메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

Treponema denticola Major Outer Sheath Protein Impairs the Cellular Phosphoinositide Balance That Regulates Neutrophil Chemotaxis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BACTERIAL PROTEIN; FORMYLMETHIONYLLEUCYLPHENYLALANINE; GELSOLIN; MAJOR OUTER SHEATH PROTEIN; PHOSPHATIDYLINOSITIDE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN CAPZ; PROTEIN KINASE B; RAC1 PROTEIN; UNCLASSIFIED DRUG; CHEMOTACTIC FACTOR; MAJOR OUTER SHEATH PROTEIN, TREPONEMA; NEUROPEPTIDE; PHOSPHATIDYLINOSITOL 3,4,5-TRIPHOSPHATE; POLYPHOSPHOINOSITIDE; PORIN; PTEN PROTEIN, MOUSE; RAC1 PROTEIN, MOUSE;

EID: 84878661734     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0066209     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: challenges and opportunities
    • Nathan C, (2006) Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 6: 173-182.
    • (2006) Nat Rev Immunol , vol.6 , pp. 173-182
    • Nathan, C.1
  • 2
    • 0346880066 scopus 로고    scopus 로고
    • Cytoskeletal remodeling in leukocyte function
    • Fenteany G, Glogauer M, (2004) Cytoskeletal remodeling in leukocyte function. Curr Opin Hematol 11: 15-24.
    • (2004) Curr Opin Hematol , vol.11 , pp. 15-24
    • Fenteany, G.1    Glogauer, M.2
  • 3
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG, (2003) Cellular motility driven by assembly and disassembly of actin filaments. Cell 112: 453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 4
    • 77957259884 scopus 로고    scopus 로고
    • The signaling mechanisms underlying cell polarity and chemotaxis
    • Wang F, (2009) The signaling mechanisms underlying cell polarity and chemotaxis. Cold Spring Harb Perspect Biol 1: a002980.
    • (2009) Cold Spring Harb Perspect Biol , vol.1
    • Wang, F.1
  • 5
    • 0036076652 scopus 로고    scopus 로고
    • Chemotactic signaling pathways in neutrophils: from receptor to actin assembly
    • Cicchetti G, Allen PG, Glogauer M, (2002) Chemotactic signaling pathways in neutrophils: from receptor to actin assembly. Crit Rev Oral Biol Med 13: 220-228.
    • (2002) Crit Rev Oral Biol Med , vol.13 , pp. 220-228
    • Cicchetti, G.1    Allen, P.G.2    Glogauer, M.3
  • 6
    • 83055161506 scopus 로고    scopus 로고
    • Rac regulates PtdInsP(3) signaling and the chemotactic compass through a redox-mediated feedback loop
    • Kuiper JW, Sun C, Magalhaes MA, Glogauer M, (2011) Rac regulates PtdInsP(3) signaling and the chemotactic compass through a redox-mediated feedback loop. Blood 118: 6164-6171.
    • (2011) Blood , vol.118 , pp. 6164-6171
    • Kuiper, J.W.1    Sun, C.2    Magalhaes, M.A.3    Glogauer, M.4
  • 7
    • 9444238519 scopus 로고    scopus 로고
    • Rac1 is the small GTPase responsible for regulating the neutrophil chemotaxis compass
    • Sun CX, Downey GP, Zhu F, Koh AL, Thang H, et al. (2004) Rac1 is the small GTPase responsible for regulating the neutrophil chemotaxis compass. Blood 104: 3758-3765.
    • (2004) Blood , vol.104 , pp. 3758-3765
    • Sun, C.X.1    Downey, G.P.2    Zhu, F.3    Koh, A.L.4    Thang, H.5
  • 8
    • 0036308458 scopus 로고    scopus 로고
    • Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils
    • Wang F, Herzmark P, Weiner OD, Srinivasan S, Servant G, et al. (2002) Lipid products of PI(3)Ks maintain persistent cell polarity and directed motility in neutrophils. Nat Cell Biol 4: 513-518.
    • (2002) Nat Cell Biol , vol.4 , pp. 513-518
    • Wang, F.1    Herzmark, P.2    Weiner, O.D.3    Srinivasan, S.4    Servant, G.5
  • 10
    • 0036532121 scopus 로고    scopus 로고
    • Roles of PI3Ks in leukocyte chemotaxis and phagocytosis
    • Stephens L, Ellson C, Hawkins P, (2002) Roles of PI3Ks in leukocyte chemotaxis and phagocytosis. Curr Opin Cell Biol 14: 203-213.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 203-213
    • Stephens, L.1    Ellson, C.2    Hawkins, P.3
  • 12
    • 0029978202 scopus 로고    scopus 로고
    • The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase
    • Damen JE, Liu L, Rosten P, Humphries RK, Jefferson AB, et al. (1996) The 145-kDa protein induced to associate with Shc by multiple cytokines is an inositol tetraphosphate and phosphatidylinositol 3,4,5-triphosphate 5-phosphatase. Proc Natl Acad Sci U S A 93: 1689-1693.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1689-1693
    • Damen, J.E.1    Liu, L.2    Rosten, P.3    Humphries, R.K.4    Jefferson, A.B.5
  • 13
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T, Dixon JE, (1998) The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 273: 13375-13378.
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 14
    • 0037133606 scopus 로고    scopus 로고
    • Neutrophils lacking phosphoinositide 3-kinase gamma show loss of directionality during N-formyl-Met-Leu-Phe-induced chemotaxis
    • Hannigan M, Zhan L, Li Z, Ai Y, Wu D, et al. (2002) Neutrophils lacking phosphoinositide 3-kinase gamma show loss of directionality during N-formyl-Met-Leu-Phe-induced chemotaxis. Proc Natl Acad Sci U S A 99: 3603-3608.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3603-3608
    • Hannigan, M.1    Zhan, L.2    Li, Z.3    Ai, Y.4    Wu, D.5
  • 15
    • 38949147037 scopus 로고    scopus 로고
    • PI3K accelerates, but is not required for, neutrophil chemotaxis to fMLP
    • Heit B, Liu L, Colarusso P, Puri KD, Kubes P, (2008) PI3K accelerates, but is not required for, neutrophil chemotaxis to fMLP. J Cell Sci 121: 205-214.
    • (2008) J Cell Sci , vol.121 , pp. 205-214
    • Heit, B.1    Liu, L.2    Colarusso, P.3    Puri, K.D.4    Kubes, P.5
  • 16
    • 45549093769 scopus 로고    scopus 로고
    • PTEN functions to 'prioritize' chemotactic cues and prevent 'distraction' in migrating neutrophils
    • Heit B, Robbins SM, Downey CM, Guan Z, Colarusso P, et al. (2008) PTEN functions to 'prioritize' chemotactic cues and prevent 'distraction' in migrating neutrophils. Nat Immunol 9: 743-752.
    • (2008) Nat Immunol , vol.9 , pp. 743-752
    • Heit, B.1    Robbins, S.M.2    Downey, C.M.3    Guan, Z.4    Colarusso, P.5
  • 17
    • 79959235806 scopus 로고    scopus 로고
    • Pretreatment with phosphatase and tensin homolog deleted on chromosome 10 (PTEN) inhibitor SF1670 augments the efficacy of granulocyte transfusion in a clinically relevant mouse model
    • Li Y, Prasad A, Jia Y, Roy SG, Loison F, et al. (2011) Pretreatment with phosphatase and tensin homolog deleted on chromosome 10 (PTEN) inhibitor SF1670 augments the efficacy of granulocyte transfusion in a clinically relevant mouse model. Blood 117: 6702-6713.
    • (2011) Blood , vol.117 , pp. 6702-6713
    • Li, Y.1    Prasad, A.2    Jia, Y.3    Roy, S.G.4    Loison, F.5
  • 18
    • 84859417595 scopus 로고    scopus 로고
    • Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion
    • Mondal S, Subramanian KK, Sakai J, Bajrami B, Luo HR, (2012) Phosphoinositide lipid phosphatase SHIP1 and PTEN coordinate to regulate cell migration and adhesion. Mol Biol Cell 23: 1219-1230.
    • (2012) Mol Biol Cell , vol.23 , pp. 1219-1230
    • Mondal, S.1    Subramanian, K.K.2    Sakai, J.3    Bajrami, B.4    Luo, H.R.5
  • 19
    • 0037369696 scopus 로고    scopus 로고
    • Essential role of phosphoinositide 3-kinase delta in neutrophil directional movement
    • Sadhu C, Masinovsky B, Dick K, Sowell CG, Staunton DE, (2003) Essential role of phosphoinositide 3-kinase delta in neutrophil directional movement. J Immunol 170: 2647-2654.
    • (2003) J Immunol , vol.170 , pp. 2647-2654
    • Sadhu, C.1    Masinovsky, B.2    Dick, K.3    Sowell, C.G.4    Staunton, D.E.5
  • 20
    • 34247360789 scopus 로고    scopus 로고
    • Tumor suppressor PTEN is a physiologic suppressor of chemoattractant-mediated neutrophil functions
    • Subramanian KK, Jia Y, Zhu D, Simms BT, Jo H, et al. (2007) Tumor suppressor PTEN is a physiologic suppressor of chemoattractant-mediated neutrophil functions. Blood 109: 4028-4037.
    • (2007) Blood , vol.109 , pp. 4028-4037
    • Subramanian, K.K.1    Jia, Y.2    Zhu, D.3    Simms, B.T.4    Jo, H.5
  • 21
    • 20444440319 scopus 로고    scopus 로고
    • Spirochetes at the forefront of periodontal infections
    • Ellen RP, Galimanas VB, (2005) Spirochetes at the forefront of periodontal infections. Periodontol 2000 38: 13-32.
    • (2005) Periodontol 2000 , vol.38 , pp. 13-32
    • Ellen, R.P.1    Galimanas, V.B.2
  • 22
    • 0034754077 scopus 로고    scopus 로고
    • Role of Treponema denticola in periodontal diseases
    • Sela MN, (2001) Role of Treponema denticola in periodontal diseases. Crit Rev Oral Biol Med 12: 399-413.
    • (2001) Crit Rev Oral Biol Med , vol.12 , pp. 399-413
    • Sela, M.N.1
  • 23
    • 0032765412 scopus 로고    scopus 로고
    • The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure
    • Caimano MJ, Bourell KW, Bannister TD, Cox DL, Radolf JD, (1999) The Treponema denticola major sheath protein is predominantly periplasmic and has only limited surface exposure. Infect Immun 67: 4072-4083.
    • (1999) Infect Immun , vol.67 , pp. 4072-4083
    • Caimano, M.J.1    Bourell, K.W.2    Bannister, T.D.3    Cox, D.L.4    Radolf, J.D.5
  • 24
    • 0026690981 scopus 로고
    • Characterization, cloning, and binding properties of the major 53-kilodalton Treponema denticola surface antigen
    • Haapasalo M, Muller KH, Uitto VJ, Leung WK, McBride BC, (1992) Characterization, cloning, and binding properties of the major 53-kilodalton Treponema denticola surface antigen. Infect Immun 60: 2058-2065.
    • (1992) Infect Immun , vol.60 , pp. 2058-2065
    • Haapasalo, M.1    Muller, K.H.2    Uitto, V.J.3    Leung, W.K.4    McBride, B.C.5
  • 25
    • 84855723374 scopus 로고    scopus 로고
    • Composition and localization of Treponema denticola outer membrane complexes
    • Godovikova V, Goetting-Minesky MP, Fenno JC, (2011) Composition and localization of Treponema denticola outer membrane complexes. Infect Immun 79: 4868-4875.
    • (2011) Infect Immun , vol.79 , pp. 4868-4875
    • Godovikova, V.1    Goetting-Minesky, M.P.2    Fenno, J.C.3
  • 26
    • 84864812761 scopus 로고    scopus 로고
    • Treponema denticola interactions with host proteins
    • Fenno JC (2012) Treponema denticola interactions with host proteins. J Oral Microbiol 4.
    • (2012) J Oral Microbiol , vol.4
    • Fenno, J.C.1
  • 27
    • 79952729069 scopus 로고    scopus 로고
    • New insights into the emerging role of oral spirochaetes in periodontal disease
    • Visser MB, Ellen RP, (2011) New insights into the emerging role of oral spirochaetes in periodontal disease. Clin Microbiol Infect 17: 502-512.
    • (2011) Clin Microbiol Infect , vol.17 , pp. 502-512
    • Visser, M.B.1    Ellen, R.P.2
  • 28
    • 39049163900 scopus 로고    scopus 로고
    • Human serum antibodies recognize Treponema denticola Msp and PrtP protease complex proteins
    • Capone R, Wang HT, Ning Y, Sweier DG, Lopatin DE, et al. (2008) Human serum antibodies recognize Treponema denticola Msp and PrtP protease complex proteins. Oral Microbiol Immunol 23: 165-169.
    • (2008) Oral Microbiol Immunol , vol.23 , pp. 165-169
    • Capone, R.1    Wang, H.T.2    Ning, Y.3    Sweier, D.G.4    Lopatin, D.E.5
  • 29
    • 2542524720 scopus 로고    scopus 로고
    • Induction of de novo subcortical actin filament assembly by Treponema denticola major outer sheath protein
    • Amin M, Ho AC, Lin JY, Batista da Silva AP, Glogauer M, et al. (2004) Induction of de novo subcortical actin filament assembly by Treponema denticola major outer sheath protein. Infect Immun 72: 3650-3654.
    • (2004) Infect Immun , vol.72 , pp. 3650-3654
    • Amin, M.1    Ho, A.C.2    Lin, J.Y.3    Batista da Silva, A.P.4    Glogauer, M.5
  • 30
    • 38049112697 scopus 로고    scopus 로고
    • The major outer sheath protein of Treponema denticola selectively inhibits Rac1 activation in murine neutrophils
    • Magalhaes MA, Sun CX, Glogauer M, Ellen RP, (2008) The major outer sheath protein of Treponema denticola selectively inhibits Rac1 activation in murine neutrophils. Cell Microbiol 10: 344-354.
    • (2008) Cell Microbiol , vol.10 , pp. 344-354
    • Magalhaes, M.A.1    Sun, C.X.2    Glogauer, M.3    Ellen, R.P.4
  • 31
    • 33644780745 scopus 로고    scopus 로고
    • Modulation of human neutrophil functions in vitro by Treponema denticola major outer sheath protein
    • Puthengady Thomas B, Sun CX, Bajenova E, Ellen RP, Glogauer M, (2006) Modulation of human neutrophil functions in vitro by Treponema denticola major outer sheath protein. Infect Immun 74: 1954-1957.
    • (2006) Infect Immun , vol.74 , pp. 1954-1957
    • Puthengady Thomas, B.1    Sun, C.X.2    Bajenova, E.3    Ellen, R.P.4    Glogauer, M.5
  • 32
    • 1842829136 scopus 로고    scopus 로고
    • The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts
    • Batista da Silva AP, Lee W, Bajenova E, McCulloch CA, Ellen RP, (2004) The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts. Cell Microbiol 6: 485-498.
    • (2004) Cell Microbiol , vol.6 , pp. 485-498
    • Batista da Silva, A.P.1    Lee, W.2    Bajenova, E.3    McCulloch, C.A.4    Ellen, R.P.5
  • 33
    • 0035933886 scopus 로고    scopus 로고
    • A spirochete surface protein uncouples store-operated calcium channels in fibroblasts: a novel cytotoxic mechanism
    • Wang Q, Ko KS, Kapus A, McCulloch CA, Ellen RP, (2001) A spirochete surface protein uncouples store-operated calcium channels in fibroblasts: a novel cytotoxic mechanism. J Biol Chem 276: 23056-23064.
    • (2001) J Biol Chem , vol.276 , pp. 23056-23064
    • Wang, Q.1    Ko, K.S.2    Kapus, A.3    McCulloch, C.A.4    Ellen, R.P.5
  • 34
    • 80052044266 scopus 로고    scopus 로고
    • Treponema denticola major outer sheath protein induces actin assembly at free barbed ends by a PIP2-dependent uncapping mechanism in fibroblasts
    • Visser MB, Koh A, Glogauer M, Ellen RP, (2011) Treponema denticola major outer sheath protein induces actin assembly at free barbed ends by a PIP2-dependent uncapping mechanism in fibroblasts. PLoS One 6: e23736.
    • (2011) PLoS One , vol.6
    • Visser, M.B.1    Koh, A.2    Glogauer, M.3    Ellen, R.P.4
  • 35
    • 35548972598 scopus 로고    scopus 로고
    • Rac1 and Rac2 differentially regulate actin free barbed end formation downstream of the fMLP receptor
    • Sun CX, Magalhaes MA, Glogauer M, (2007) Rac1 and Rac2 differentially regulate actin free barbed end formation downstream of the fMLP receptor. J Cell Biol 179: 239-245.
    • (2007) J Cell Biol , vol.179 , pp. 239-245
    • Sun, C.X.1    Magalhaes, M.A.2    Glogauer, M.3
  • 36
    • 33947496373 scopus 로고    scopus 로고
    • A small molecule inhibitor for phosphatase and tensin homologue deleted on chromosome 10 (PTEN)
    • Rosivatz E, Matthews JG, McDonald NQ, Mulet X, Ho KK, et al. (2006) A small molecule inhibitor for phosphatase and tensin homologue deleted on chromosome 10 (PTEN). ACS Chem Biol 1: 780-790.
    • (2006) ACS Chem Biol , vol.1 , pp. 780-790
    • Rosivatz, E.1    Matthews, J.G.2    McDonald, N.Q.3    Mulet, X.4    Ho, K.K.5
  • 37
    • 34447299716 scopus 로고    scopus 로고
    • The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN
    • Papakonstanti EA, Ridley AJ, Vanhaesebroeck B, (2007) The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN. EMBO J 26: 3050-3061.
    • (2007) EMBO J , vol.26 , pp. 3050-3061
    • Papakonstanti, E.A.1    Ridley, A.J.2    Vanhaesebroeck, B.3
  • 38
    • 33845889090 scopus 로고    scopus 로고
    • Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1
    • Nishio M, Watanabe K, Sasaki J, Taya C, Takasuga S, et al. (2007) Control of cell polarity and motility by the PtdIns(3,4,5)P3 phosphatase SHIP1. Nat Cell Biol 9: 36-44.
    • (2007) Nat Cell Biol , vol.9 , pp. 36-44
    • Nishio, M.1    Watanabe, K.2    Sasaki, J.3    Taya, C.4    Takasuga, S.5
  • 39
    • 0036308972 scopus 로고    scopus 로고
    • A PtdInsP(3)- and Rho GTPase-mediated positive feedback loop regulates neutrophil polarity
    • Weiner OD, Neilsen PO, Prestwich GD, Kirschner MW, Cantley LC, et al. (2002) A PtdInsP(3)- and Rho GTPase-mediated positive feedback loop regulates neutrophil polarity. Nat Cell Biol 4: 509-513.
    • (2002) Nat Cell Biol , vol.4 , pp. 509-513
    • Weiner, O.D.1    Neilsen, P.O.2    Prestwich, G.D.3    Kirschner, M.W.4    Cantley, L.C.5
  • 40
    • 77950561967 scopus 로고    scopus 로고
    • Pivotal Advance: Phospholipids determine net membrane surface charge resulting in differential localization of active Rac1 and Rac2
    • Magalhaes MA, Glogauer M, (2010) Pivotal Advance: Phospholipids determine net membrane surface charge resulting in differential localization of active Rac1 and Rac2. J Leukoc Biol 87: 545-555.
    • (2010) J Leukoc Biol , vol.87 , pp. 545-555
    • Magalhaes, M.A.1    Glogauer, M.2
  • 41
    • 33646705667 scopus 로고    scopus 로고
    • Regulation of the PTEN phosphatase
    • Gericke A, Munson M, Ross AH, (2006) Regulation of the PTEN phosphatase. Gene 374: 1-9.
    • (2006) Gene , vol.374 , pp. 1-9
    • Gericke, A.1    Munson, M.2    Ross, A.H.3
  • 42
    • 38349030742 scopus 로고    scopus 로고
    • New insights into PTEN
    • Tamguney T, Stokoe D, (2007) New insights into PTEN. J Cell Sci 120: 4071-4079.
    • (2007) J Cell Sci , vol.120 , pp. 4071-4079
    • Tamguney, T.1    Stokoe, D.2
  • 43
    • 0141817911 scopus 로고    scopus 로고
    • Allosteric activation of PTEN phosphatase by phosphatidylinositol 4,5-bisphosphate
    • Campbell RB, Liu F, Ross AH, (2003) Allosteric activation of PTEN phosphatase by phosphatidylinositol 4,5-bisphosphate. J Biol Chem 278: 33617-33620.
    • (2003) J Biol Chem , vol.278 , pp. 33617-33620
    • Campbell, R.B.1    Liu, F.2    Ross, A.H.3
  • 44
    • 0038245261 scopus 로고    scopus 로고
    • Interfacial kinetic analysis of the tumour suppressor phosphatase, PTEN: evidence for activation by anionic phospholipids
    • McConnachie G, Pass I, Walker SM, Downes CP, (2003) Interfacial kinetic analysis of the tumour suppressor phosphatase, PTEN: evidence for activation by anionic phospholipids. Biochem J 371: 947-955.
    • (2003) Biochem J , vol.371 , pp. 947-955
    • McConnachie, G.1    Pass, I.2    Walker, S.M.3    Downes, C.P.4
  • 45
    • 51849167782 scopus 로고    scopus 로고
    • Understanding PTEN regulation: PIP2, polarity and protein stability
    • Leslie NR, Batty IH, Maccario H, Davidson L, Downes CP, (2008) Understanding PTEN regulation: PIP2, polarity and protein stability. Oncogene 27: 5464-5476.
    • (2008) Oncogene , vol.27 , pp. 5464-5476
    • Leslie, N.R.1    Batty, I.H.2    Maccario, H.3    Davidson, L.4    Downes, C.P.5
  • 46
    • 11144358038 scopus 로고    scopus 로고
    • Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes
    • Seshadri R, Myers GS, Tettelin H, Eisen JA, Heidelberg JF, et al. (2004) Comparison of the genome of the oral pathogen Treponema denticola with other spirochete genomes. Proc Natl Acad Sci U S A 101: 5646-5651.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 5646-5651
    • Seshadri, R.1    Myers, G.S.2    Tettelin, H.3    Eisen, J.A.4    Heidelberg, J.F.5
  • 47
    • 0031900968 scopus 로고    scopus 로고
    • Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola
    • Fenno JC, Hannam PM, Leung WK, Tamura M, Uitto VJ, et al. (1998) Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola. Infect Immun 66: 1869-1877.
    • (1998) Infect Immun , vol.66 , pp. 1869-1877
    • Fenno, J.C.1    Hannam, P.M.2    Leung, W.K.3    Tamura, M.4    Uitto, V.J.5
  • 48
    • 0027210973 scopus 로고
    • Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola
    • Egli C, Leung WK, Muller KH, Hancock RE, McBride BC, (1993) Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola. Infect Immun 61: 1694-1699.
    • (1993) Infect Immun , vol.61 , pp. 1694-1699
    • Egli, C.1    Leung, W.K.2    Muller, K.H.3    Hancock, R.E.4    McBride, B.C.5
  • 49
    • 0030017433 scopus 로고    scopus 로고
    • The major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes
    • Mathers DA, Leung WK, Fenno JC, Hong Y, McBride BC, (1996) The major surface protein complex of Treponema denticola depolarizes and induces ion channels in HeLa cell membranes. Infect Immun 64: 2904-2910.
    • (1996) Infect Immun , vol.64 , pp. 2904-2910
    • Mathers, D.A.1    Leung, W.K.2    Fenno, J.C.3    Hong, Y.4    McBride, B.C.5
  • 50
    • 33750722808 scopus 로고    scopus 로고
    • Bacterial protein toxins and lipids: role in toxin targeting and activity
    • Geny B, Popoff MR, (2006) Bacterial protein toxins and lipids: role in toxin targeting and activity. Biol Cell 98: 633-651.
    • (2006) Biol Cell , vol.98 , pp. 633-651
    • Geny, B.1    Popoff, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.