984
    • Reneer, D.V.1
  • 27
    • 2942654840 scopus 로고    scopus 로고
    • Infection of endothelial cells with Anaplasma marginale and A. phagocytophilum
    • Munderloh, U. G. et al. Infection of endothelial cells with Anaplasma marginale and A. phagocytophilum. Vet. Microbiol. 101, 53-64 (2004).
    • (2004) Vet. Microbiol. , vol.101 , pp. 53-64
    • Munderloh, U.G.1
  • 28
    • 0142214543 scopus 로고    scopus 로고
    • Murine neutrophils require α1,3-fucosylation but not PSGL-1 for productive infection with Anaplasma phagocytophilum
    • Carlyon, J. A. et al. Murine neutrophils require α1,3-fucosylation but not PSGL-1 for productive infection with Anaplasma phagocytophilum. Blood 102, 3387-3395 (2003).
    • (2003) Blood , vol.102 , pp. 3387-3395
    • Carlyon, J.A.1
  • 29
    • 0142217168 scopus 로고    scopus 로고
    • Obligatory intracellular parasitism by Ehrlichia chaffeensis and Anaplasma phagocytophilum involves caveolae and glycosylphosphatidylinositol- anchored proteins
    • Lin, M. & Rikihisa, Y. Obligatory intracellular parasitism by Ehrlichia chaffeensis and Anaplasma phagocytophilum involves caveolae and glycosylphosphatidylinositol-anchored proteins. Cell. Microbiol. 5, 809-820 (2003).
    • (2003) Cell. Microbiol. , vol.5 , pp. 809-820
    • Lin, M.1    Rikihisa, Y.2
  • 30
    • 0036181922 scopus 로고    scopus 로고
    • Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells
    • Mott, J., Rikihisa, Y. & Tsunawaki, S. Effects of Anaplasma phagocytophila on NADPH oxidase components in human neutrophils and HL-60 cells. Infect. Immun. 70, 1359-1366 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 1359-1366
    • Mott, J.1    Rikihisa, Y.2    Tsunawaki, S.3
  • 31
    • 3342959166 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection
    • Carlyon, J. A., Abdel-Latif, D., Pypaert, M., Lacy, P. & Fikrig, E. Anaplasma phagocytophilum utilizes multiple host evasion mechanisms to thwart NADPH oxidase-mediated killing during neutrophil infection. Infect. Immun. 72, 4772-4783 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 4772-4783
    • Carlyon, J.A.1    Abdel-Latif, D.2    Pypaert, M.3    Lacy, P.4    Fikrig, E.5
  • 32
    • 4544382411 scopus 로고    scopus 로고
    • Neutrophil NADPH oxidase is reduced at the Anaplasma phagocytophilum phagosome
    • IJdo, J. & Mueller, A. C. Neutrophil NADPH oxidase is reduced at the Anaplasma phagocytophilum phagosome. Infect. Immun. 72, 5392-5401 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 5392-5401
    • Ijdo, J.1    Mueller, A.C.2
  • 33
    • 33947101530 scopus 로고    scopus 로고
    • phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes
    • phox and inhibition of superoxide generation by Ehrlichia chaffeensis in human monocytes. Cell. Microbiol. 9, 861-874 (2007).
    • (2007) Cell. Microbiol. , vol.9 , pp. 861-874
    • Lin, M.1    Rikihisa, Y.2
  • 34
    • 0032080403 scopus 로고    scopus 로고
    • The agent of Human Granulocytic Ehrlichiosis resides in an endosomal compartment
    • Webster, P., IJdo, J. W., Chicoine, L. M. & Fikrig, E. The agent of Human Granulocytic Ehrlichiosis resides in an endosomal compartment. J. Clin. Invest. 101, 1932-1941 (1998).
    • (1998) J. Clin. Invest. , vol.101 , pp. 1932-1941
    • Webster, P.1    Ijdo, J.W.2    Chicoine, L.M.3    Fikrig, E.4
  • 35
    • 0033009747 scopus 로고    scopus 로고
    • Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells
    • Mott, J., Barnewall, R. E. & Rikihisa, Y. Human granulocytic ehrlichiosis agent and Ehrlichia chaffeensis reside in different cytoplasmic compartments in HL-60 cells. Infect. Immun. 67, 1368-1378 (1999).
    • (1999) Infect. Immun. , vol.67 , pp. 1368-1378
    • Mott, J.1    Barnewall, R.E.2    Rikihisa, Y.3
  • 36
    • 38849200959 scopus 로고    scopus 로고
    • Subversion of cellular autophagy by Anaplasma phagocytophilum
    • Niu, H., Yamaguchi, M. & Rikihisa, Y. Subversion of cellular autophagy by Anaplasma phagocytophilum. Cell. Microbiol. 10, 593-605 (2008).
    • (2008) Cell. Microbiol. , vol.10 , pp. 593-605
    • Niu, H.1    Yamaguchi, M.2    Rikihisa, Y.3
  • 37
    • 33645760951 scopus 로고    scopus 로고
    • Comparative genomics of emerging human ehrlichiosis agents
    • Dunning Hotopp, J. C. et al. Comparative genomics of emerging human ehrlichiosis agents. PLoS Genet. 2, e21 (2006).
    • (2006) PLoS Genet. , vol.2
    • Dunning Hotopp, J.C.1
  • 38
    • 63149160427 scopus 로고    scopus 로고
    • Host cell-free growth of the Q fever bacterium Coxiella burnetii
    • Omsland, A. et al. Host cell-free growth of the Q fever bacterium Coxiella burnetii. Proc. Natl Acad. Sci. USA 106, 4430-4434 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 4430-4434
    • Omsland, A.1
  • 39
    • 0032512051 scopus 로고    scopus 로고
    • The genome sequence of Rickettsia prowazekii and the origin of mitochondria
    • Andersson, S. G. et al. The genome sequence of Rickettsia prowazekii and the origin of mitochondria. Nature 396, 133-140 (1998).
    • (1998) Nature , vol.396 , pp. 133-140
    • Andersson, S.G.1
  • 40
    • 0032561496 scopus 로고    scopus 로고
    • Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis
    • Stephens, R. S. et al. Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis. Science 282, 754-759 (1998).
    • (1998) Science , vol.282 , pp. 754-759
    • Stephens, R.S.1
  • 41
    • 0038222539 scopus 로고    scopus 로고
    • Complete genome sequence of the Q-fever pathogen Coxiella burnetii
    • Seshadri, R. et al. Complete genome sequence of the Q-fever pathogen Coxiella burnetii. Proc. Natl Acad. Sci. USA 100, 5455-5460 (2003).
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 5455-5460
    • Seshadri, R.1
  • 42
    • 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. & Rikihisa, Y. Analysis of complete genome sequence of Neorickettsia risticii: causative agent of Potomac horse fever. Nucleic Acid Res. 37, 6076-6079 (2009).
    • (2009) Nucleic Acid Res. , vol.37 , pp. 6076-6079
    • Lin, M.1    Zhang, C.2    Gibson, K.3    Rikihisa, Y.4
  • 43
    • 21144432943 scopus 로고    scopus 로고
    • The Wolbachia genome of Brugia malayi: Endosymbiont evolution within a human pathogenic nematode
    • Foster, J. et al. The Wolbachia genome of Brugia malayi: endosymbiont evolution within a human pathogenic nematode. PLoS Biol. 3, e121 (2005).
    • (2005) PLoS Biol. , vol.3
    • Foster, J.1
  • 44
    • 19344378727 scopus 로고    scopus 로고
    • Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: A streamlined genome overrun by mobile genetic elements
    • Wu, M. et al. Phylogenomics of the reproductive parasite Wolbachia pipientis wMel: a streamlined genome overrun by mobile genetic elements. PLoS Biol. 2, e69 (2004).
    • (2004) PLoS Biol. , vol.2
    • Wu, M.1
  • 45
    • 14144250820 scopus 로고    scopus 로고
    • Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins
    • Brayton, K. A. et al. Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins. Proc. Natl Acad. Sci. USA 10 2, 844-849 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.10 , Issue.2 , pp. 844-849
    • Brayton, K.A.1
  • 46
    • 20044391604 scopus 로고    scopus 로고
    • The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number
    • Collins, N. E. et al. The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number. Proc. Natl Acad. Sci. USA 10 2, 838-843 (2005).
    • (2005) Proc. Natl Acad. Sci. USA , vol.10 , Issue.2 , pp. 838-843
    • Collins, N.E.1
  • 47
    • 33744820791 scopus 로고    scopus 로고
    • The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies
    • Mavromatis, K. et al. The genome of the obligately intracellular bacterium Ehrlichia canis reveals themes of complex membrane structure and immune evasion strategies. J. Bacteriol. 188, 4015-4023 (2006).
    • (2006) J. Bacteriol. , vol.188 , pp. 4015-4023
    • Mavromatis, K.1
  • 48
    • 0035860458 scopus 로고    scopus 로고
    • Mechanisms of evolution in Rickettsia conorii and R. prowazekii
    • Ogata, H. et al. Mechanisms of evolution in Rickettsia conorii and R. prowazekii. Science 293, 2093-2098 (2001).
    • (2001) Science , vol.293 , pp. 2093-2098
    • Ogata, H.1
  • 49
    • 33750917844 scopus 로고    scopus 로고
    • Transformation of Anaplasma phagocytophilum
    • Felsheim, R. F. et al. Transformation of Anaplasma phagocytophilum. BMC Biotechnol. 6, 42 (2006). This article describes the first transformation of A. phagocytophilum with the Himar transposase system.
    • (2006) BMC Biotechnol. , vol.6 , pp. 42
    • Felsheim, R.F.1
  • 50
    • 35648974248 scopus 로고    scopus 로고
    • Identification of novel surface proteins of Anaplasma phagocytophilum by affinity purification and proteomics
    • Ge, Y. & Rikihisa, Y. Identification of novel surface proteins of Anaplasma phagocytophilum by affinity purification and proteomics. J. Bacteriol. 189, 7819-7828 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 7819-7828
    • Ge, Y.1    Rikihisa, Y.2
  • 51
    • 34547640142 scopus 로고    scopus 로고
    • Surface-exposed proteins of Ehrlichia chaffeensis
    • Ge, Y. & Rikihisa, Y. Surface-exposed proteins of Ehrlichia chaffeensis. Infect. Immun. 75, 3833-3841 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 3833-3841
    • Ge, Y.1    Rikihisa, Y.2
  • 52
    • 0034764937 scopus 로고    scopus 로고
    • Western blot analysis of sera reactive to human monocytic ehrlichiosis and human granulocytic ehrlichiosis agents
    • Unver, A. et al. Western blot analysis of sera reactive to human monocytic ehrlichiosis and human granulocytic ehrlichiosis agents. J. Clin. Microbiol. 39, 3982-3986 (2001).
    • (2001) J. Clin. Microbiol. , vol.39 , pp. 3982-3986
    • Unver, A.1
  • 53
    • 0032728572 scopus 로고    scopus 로고
    • Western and dot blotting analyses of Ehrlichia chaffeensis indirect fluorescent-antibody assay-positive and-negative human sera by using native and recombinant E. chaffeensis and E. canis antigens
    • Unver, A. et al. Western and dot blotting analyses of Ehrlichia chaffeensis indirect fluorescent-antibody assay-positive and-negative human sera by using native and recombinant E. chaffeensis and E. canis antigens. J. Clin. Microbiol. 37, 3888-3895 (1999).
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 3888-3895
    • Unver, A.1
  • 54
    • 0031957208 scopus 로고    scopus 로고
    • Cloning and expression of the 44-kilodalton major outer membrane protein gene of the human granulocytic ehrlichiosis agent and application of the recombinant protein to serodiagnosis
    • Zhi, N. et al. Cloning and expression of the 44-kilodalton major outer membrane protein gene of the human granulocytic ehrlichiosis agent and application of the recombinant protein to serodiagnosis. J. Clin. Microbiol. 36, 1666-1673 (1998).
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 1666-1673
    • Zhi, N.1
  • 55
    • 0030803193 scopus 로고    scopus 로고
    • Comparison of major antigenic proteins of six strains of the human granulocytic ehrlichiosis agent by Western immunoblot analysis
    • Zhi, N., Rikihisa, Y., Kim, H. Y., Wormser, G. P. & Horowitz, H. W. Comparison of major antigenic proteins of six strains of the human granulocytic ehrlichiosis agent by Western immunoblot analysis. J. Clin. Microbiol. 35, 2606-2611 (1997).
    • (1997) J. Clin. Microbiol. , vol.35 , pp. 2606-2611
    • Zhi, N.1    Rikihisa, Y.2    Kim, H.Y.3    Wormser, G.P.4    Horowitz, H.W.5
  • 56
    • 0032836127 scopus 로고    scopus 로고
    • Serodiagnosis of human granulocytic ehrlichiosis by a recombinant HGE-44-based enzyme-linked immunosorbent assay
    • IJdo, J. W., Wu, C., Magnarelli, L. A. & Fikrig, E. Serodiagnosis of human granulocytic ehrlichiosis by a recombinant HGE-44-based enzyme-linked immunosorbent assay. J. Clin. Microbiol. 37, 3540-3544 (1999).
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 3540-3544
    • Ijdo, J.W.1    Wu, C.2    Magnarelli, L.A.3    Fikrig, E.4
  • 57
    • 0141669063 scopus 로고    scopus 로고
    • Mechanisms of variable p44 expression by Anaplasma phagocytophilum
    • Lin, Q., Rikihisa, Y., Ohashi, N. & Zhi, N. Mechanisms of variable p44 expression by Anaplasma phagocytophilum. Infect. Immun. 71, 5650-5661 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 5650-5661
    • Lin, Q.1    Rikihisa, Y.2    Ohashi, N.3    Zhi, N.4
  • 58
    • 0036702309 scopus 로고    scopus 로고
    • Analysis of sequences and loci of p44 homologs expressed by Anaplasma phagocytophila in acutely infected patients
    • Lin, Q. et al. Analysis of sequences and loci of p44 homologs expressed by Anaplasma phagocytophila in acutely infected patients. J. Clin. Microbiol. 40, 2981-2988 (2002).
    • (2002) J. Clin. Microbiol. , vol.40 , pp. 2981-2988
    • Lin, Q.1
  • 59
    • 0033580934 scopus 로고    scopus 로고
    • Multiple p44 genes encoding major outer membrane proteins are expressed in the human granulocytic ehrlichiosis agent
    • Zhi, N., Ohashi, N. & Rikihisa, Y. Multiple p44 genes encoding major outer membrane proteins are expressed in the human granulocytic ehrlichiosis agent. J. Biol. Chem. 274, 17828-17836 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 17828-17836
    • Zhi, N.1    Ohashi, N.2    Rikihisa, Y.3
  • 60
    • 0033789586 scopus 로고    scopus 로고
    • Antigenic variation of Anaplasma marginale by expression of MSP2 mosaics
    • Barbet, A. F., Lundgren, A., Yi, J., Rurangirwa, F. R. & Palmer, G. H. Antigenic variation of Anaplasma marginale by expression of MSP2 mosaics. Infect. Immun. 68, 6133-6138 (2000)
    • (2000) Infect. Immun. , vol.68 , pp. 6133-6138
    • Barbet, A.F.1    Lundgren, A.2    Yi, J.3    Rurangirwa, F.R.4    Palmer, G.H.5
  • 61
    • 0037378109 scopus 로고    scopus 로고
    • Expression of multiple outer membrane protein sequence variants from a single genomic locus of Anaplasma phagocytophilum
    • Barbet, A. F. et al. Expression of multiple outer membrane protein sequence variants from a single genomic locus of Anaplasma phagocytophilum. Infect. Immun. 71, 1706-1718 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 1706-1718
    • Barbet, A.F.1
  • 62
    • 23444434654 scopus 로고    scopus 로고
    • Establishment of cloned Anaplasma phagocytophilum and analysis of p44 gene conversion within an infected horse and infected SCID mice
    • Lin, Q. & Rikihisa, Y. Establishment of cloned Anaplasma phagocytophilum and analysis of p44 gene conversion within an infected horse and infected SCID mice. Infect. Immun. 73, 5106-5114 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 5106-5114
    • Lin, Q.1    Rikihisa, Y.2
  • 63
    • 33645547831 scopus 로고    scopus 로고
    • Analysis of involvement of the RecF pathway in p44 recombination in Anaplasma phagocytophilum and in Escherichia coli by using a plasmid carrying the p44 expression and p44 donor loci
    • Lin, Q., Zhang, C. & Rikihisa, Y. Analysis of involvement of the RecF pathway in p44 recombination in Anaplasma phagocytophilum and in Escherichia coli by using a plasmid carrying the p44 expression and p44 donor loci. Infect. Immun. 74, 2052-2062 (2006)
    • (2006) Infect. Immun. , vol.74 , pp. 2052-2062
    • Lin, Q.1    Zhang, C.2    Rikihisa, Y.3
  • 64
    • 9344261822 scopus 로고    scopus 로고
    • Rapid sequential changeover of expressed p44 genes during the acute phase of Anaplasma phagocytophilum infection in horses
    • Wang, X. et al. Rapid sequential changeover of expressed p44 genes during the acute phase of Anaplasma phagocytophilum infection in horses. Infect. Immun. 72, 6852-6859 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 6852-6859
    • Wang, X.1
  • 65
    • 72449167889 scopus 로고    scopus 로고
    • Variant-specific and diminishing immune responses towards the highly variable MSP2(P44) outer membrane protein of Anaplasma phagocytophilum during persistent infection in lambs
    • Granquist, E. G. et al. Variant-specific and diminishing immune responses towards the highly variable MSP2(P44) outer membrane protein of Anaplasma phagocytophilum during persistent infection in lambs. Vet. Immunol. Immunopathol. 133, 117-124 (2009).
    • (2009) Vet. Immunol. Immunopathol. , vol.133 , pp. 117-124
    • Granquist, E.G.1
  • 66
    • 37749023983 scopus 로고    scopus 로고
    • Outer membrane protein sequence variation in lambs experimentally infected with Anaplasma phagocytophilum
    • Granquist, E. G., Stuen, S., Lundgren, A. M., Braten, M. & Barbet, A. F. Outer membrane protein sequence variation in lambs experimentally infected with Anaplasma phagocytophilum. Infect. Immun. 76, 120-126 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 120-126
    • Granquist, E.G.1    Stuen, S.2    Lundgren, A.M.3    Braten, M.4    Barbet, A.F.5
  • 67
    • 43249114430 scopus 로고    scopus 로고
    • Dynamic transmission of numerous Anaplasma phagocytophilum genotypes among lambs in an infected sheep flock in an area of anaplasmosis endemicity
    • Ladbury, G. A. et al. Dynamic transmission of numerous Anaplasma phagocytophilum genotypes among lambs in an infected sheep flock in an area of anaplasmosis endemicity. J. Clin. Microbiol. 46, 1686-1691 (2008).
    • (2008) J. Clin. Microbiol. , vol.46 , pp. 1686-1691
    • Ladbury, G.A.1
  • 68
    • 42949116993 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum MSP2(P44)-18 predominates and is modified into multiple isoforms in human myeloid cells
    • Sarkar, M. et al. Anaplasma phagocytophilum MSP2(P44)-18 predominates and is modified into multiple isoforms in human myeloid cells. Infect. Immun. 76, 2090-2098 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 2090-2098
    • Sarkar, M.1
  • 69
    • 65449156907 scopus 로고    scopus 로고
    • Differential expression and glycosylation of Anaplasma phagocytophilum major surface protein 2 paralogs during cultivation in sialyl Lewis x-deficient host cells
    • Troese, M. J. et al. Differential expression and glycosylation of Anaplasma phagocytophilum major surface protein 2 paralogs during cultivation in sialyl Lewis x-deficient host cells. Infect. Immun. 77, 1746-1756 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 1746-1756
    • Troese, M.J.1
  • 70
    • 2942596226 scopus 로고    scopus 로고
    • Restricted changes in major surface protein-2 (msp2) transcription after prolonged in vitro passage of Anaplasma phagocytophilum
    • Scorpio, D. G., Caspersen, K., Ogata, H., Park, J. & Dumler, J. S. Restricted changes in major surface protein-2 (msp2) transcription after prolonged in vitro passage of Anaplasma phagocytophilum. BMC Microbiol. 4, 1 (2004).
    • (2004) BMC Microbiol. , vol.4 , pp. 1
    • Scorpio, D.G.1    Caspersen, K.2    Ogata, H.3    Park, J.4    Dumler, J.S.5
  • 71
    • 0036175313 scopus 로고    scopus 로고
    • Transcript heterogeneity of the p44 multigene family in a human granulocytic ehrlichiosis agent transmitted by ticks
    • Zhi, N. et al. Transcript heterogeneity of the p44 multigene family in a human granulocytic ehrlichiosis agent transmitted by ticks. Infect. Immun. 70, 1175-1184 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 1175-1184
    • Zhi, N.1
  • 72
    • 0842265986 scopus 로고    scopus 로고
    • Sequence analysis of p44 homologs expressed by Anaplasma phagocytophilum in infected ticks feeding on naive hosts and in mice infected by tick attachment
    • Felek, S., Telford, S. 3rd, Falco, R. C. & Rikihisa, Y. Sequence analysis of p44 homologs expressed by Anaplasma phagocytophilum in infected ticks feeding on naive hosts and in mice infected by tick attachment. Infect. Immun. 72, 659-666 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 659-666
    • Felek, S.1    Telford III, S.2    Falco, R.C.3    Rikihisa, Y.4
  • 73
    • 33750440807 scopus 로고    scopus 로고
    • Structure of the expression site reveals global diversity in MSP2 (P44) variants in Anaplasma phagocytophilum
    • Barbet, A. F. et al. Structure of the expression site reveals global diversity in MSP2 (P44) variants in Anaplasma phagocytophilum. Infect. Immun. 74, 6429-6437 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 6429-6437
    • Barbet, A.F.1
  • 74
    • 36749006069 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum p44 mRNA expression is differentially regulated in mammalian and tick host cells: Involvement of the DNA binding protein ApxR
    • Wang, X., Cheng, Z., Zhang, C., Kikuchi, T. & Rikihisa, Y. Anaplasma phagocytophilum p44 mRNA expression is differentially regulated in mammalian and tick host cells: involvement of the DNA binding protein ApxR. J. Bacteriol. 189, 8651-8659 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 8651-8659
    • Wang, X.1    Cheng, Z.2    Zhang, C.3    Kikuchi, T.4    Rikihisa, Y.5
  • 75
    • 34347388440 scopus 로고    scopus 로고
    • Proteomic identification of a novel Anaplasma phagocytophilum DNA binding protein that regulates a putative transcription factor
    • Wang, X., Kikuchi, T. & Rikihisa, Y. Proteomic identification of a novel Anaplasma phagocytophilum DNA binding protein that regulates a putative transcription factor. J. Bacteriol. 189, 4880-4886 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 4880-4886
    • Wang, X.1    Kikuchi, T.2    Rikihisa, Y.3
  • 76
    • 50849100137 scopus 로고    scopus 로고
    • Whole genome transcription profiling of Anaplasma phagocytophilum in human and tick host cells by tiling array analysis
    • Nelson, C. M. et al. Whole genome transcription profiling of Anaplasma phagocytophilum in human and tick host cells by tiling array analysis. BMC Genomics 9, 364 (2008).
    • (2008) BMC Genomics , vol.9 , pp. 364
    • Nelson, C.M.1
  • 77
    • 0035081047 scopus 로고    scopus 로고
    • Analysis of transcriptionally active gene clusters of major outer membrane protein multigene family in Ehrlichia canis and E. chaffeensis
    • DOI 10.1128/IAI.69.4.2083-2091.2001
    • Ohashi, N., Rikihisa, Y. & Unver, A. Analysis of transcriptionally active gene clusters of major outer membrane protein multigene family in Ehrlichia canis and E. chaffeensis. Infect. Immun. 69, 2083-2091 (2001). (Pubitemid 32239672)
    • (2001) Infection and Immunity , vol.69 , Issue.4 , pp. 2083-2091
    • Ohashi, N.1    Rikihisa, Y.2    Unver, A.3
  • 78
    • 42049107798 scopus 로고    scopus 로고
    • Identification of 19 polymorphic major outer membrane protein genes and their immunogenic peptides in Ehrlichia ewingii for use in a serodiagnostic assay
    • Zhang, C., Xiong, Q., Kikuchi, T. & Rikihisa, Y. Identification of 19 polymorphic major outer membrane protein genes and their immunogenic peptides in Ehrlichia ewingii for use in a serodiagnostic assay. Clin. Vaccine Immunol. 15, 402-411 (2008).
    • (2008) Clin. Vaccine Immunol. , vol.15 , pp. 402-411
    • Zhang, C.1    Xiong, Q.2    Kikuchi, T.3    Rikihisa, Y.4
  • 79
    • 1942456753 scopus 로고    scopus 로고
    • Characterization of a major outer membrane protein multigene family in Ehrlichia ruminantium
    • van Heerden, H., Collins, N. E., Brayton, K. A., Rademeyer, C. & Allsopp, B. A. Characterization of a major outer membrane protein multigene family in Ehrlichia ruminantium. Gene 330, 159-168 (2004).
    • (2004) Gene , vol.330 , pp. 159-168
    • Van Heerden, H.1    Collins, N.E.2    Brayton, K.A.3    Rademeyer, C.4    Allsopp, B.A.5
  • 80
    • 34447255930 scopus 로고    scopus 로고
    • Virulence potential of Ehrlichia chaffeensis strains of distinct genome sequences
    • Miura, K. & Rikihisa, Y. Virulence potential of Ehrlichia chaffeensis strains of distinct genome sequences. Infect. Immun. 75, 3604-3613 (2007).
    • (2007) Infect. Immun. , vol.75 , pp. 3604-3613
    • Miura, K.1    Rikihisa, Y.2
  • 82
    • 0037217289 scopus 로고    scopus 로고
    • Isolates determined by sequence analysis of the 28-kilodalton outer membrane protein genes and other regions of the genome
    • Isolates determined by sequence analysis of the 28-kilodalton outer membrane protein genes and other regions of the genome. Infect. Immun. 71, 187-195 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 187-195
  • 83
    • 0036130678 scopus 로고    scopus 로고
    • Antigenic variation of Ehrlichia chaffeensis resulting from differential expression of the 28-kilodalton protein gene family
    • Long, S. W. et al. Antigenic variation of Ehrlichia chaffeensis resulting from differential expression of the 28-kilodalton protein gene family. Infect. Immun. 70, 1824-1831 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 1824-1831
    • Long, S.W.1
  • 84
    • 0344507504 scopus 로고    scopus 로고
    • Genetic diversity of the 28-kilodalton outer membrane protein gene in human isolates of Ehrlichia chaffeensis
    • Yu, X. J., McBride, J. W. & Walker, D. H. Genetic diversity of the 28-kilodalton outer membrane protein gene in human isolates of Ehrlichia chaffeensis. J. Clin. Microbiol. 37, 1137-1143 (1999).
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 1137-1143
    • Yu, X.J.1    McBride, J.W.2    Walker, D.H.3
  • 85
    • 0036070770 scopus 로고    scopus 로고
    • The omp-1 major outer membrane multigene family of Ehrlichia chaffeensis is differentially expressed in canine and tick hosts
    • Unver, A., Rikihisa, Y., Stich, R. W., Ohashi, N. & Felek, S. The omp-1 major outer membrane multigene family of Ehrlichia chaffeensis is differentially expressed in canine and tick hosts. Infect. Immun. 70, 4701-4704 (2002).
    • (2002) Infect. Immun. , vol.70 , pp. 4701-4704
    • Unver, A.1    Rikihisa, Y.2    Stich, R.W.3    Ohashi, N.4    Felek, S.5
  • 86
    • 3342964429 scopus 로고    scopus 로고
    • Expression of members of the 28-kilodalton major outer membrane protein family of Ehrlichia chaffeensis during persistent infection
    • Zhang, J. Z., Guo, H., Winslow, G. M. & Yu, X. J. Expression of members of the 28-kilodalton major outer membrane protein family of Ehrlichia chaffeensis during persistent infection. Infect. Immun. 72, 4336-4343 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 4336-4343
    • Zhang, J.Z.1    Guo, H.2    Winslow, G.M.3    Yu, X.J.4
  • 87
    • 11044231152 scopus 로고    scopus 로고
    • Ehrlichia chaffeensis expresses macrophage-and tick cell-specific 28-kilodalton outer membrane proteins
    • Singu, V., Liu, H., Cheng, C. & Ganta, R. R. Ehrlichia chaffeensis expresses macrophage-and tick cell-specific 28-kilodalton outer membrane proteins. Infect. Immun. 73, 79-87 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 79-87
    • Singu, V.1    Liu, H.2    Cheng, C.3    Ganta, R.R.4
  • 88
    • 0034832883 scopus 로고    scopus 로고
    • Transcriptional analysis of p30 major outer membrane multigene family of Ehrlichia canis in dogs, ticks, and cell culture at different temperatures
    • Unver, A. et al. Transcriptional analysis of p30 major outer membrane multigene family of Ehrlichia canis in dogs, ticks, and cell culture at different temperatures. Infect. Immun. 69, 6172-6178 (2001).
    • (2001) Infect. Immun. , vol.69 , pp. 6172-6178
    • Unver, A.1
  • 89
    • 0031717461 scopus 로고    scopus 로고
    • Characterization of monoclonal antibodies to the 44-kilodalton major outer membrane protein of the human granulocytic ehrlichiosis agent
    • Kim, H. Y. & Rikihisa, Y. Characterization of monoclonal antibodies to the 44-kilodalton major outer membrane protein of the human granulocytic ehrlichiosis agent. J. Clin. Microbiol. 36, 3278-3284 (1998).
    • (1998) J. Clin. Microbiol. , vol.36 , pp. 3278-3284
    • Kim, H.Y.1    Rikihisa, Y.2
  • 90
    • 33644784687 scopus 로고    scopus 로고
    • Two monoclonal antibodies with defined epitopes of P44 major surface proteins neutralize Anaplasma phagocytophilum by distinct mechanisms
    • Wang, X., Kikuchi, T. & Rikihisa, Y. Two monoclonal antibodies with defined epitopes of P44 major surface proteins neutralize Anaplasma phagocytophilum by distinct mechanisms. Infect. Immun. 74, 1873-1882 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 1873-1882
    • Wang, X.1    Kikuchi, T.2    Rikihisa, Y.3
  • 91
    • 0037972480 scopus 로고    scopus 로고
    • Major surface protein 2 of Anaplasma phagocytophilum facilitates adherence to granulocytes
    • DOI 10.1128/IAI.71.7.4018-4025.2003
    • Park, J., Choi, K. S. & Dumler, J. S. Major surface protein 2 of Anaplasma phagocytophilum facilitates adherence to granulocytes. Infect. Immun. 71, 4018-4025 (2003). (Pubitemid 36753728)
    • (2003) Infection and Immunity , vol.71 , Issue.7 , pp. 4018-4025
    • Park, J.1    Choi, K.S.2    Dumler, J.S.3
  • 92
    • 0031976047 scopus 로고    scopus 로고
    • Immunodominant major outer membrane proteins of Ehrlichia chaffeensis are encoded by a polymorphic multigene family
    • Ohashi, N., Zhi, N., Zhang, Y. & Rikihisa, Y. Immunodominant major outer membrane proteins of Ehrlichia chaffeensis are encoded by a polymorphic multigene family. Infect. Immun. 66, 132-139 (1998).
    • (1998) Infect. Immun. , vol.66 , pp. 132-139
    • Ohashi, N.1    Zhi, N.2    Zhang, Y.3    Rikihisa, Y.4
  • 93
    • 0036681845 scopus 로고    scopus 로고
    • Antibodies highly effective in SCID mice during infection by the intracellular bacterium Ehrlichia chaffeensis are of picomolar affinity and exhibit preferential epitope and isotype utilization
    • Li, J. S., Chu, F., Reilly, A. & Winslow, G. M. Antibodies highly effective in SCID mice during infection by the intracellular bacterium Ehrlichia chaffeensis are of picomolar affinity and exhibit preferential epitope and isotype utilization. J. Immunol. 169, 1419-1425 (2002).
    • (2002) J. Immunol. , vol.169 , pp. 1419-1425
    • Li, J.S.1    Chu, F.2    Reilly, A.3    Winslow, G.M.4
  • 94
    • 0034060810 scopus 로고    scopus 로고
    • Antibody-mediated elimination of the obligate intracellular bacterial pathogen Ehrlichia chaffeensis during active infection
    • Winslow, G. M. et al. Antibody-mediated elimination of the obligate intracellular bacterial pathogen Ehrlichia chaffeensis during active infection. Infect. Immun. 68, 2187-2195 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 2187-2195
    • Winslow, G.M.1
  • 95
    • 47049114343 scopus 로고    scopus 로고
    • And porin activity of P28 and OMP-1F during intracellular Ehrlichia chaffeensis development
    • Kumagai, Y., Huang, H. & Rikihisa, Y. Expression and porin activity of P28 and OMP-1F during intracellular Ehrlichia chaffeensis development. J. Bacteriol. 190, 3597-3605 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 3597-3605
    • Kumagai, Y.1    Huang, H.2    Expression, R.Y.3
  • 96
    • 33947410383 scopus 로고    scopus 로고
    • Porin activity of Anaplasma phagocytophilum outer membrane fraction and purified P44
    • Huang, H., Wang, X., Kikuchi, T., Kumagai, Y. & Rikihisa, Y. Porin activity of Anaplasma phagocytophilum outer membrane fraction and purified P44. J. Bacteriol. 189, 1998-2006 (2007).
    • (2007) J. Bacteriol. , vol.189 , pp. 1998-2006
    • Huang, H.1    Wang, X.2    Kikuchi, T.3    Kumagai, Y.4    Rikihisa, Y.5
  • 97
    • 28244436432 scopus 로고    scopus 로고
    • Molecular architecture and function of the Omp85 family of proteins
    • Gentle, I. E., Burri, L. & Lithgow, T. Molecular architecture and function of the Omp85 family of proteins. Mol. Microbiol. 58, 1216-1225 (2005).
    • (2005) Mol. Microbiol. , vol.58 , pp. 1216-1225
    • Gentle, I.E.1    Burri, L.2    Lithgow, T.3
  • 98
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M. & Tommassen, J. Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299, 262-265 (2003).
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 99
    • 0033823329 scopus 로고    scopus 로고
    • The 120 kDa outer membrane protein of Ehrlichia chaffeensis: Preferential expression on dense-core cells and gene expression in Escherichia coli associated with attachment and entry
    • Popov, V. L., Yu, X. & Walker, D. H. The 120 kDa outer membrane protein of Ehrlichia chaffeensis: preferential expression on dense-core cells and gene expression in Escherichia coli associated with attachment and entry. Microb. Pathog. 28, 71-80 (2000).
    • (2000) Microb. Pathog. , vol.28 , pp. 71-80
    • Popov, V.L.1    Yu, X.2    Walker, D.H.3
  • 100
    • 29644434935 scopus 로고    scopus 로고
    • Differentially expressed and secreted major immunoreactive protein orthologs of Ehrlichia canis and E. chaffeensis elicit early antibody responses to epitopes on glycosylated tandem repeats
    • Doyle, C. K., Nethery, K. A., Popov, V. L. & McBride, J. W. Differentially expressed and secreted major immunoreactive protein orthologs of Ehrlichia canis and E. chaffeensis elicit early antibody responses to epitopes on glycosylated tandem repeats. Infect. Immun. 74, 711-720 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 711-720
    • Doyle, C.K.1    Nethery, K.A.2    Popov, V.L.3    McBride, J.W.4
  • 101
    • 42149191556 scopus 로고    scopus 로고
    • A variable-length PCR target protein of Ehrlichia chaffeensis contains major species-specific antibody epitopes in acidic serine-rich tandem repeats
    • Luo, T., Zhang, X., Wakeel, A., Popov, V. L. & McBride, J. W. A variable-length PCR target protein of Ehrlichia chaffeensis contains major species-specific antibody epitopes in acidic serine-rich tandem repeats. Infect. Immun. 76, 1572-1580 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 1572-1580
    • Luo, T.1    Zhang, X.2    Wakeel, A.3    Popov, V.L.4    McBride, J.W.5
  • 102
    • 0034702879 scopus 로고    scopus 로고
    • A conserved, transcriptionally active p28 multigene locus of Ehrlichia canis
    • McBride, J. W., Yu, X. J. & Walker, D. H. A conserved, transcriptionally active p28 multigene locus of Ehrlichia canis. Gene 254, 245-252 (2000).
    • (2000) Gene , vol.254 , pp. 245-252
    • McBride, J.W.1    Yu, X.J.2    Walker, D.H.3
  • 103
    • 0033984293 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the 120-kilodalton protein gene of Ehrlichia canis and application of the recombinant 120-kilodalton protein for serodiagnosis of canine ehrlichiosis
    • Yu, X. J., McBride, J. W., Diaz, C. M. & Walker, D. H. Molecular cloning and characterization of the 120-kilodalton protein gene of Ehrlichia canis and application of the recombinant 120-kilodalton protein for serodiagnosis of canine ehrlichiosis. J. Clin. Microbiol. 38, 369-374 (2000).
    • (2000) J. Clin. Microbiol. , vol.38 , pp. 369-374
    • Yu, X.J.1    McBride, J.W.2    Diaz, C.M.3    Walker, D.H.4
  • 104
    • 0033985107 scopus 로고    scopus 로고
    • Glycosylation of homologous immunodominant proteins of Ehrlichia chaffeensis and Ehrlichia canis
    • McBride, J. W., Yu, X. J. & Walker, D. H. Glycosylation of homologous immunodominant proteins of Ehrlichia chaffeensis and Ehrlichia canis. Infect. Immun. 68, 13-18 (2000).
    • (2000) Infect. Immun. , vol.68 , pp. 13-18
    • McBride, J.W.1    Yu, X.J.2    Walker, D.H.3
  • 105
    • 67650410438 scopus 로고    scopus 로고
    • Major species-specific antibody epitopes of the Ehrlichia chaffeensis p120 and E. canis p140 orthologs in surface-exposed tandem repeat regions
    • Luo, T., Zhang, X. & McBride, J. W. Major species-specific antibody epitopes of the Ehrlichia chaffeensis p120 and, E. canis p140 orthologs in surface-exposed tandem repeat regions. Clin. Vaccine Immunol. 16, 982-990 (2009).
    • (2009) Clin. Vaccine Immunol. , vol.16 , pp. 982-990
    • Luo, T.1    Zhang, X.2    McBride, J.W.3
  • 106
    • 48849086594 scopus 로고    scopus 로고
    • Proteomic analysis of and immune responses to Ehrlichia chaffeensis lipoproteins
    • Huang, H. et al. Proteomic analysis of and immune responses to Ehrlichia chaffeensis lipoproteins. Infect. Immun. 76, 3405-3414 (2008).
    • (2008) Infect. Immun. , vol.76 , pp. 3405-3414
    • Huang, H.1
  • 107
    • 0025777206 scopus 로고
    • The tribe Ehrlichieae and ehrlichial diseases
    • Rikihisa, Y. The tribe Ehrlichieae and ehrlichial diseases. Clin. Microbiol. Rev. 4, 286-308 (1991).
    • (1991) Clin. Microbiol. Rev. , vol.4 , pp. 286-308
    • Rikihisa, Y.1
  • 108
    • 70449573110 scopus 로고    scopus 로고
    • Inoculation of white-tailed deer (Odocoileus virginianus) with Ap-V1 or NY-18 strains of Anaplasma phagocytophilum and microscopic demonstration of Ap-V1 in Ixodes scapularis adults that acquired infection from deer as nymphs
    • Reichard, M. V. et al. Inoculation of white-tailed deer (Odocoileus virginianus) with Ap-V1 or NY-18 strains of Anaplasma phagocytophilum and microscopic demonstration of Ap-V1 In Ixodes scapularis adults that acquired infection from deer as nymphs. Vector Borne Zoonotic Dis. 9, 565-568 (2009).
    • (2009) Vector Borne Zoonotic Dis. , vol.9 , pp. 565-568
    • Reichard, M.V.1
  • 109
    • 0020378290 scopus 로고
    • Stages in the development of Cytoecetes phagocytophila, the causative agent of tick-borne fever
    • DOI 10.1016/0021-9975(82)90033-0
    • Woldehiwet, Z. & Scott, G. R. Stages in the development of Cytoecetes phagocytophila, the causative agent of tick-borne fever. J. Comp. Pathol. 92, 469-474 (1982). (Pubitemid 13246722)
    • (1982) Journal of Comparative Pathology , vol.92 , Issue.3 , pp. 469-474
    • Woldehiwet, Z.1    Scott, G.R.2
  • 110
    • 0028788919 scopus 로고
    • Ultrastructural variation of cultured Ehrlichia chaffeensis
    • Popov, V. L., Chen, S. M., Feng, H. M. & Walker, D. H. Ultrastructural variation of cultured Ehrlichia chaffeensis. J. Med. Microbiol. 43, 411-421 (1995).
    • (1995) J. Med. Microbiol. , vol.43 , pp. 411-421
    • Popov, V.L.1    Chen, S.M.2    Feng, H.M.3    Walker, D.H.4
  • 111
    • 0032812655 scopus 로고    scopus 로고
    • Invasion and intracellular development of the human granulocytic ehrlichiosis agent in tick cell culture
    • Munderloh, U. G. et al. Invasion and intracellular development of the human granulocytic ehrlichiosis agent in tick cell culture. J. Clin. Microbiol. 37, 2518-2524 (1999).
    • (1999) J. Clin. Microbiol. , vol.37 , pp. 2518-2524
    • Munderloh, U.G.1
  • 112
    • 69049095022 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum dense-cored organisms mediate cellular adherence through recognition of human P-selectin glycoprotein ligand 1
    • Troese, M. J. & Carlyon, J. A. Anaplasma phagocytophilum dense-cored organisms mediate cellular adherence through recognition of human P-selectin glycoprotein ligand 1. Infect. Immun. 77, 4018-4027 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 4018-4027
    • Troese, M.J.1    Carlyon, J.A.2
  • 113
    • 33846934966 scopus 로고    scopus 로고
    • The developmental cycle of Ehrlichia chaffeensis in vertebrate cells
    • Zhang, J. Z., Popov, V. L., Gao, S., Walker, D. H. & Yu, X. J. The developmental cycle of Ehrlichia chaffeensis in vertebrate cells. Cell. Microbiol. 9, 610-618 (2007).
    • (2007) Cell. Microbiol. , vol.9 , pp. 610-618
    • Zhang, J.Z.1    Popov, V.L.2    Gao, S.3    Walker, D.H.4    Yu, X.J.5
  • 114
    • 0001819296 scopus 로고
    • eds Burgdorfer W. & Anacker R. L. Academic Press, New York
    • Ito, S. & Rikihisa, Y. inRickettsiae and Rickettsial Diseases (eds Burgdorfer, W. & Anacker, R. L.) 213-227 (Academic Press, New York, 1981).
    • (1981) InRickettsiae and Rickettsial Diseases , pp. 213-227
    • Ito, S.1    Rikihisa, Y.2
  • 115
    • 40449139085 scopus 로고    scopus 로고
    • Regulation of type IV secretion apparatus genes during Ehrlichia chaffeensis intracellular development by a previously unidentified protein
    • Cheng, Z., Wang, X. & Rikihisa, Y. Regulation of type IV secretion apparatus genes during Ehrlichia chaffeensis intracellular development by a previously unidentified protein. J. Bacteriol. 190, 2096-2105 (2008).
    • (2008) J. Bacteriol. , vol.190 , pp. 2096-2105
    • Cheng, Z.1    Wang, X.2    Rikihisa, Y.3
  • 116
    • 63449138218 scopus 로고    scopus 로고
    • The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic di-GMP in host cell infection
    • Lai, T. H., Kumagai, Y., Hyodo, M., Hayakawa, Y. & Rikihisa, Y. The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic di-GMP in host cell infection. J. Bacteriol. 191, 693-700 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 693-700
    • Lai, T.H.1    Kumagai, Y.2    Hyodo, M.3    Hayakawa, Y.4    Rikihisa, Y.5
  • 117
    • 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. & 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, 523-534 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 523-534
    • Niu, H.1    Rikihisa, Y.2    Yamaguchi, M.3    Ohashi, N.4
  • 118
    • 0029784238 scopus 로고    scopus 로고
    • A developmental stage-specific histone H1 homolog of Coxiella burnetii
    • Heinzen, R. A. & Hackstadt, T. A developmental stage-specific histone H1 homolog of Coxiella burnetii. J. Bacteriol. 178, 5049-5052 (1996).
    • (1996) J. Bacteriol. , vol.178 , pp. 5049-5052
    • Heinzen, R.A.1    Hackstadt, T.2
  • 119
    • 0025870123 scopus 로고
    • Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1
    • Hackstadt, T., Baehr, W. & Ying, Y. Chlamydia trachomatis developmentally regulated protein is homologous to eukaryotic histone H1. Proc. Natl Acad. Sci. USA 88, 3937-3941 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 3937-3941
    • Hackstadt, T.1    Baehr, W.2    Ying, Y.3
  • 120
    • 33745771590 scopus 로고    scopus 로고
    • Intra-leukocyte expression of two-component systems in Ehrlichia chaffeensis and Anaplasma phagocytophilum and effects of the histidine kinase inhibitor closantel
    • Cheng, Z., Kumagai, Y., Lin, M., Zhang, C. & Rikihisa, Y. Intra-leukocyte expression of two-component systems in Ehrlichia chaffeensis and Anaplasma phagocytophilum and effects of the histidine kinase inhibitor closantel. Cell. Microbiol. 8, 1241-1252 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 1241-1252
    • Cheng, Z.1    Kumagai, Y.2    Lin, M.3    Zhang, C.4    Rikihisa, Y.5
  • 121
    • 33748045474 scopus 로고    scopus 로고
    • Biochemical activities of three pairs of Ehrlichia chaffeensis two-component regulatory system proteins involved in inhibition of lysosomal fusion
    • Kumagai, Y., Cheng, Z., Lin, M. & Rikihisa, Y. Biochemical activities of three pairs of Ehrlichia chaffeensis two-component regulatory system proteins involved in inhibition of lysosomal fusion. Infect. Immun. 74, 5014-5022 (2006).
    • (2006) Infect. Immun. , vol.74 , pp. 5014-5022
    • Kumagai, Y.1    Cheng, Z.2    Lin, M.3    Rikihisa, Y.4
  • 122
    • 63449126394 scopus 로고    scopus 로고
    • Cyclic di-GMP (c-di-GMP) goes into host cells\c-di-GMP signaling in the obligate intracellular pathogen Anaplasma phagocytophilum
    • Romling, U. Cyclic di-GMP (c-di-GMP) goes into host cells\c-di-GMP signaling in the obligate intracellular pathogen Anaplasma phagocytophilum. J. Bacteriol. 191, 683-686 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 683-686
    • Romling, U.1
  • 123
    • 71449116162 scopus 로고    scopus 로고
    • Biological diversities of prokaryotic type IV secretion systems. Microbiol
    • Alvarez-Marinez, C. E. & Christie, P. J. C. Biological diversities of prokaryotic type IV secretion systems. Microbiol. Mol. Biol. Rev. 73, 775-808 (2009).
    • (2009) Mol. Biol. Rev. , vol.73 , pp. 775-808
    • Alvarez-Marinez, C.E.1    Christie, P.J.C.2
  • 124
    • 75249092539 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum and Ehrlichia chaffeensis type IV secretion and Ank proteins
    • Rikihisa, Y. & Lin, M. Anaplasma phagocytophilum and Ehrlichia chaffeensis type IV secretion and Ank proteins. Curr. Opin. Microbiol. 13, 59-66 (2010).
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 59-66
    • Rikihisa, Y.1    Lin, M.2
  • 125
    • 58149490639 scopus 로고    scopus 로고
    • Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles
    • Bao, W. et al. Four VirB6 paralogs and VirB9 are expressed and interact in Ehrlichia chaffeensis-containing vacuoles. J. Bacteriol. 191, 278-286 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 278-286
    • Bao, W.1
  • 126
    • 34848862803 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection
    • Lin, M., den Dulk-Ras, A., Hooykaas, P. J. & Rikihisa, Y. Anaplasma phagocytophilum AnkA secreted by type IV secretion system is tyrosine phosphorylated by Abl-1 to facilitate infection. Cell. Microbiol. 9, 2644-2657 (2007)
    • (2007) Cell. Microbiol. , vol.9 , pp. 2644-2657
    • Lin, M.1    Den Dulk-Ras, A.2    Hooykaas, P.J.3    Rikihisa, Y.4
  • 127
    • 34147154867 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection
    • IJdo, J., Carlson, A. C. & Kennedy, E. L. Anaplasma phagocytophilum AnkA is tyrosine-phosphorylated at EPIYA motifs and recruits SHP-1 during early infection. Cell. Microbiol. 9, 1284-1296 (2007).
    • (2007) Cell. Microbiol. , vol.9 , pp. 1284-1296
    • Ijdo, J.1    Carlson, A.C.2    Kennedy, E.L.3
  • 128
    • 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. & Dumler, J. S. Anaplasma phagocytophilum AnkA binds to granulocyte DNA and nuclear proteins. Cell. Microbiol. 6, 743-751 (2004).
    • (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
  • 129
    • 66549089938 scopus 로고    scopus 로고
    • Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum
    • Garcia-Garcia, J. C., Rennoll-Bankert, K. E., Pelly, S., Milstone, A. M. & Dumler, J. S. Silencing of host cell CYBB gene expression by the nuclear effector AnkA of the intracellular pathogen Anaplasma phagocytophilum. Infect. Immun. 77, 2385-2391 (2009).
    • (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
  • 130
    • 67650886021 scopus 로고    scopus 로고
    • Epigenetic silencing of host cell defense genes enhances intracellular survival of the rickettsial pathogen Anaplasma phagocytophilum
    • Garcia-Garcia, J. C., Barat, N. C., Trembley, S. J. & Dumler, J. S. Epigenetic silencing of host cell defense genes enhances intracellular survival of the rickettsial pathogen Anaplasma phagocytophilum. PLoS Path. 5, e1000488 (2009)
    • (2009) PLoS Path. , vol.5
    • Garcia-Garcia, J.C.1    Barat, N.C.2    Trembley, S.J.3    Dumler, J.S.4
  • 131
    • 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
    • Zhu, B. et al. Nuclear translocated Ehrlichia chaffeensis ankyrin protein interacts with a specific adenine-rich motif of host promoter and intronic Alu elements. Infect. Immun. 77, 4243-4255 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 4243-4255
    • Zhu, B.1
  • 132
    • 46249111623 scopus 로고    scopus 로고
    • Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors
    • Pan, X., Luhrmann, A., Satoh, A., Laskowski-Arce, M. A. & Roy., C. R. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320, 1651-1654 (2008).
    • (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
  • 133
    • 65449163095 scopus 로고    scopus 로고
    • An Ehrlichia chaffeensis tandem repeat protein interacts with multiple host targets involved in cell signaling, transcriptional regulation, and vesicle trafficking
    • Wakeel, A., Kuriakose, J. A. & McBride, J. W. An Ehrlichia chaffeensis tandem repeat protein interacts with multiple host targets involved in cell signaling, transcriptional regulation, and vesicle trafficking. Infect. Immun. 77, 1734-1745 (2009).
    • (2009) Infect. Immun. , vol.77 , pp. 1734-1745
    • Wakeel, A.1    Kuriakose, J.A.2    McBride, J.W.3
  • 134
    • 0033969660 scopus 로고    scopus 로고
    • Intracellular infection by the human granulocytic ehrlichiosis agent inhibits human neutrophil apoptosis
    • DOI 10.1128/IAI.68.3.1125-1133.2000
    • Yoshiie, K., Kim, H. Y., Mott, J. & Rikihisa, Y. Intracellular infection by the human granulocytic ehrlichiosis agent inhibits human neutrophil apoptosis. Infect. Immun. 68, 1125-1133 (2000). (Pubitemid 30108500)
    • (2000) Infection and Immunity , vol.68 , Issue.3 , pp. 1125-1133
    • Yoshiie, K.1    Kim, H.-Y.2    Mott, J.3    Rikihisa, Y.4
  • 135
    • 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. & 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, 29-38 (2005).
    • (2005) Cell. Microbiol. , vol.7 , pp. 29-38
    • Ge, Y.1    Yoshiie, K.2    Kuribayashi, F.3    Lin, M.4    Rikihisa, Y.5
  • 136
    • 0344405661 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum reduces neutrophil apoptosis in vivo
    • Scaife, H., Woldehiwet, Z., Hart, C. A. & Edwards, S. W. Anaplasma phagocytophilum reduces neutrophil apoptosis in vivo. Infect. Immun. 71, 1995-2001 (2003).
    • (2003) Infect. Immun. , vol.71 , pp. 1995-2001
    • Scaife, H.1    Woldehiwet, Z.2    Hart, C.A.3    Edwards, S.W.4
  • 137
    • 18744367006 scopus 로고    scopus 로고
    • Insights into pathogen immune evasion mechanisms: Anaplasma phagocytophilum fails to induce an apoptosis differentiation program in human neutrophils
    • Borjesson, D. L. et al. Insights into pathogen immune evasion mechanisms: Anaplasma phagocytophilum fails to induce an apoptosis differentiation program in human neutrophils. J. Immunol. 174, 6364-6372 (2005).
    • (2005) J. Immunol. , vol.174 , pp. 6364-6372
    • Borjesson, D.L.1
  • 138
    • 28444458847 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum delay of neutrophil apoptosis through the p38 mitogen-activated protein kinase signal pathway
    • Choi, K. S., Park, J. T. & Dumler, J. S. Anaplasma phagocytophilum delay of neutrophil apoptosis through the p38 mitogen-activated protein kinase signal pathway. Infect. Immun. 73, 8209-8218 (2005).
    • (2005) Infect. Immun. , vol.73 , pp. 8209-8218
    • Choi, K.S.1    Park, J.T.2    Dumler, J.S.3
  • 139
    • 33748876775 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum causes global induction of antiapoptosis in human neutrophils
    • Lee, H. C. & Goodman, J. L. Anaplasma phagocytophilum causes global induction of antiapoptosis in human neutrophils. Genomics 88, 496-503 (2006).
    • (2006) Genomics , vol.88 , pp. 496-503
    • Lee, H.C.1    Goodman, J.L.2
  • 140
    • 33746921665 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum delays spontaneous human neutrophil apoptosis by modulation of multiple apoptotic pathways
    • Ge, Y. & Rikihisa, Y. Anaplasma phagocytophilum delays spontaneous human neutrophil apoptosis by modulation of multiple apoptotic pathways. Cell. Microbiol. 8, 1406-1416 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 1406-1416
    • Ge, Y.1    Rikihisa, Y.2
  • 141
    • 23344451806 scopus 로고    scopus 로고
    • Modulation of NB4 promyelocytic leukemic cell machinery by Anaplasma phagocytophilum
    • Pedra, J. H., Sukumaran, B., Carlyon, J. A., Berliner, N. & Fikrig, E. Modulation of NB4 promyelocytic leukemic cell machinery by Anaplasma phagocytophilum. Genomics 86, 365-377 (2005).
    • (2005) Genomics , vol.86 , pp. 365-377
    • Pedra, J.H.1    Sukumaran, B.2    Carlyon, J.A.3    Berliner, N.4    Fikrig, E.5
  • 142
    • 0347511899 scopus 로고    scopus 로고
    • Survival strategy of obligately intracellular Ehrlichia chaffeensis: Novel modulation of immune response and host cell cycles
    • Zhang, J. Z., Sinha, M., Luxon, B. A. & Yu, X. J. Survival strategy of obligately intracellular Ehrlichia chaffeensis: novel modulation of immune response and host cell cycles. Infect. Immun. 72, 498-507 (2004).
    • (2004) Infect. Immun. , vol.72 , pp. 498-507
    • Zhang, J.Z.1    Sinha, M.2    Luxon, B.A.3    Yu, X.J.4
  • 143
    • 77649251212 scopus 로고    scopus 로고
    • Anaplasma phagocytophilum Ats-1 is Imported into host cell mitochondria
    • Niu, H., Kozjak-Pavlovic, V., Rudel, T. & Rikihisa, Y. Anaplasma phagocytophilum Ats-1 is Imported into host cell mitochondria. PLoS Path. 6, e1000774 (2010).
    • (2010) PLoS Path. , vol.6
    • Niu, H.1    Kozjak-Pavlovic, V.2    Rudel, T.3    Rikihisa, Y.4
  • 144
    • 33750322790 scopus 로고    scopus 로고
    • Autophagy in innate immunity against intracellular bacteria
    • Amano, A., Nakagawa, I. & Yoshimori, T. Autophagy in innate immunity against intracellular bacteria. J. Biochem. 140, 161-166 (2006).
    • (2006) J. Biochem. , vol.140 , pp. 161-166
    • Amano, A.1    Nakagawa, I.2    Yoshimori, T.3
  • 145
    • 33748444233 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages
    • Ling, Y. M. et al. Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages. J. Exp.Med. 203, 2063-2071 (2006).
    • (2006) J. Exp.Med. , vol.203 , pp. 2063-2071
    • Ling, Y.M.1
  • 146
    • 33344475671 scopus 로고    scopus 로고
    • Autophagy in innate and adaptive immunity against intracellular pathogens
    • Schmid, D., Dengjel, J., Schoor, O., Stevanovic, S. & Munz, C. Autophagy in innate and adaptive immunity against intracellular pathogens. J. Mol. Med. 84, 194-202 (2006).
    • (2006) J. Mol. Med. , vol.84 , pp. 194-202
    • Schmid, D.1    Dengjel, J.2    Schoor, O.3    Stevanovic, S.4    Munz, C.5
  • 147
    • 63549109967 scopus 로고    scopus 로고
    • Cholesterol-dependent Anaplasma phagocytophilum exploits the low-density lipoprotein uptake pathway
    • Xiong, Q., Lin, M. & Rikihisa, Y. Cholesterol-dependent Anaplasma phagocytophilum exploits the low-density lipoprotein uptake pathway. PLoS Path. 5, e1000329 (2009).
    • (2009) PLoS Path. , vol.5
    • Xiong, Q.1    Lin, M.2    Rikihisa, Y.3
  • 148
    • 0033059778 scopus 로고    scopus 로고
    • Ehrlichial meningitis with cerebrospinal fluid morulae. Pediatr
    • Berry, D. S. et al. Ehrlichial meningitis with cerebrospinal fluid morulae. Pediatr. Infect. Dis. J. 18, 552-555 (1999).
    • (1999) Infect. Dis J. , vol.18 , pp. 552-555
    • Berry, D.S.1
  • 149
    • 0026691746 scopus 로고
    • Identification of Ehrlichia chaffeensis morulae in cerebrospinal fluid mononuclear cells
    • Dunn, B. E. et al. Identification of Ehrlichia chaffeensis morulae in cerebrospinal fluid mononuclear cells. J. Clin. Microbiol. 30, 2207-2210 (1992).
    • (1992) J. Clin. Microbiol. , vol.30 , pp. 2207-2210
    • Dunn, B.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.