메뉴 건너뛰기




Volumn 80, Issue , 2014, Pages 161-195

Multifaceted activity of listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes

Author keywords

Bacterial toxin; Cholesterol dependent cytolysin; Infectious disease; Listeria monocytogenes; Listeriolysin O

Indexed keywords

BACTERIA (MICROORGANISMS); LISTERIA MONOCYTOGENES; POSIBACTERIA;

EID: 84906314749     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-017-8881-6_9     Document Type: Article
Times cited : (71)

References (189)
  • 1
    • 77953405736 scopus 로고    scopus 로고
    • Rhombencephalitis caused by Listeria monocytogenes in humans and ruminants: A zoonosis on the rise?
    • Oevermann A, Zurbriggen A, Vandevelde M (2010) Rhombencephalitis caused by Listeria monocytogenes in humans and ruminants: a zoonosis on the rise? Interdiscip Perspect Infect Dis 2010: 632513.
    • (2010) Interdiscip Perspect Infect Dis , vol.2010
    • Oevermann, A.1    Zurbriggen, A.2    Vandevelde, M.3
  • 2
    • 34548484138 scopus 로고    scopus 로고
    • The epidemiology of human listeriosis
    • Swaminathan B, Gerner-Smidt P (2007) The epidemiology of human listeriosis. Microbes Infect 9: 1236-1243.
    • (2007) Microbes Infect , vol.9 , pp. 1236-1243
    • Swaminathan, B.1    Gerner-Smidt, P.2
  • 4
    • 0000909738 scopus 로고
    • A disease of rabbits characterized by a large mononuclear leucoytosis caused by a hitherto undescribed bacillus Bacterium monocytogenes
    • Murray EGD, Webb RA, HBR S (1926) A disease of rabbits characterized by a large mononuclear leucoytosis caused by a hitherto undescribed bacillus Bacterium monocytogenes. J Pathol Bacteriol 29: 407-439.
    • (1926) J Pathol Bacteriol , vol.29 , pp. 407-439
    • Murray, E.G.D.1    Webb, R.A.2    Hbr, S.3
  • 6
    • 75649104350 scopus 로고    scopus 로고
    • Listeria as an enteroinvasive gastrointestinal pathogen
    • Barbuddhe SB, Chakraborty T (2009) Listeria as an enteroinvasive gastrointestinal pathogen. Curr Top Microbiol Immunol 337: 173-195.
    • (2009) Curr Top Microbiol Immunol , vol.337 , pp. 173-195
    • Barbuddhe, S.B.1    Chakraborty, T.2
  • 7
    • 0036956818 scopus 로고    scopus 로고
    • Bile stress response in Listeria monocytogenes LO28: Adaptation, cross-protection, and identification of genetic loci involved in bile resistance
    • Begley M, Gahan CG, Hill C (2002) Bile stress response in Listeria monocytogenes LO28: adaptation, cross-protection, and identification of genetic loci involved in bile resistance. Appl Environ Microbiol 68: 6005-6012.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 6005-6012
    • Begley, M.1    Gahan, C.G.2    Hill, C.3
  • 9
    • 0036037505 scopus 로고    scopus 로고
    • Listeria monocytogenes bile salt hydrolase is a PrfA-regulated virulence factor involved in the intestinal and hepatic phases of listeriosis
    • Dussurget O, Cabanes D, Dehoux P, Lecuit M, Buchrieser C, Glaser P, Cossart P (2002) Listeria monocytogenes bile salt hydrolase is a PrfA-regulated virulence factor involved in the intestinal and hepatic phases of listeriosis. Mol Microbiol 45: 1095-1106.
    • (2002) Mol Microbiol , vol.45 , pp. 1095-1106
    • Dussurget, O.1    Cabanes, D.2    Dehoux, P.3    Lecuit, M.4    Buchrieser, C.5    Glaser, P.6    Cossart, P.7
  • 10
    • 0037221016 scopus 로고    scopus 로고
    • Incidence of fecal carriage of Listeria monocytogenes in three healthy volunteers: A one-year prospective stool survey
    • Grif K, Patscheider G, Dierich MP, Allerberger F (2003) Incidence of fecal carriage of Listeria monocytogenes in three healthy volunteers: a one-year prospective stool survey. Eur J Clin Microbiol Infect Dis 22: 16-20.
    • (2003) Eur J Clin Microbiol Infect Dis , vol.22 , pp. 16-20
    • Grif, K.1    Patscheider, G.2    Dierich, M.P.3    Allerberger, F.4
  • 11
    • 17644378780 scopus 로고    scopus 로고
    • Gastroenteritis due to Listeria monocytogenes
    • Ooi ST, Lorber B (2005) Gastroenteritis due to Listeria monocytogenes. Clin Infect Dis 40: 1327-1332.
    • (2005) Clin Infect Dis , vol.40 , pp. 1327-1332
    • Ooi, S.T.1    Lorber, B.2
  • 12
    • 0037083267 scopus 로고    scopus 로고
    • Listeria monocytogenes: Clinical and experimental update
    • Wing EJ, Gregory SH (2002) Listeria monocytogenes: clinical and experimental update. J Infect Dis 185: S18-S24.
    • (2002) J Infect Dis , vol.185 , pp. S18-S24
    • Wing, E.J.1    Gregory, S.H.2
  • 13
    • 79953008676 scopus 로고    scopus 로고
    • Evidence for subpopulations of Listeria monocytogenes with enhanced invasion of cardiac cells
    • Alonzo F 3rd, Bobo LD, Skiest DJ, Freitag NE (2011) Evidence for subpopulations of Listeria monocytogenes with enhanced invasion of cardiac cells. J Med Microbiol 60: 423-434.
    • (2011) J Med Microbiol , vol.60 , pp. 423-434
    • Alonzo, F.1    Bobo, L.D.2    Skiest, D.J.3    Freitag, N.E.4
  • 14
    • 84862838853 scopus 로고    scopus 로고
    • Targeting of the central nervous system by Listeria monocytogenes
    • Disson O, Lecuit M (2012) Targeting of the central nervous system by Listeria monocytogenes. Virulence 3: 213-221.
    • (2012) Virulence , vol.3 , pp. 213-221
    • Disson, O.1    Lecuit, M.2
  • 16
    • 84891057618 scopus 로고    scopus 로고
    • Pathogenesis of listeriosis during pregnancy
    • Poulsen KP, Czuprynski CJ (2013) Pathogenesis of listeriosis during pregnancy. Anim Health Res Rev 14: 30-39.
    • (2013) Anim Health Res Rev , vol.14 , pp. 30-39
    • Poulsen, K.P.1    Czuprynski, C.J.2
  • 19
    • 0034056366 scopus 로고    scopus 로고
    • Treatment of listeriosis
    • Temple ME, Nahata MC (2000) Treatment of listeriosis. Ann Pharmacother 34(5): 656-661.
    • (2000) Ann Pharmacother , vol.34 , Issue.5 , pp. 656-661
    • Temple, M.E.1    Nahata, M.C.2
  • 20
    • 80355126239 scopus 로고    scopus 로고
    • Diagnosis of Listeria monocytogenes meningoencephalitis by real-time PCR for the hly gene
    • Le Monnier A, Abachin E, Beretti JL, Berche P, Kayal S (2011) Diagnosis of Listeria monocytogenes meningoencephalitis by real-time PCR for the hly gene. J Clin Microbiol 49: 3917-3923.
    • (2011) J Clin Microbiol , vol.49 , pp. 3917-3923
    • Le Monnier, A.1    Abachin, E.2    Beretti, J.L.3    Berche, P.4    Kayal, S.5
  • 23
    • 84880680198 scopus 로고    scopus 로고
    • A differential fluorescence-based genetic screen identifies Listeria monocytogenes determinants required for intracellular replication
    • (in press)
    • Perry KJ, Higgins DE (2013) A differential fluorescence-based genetic screen identifies Listeria monocytogenes determinants required for intracellular replication. J Bacteriol. doi: 10. 1128/JB. 00210-13 (in press).
    • (2013) J Bacteriol
    • Perry, K.J.1    Higgins, D.E.2
  • 25
    • 30744447972 scopus 로고    scopus 로고
    • Identification of Listeria monocytogenes genes contributing to intracellular replication by expression profiling and mutant screening
    • Joseph B, Przybilla K, Stuhler C, Schauer K, Slaghuis J, Fuchs TM, Goebel W (2006) Identification of Listeria monocytogenes genes contributing to intracellular replication by expression profiling and mutant screening. J Bacteriol 188: 556-568.
    • (2006) J Bacteriol , vol.188 , pp. 556-568
    • Joseph, B.1    Przybilla, K.2    Stuhler, C.3    Schauer, K.4    Slaghuis, J.5    Fuchs, T.M.6    Goebel, W.7
  • 26
    • 0023617861 scopus 로고
    • In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2
    • Gaillard JL, Berche P, Mounier J, Richard S, Sansonetti P (1987) In vitro model of penetration and intracellular growth of Listeria monocytogenes in the human enterocyte-like cell line Caco-2. Infect Immun 55: 2822-2829.
    • (1987) Infect Immun , vol.55 , pp. 2822-2829
    • Gaillard, J.L.1    Berche, P.2    Mounier, J.3    Richard, S.4    Sansonetti, P.5
  • 27
    • 0031594726 scopus 로고    scopus 로고
    • The InIB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells
    • Braun L, Ohayon H, Cossart P (1998) The InIB protein of Listeria monocytogenes is sufficient to promote entry into mammalian cells. Mol Microbiol 27: 1077-1087.
    • (1998) Mol Microbiol , vol.27 , pp. 1077-1087
    • Braun, L.1    Ohayon, H.2    Cossart, P.3
  • 28
    • 0029063839 scopus 로고
    • Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family
    • Dramsi S, Biswas I, Maguin E, Braun L, Mastroeni P, Cossart P (1995) Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family. Mol Microbiol 16: 251-261.
    • (1995) Mol Microbiol , vol.16 , pp. 251-261
    • Dramsi, S.1    Biswas, I.2    Maguin, E.3    Braun, L.4    Mastroeni, P.5    Cossart, P.6
  • 29
    • 0025739814 scopus 로고
    • Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from grampositive cocci
    • Gaillard JL, Berche P, Frehel C, Gouin E, Cossart P (1991) Entry of L. monocytogenes into cells is mediated by internalin, a repeat protein reminiscent of surface antigens from grampositive cocci. Cell 65: 1127-1141.
    • (1991) Cell , vol.65 , pp. 1127-1141
    • Gaillard, J.L.1    Berche, P.2    Frehel, C.3    Gouin, E.4    Cossart, P.5
  • 30
    • 0033404562 scopus 로고    scopus 로고
    • Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: A novel mechanism of protein association at the surface of gram-positive bacteria
    • Jonquieres R, Bierne H, Fiedler F, Gounon P, Cossart P (1999) Interaction between the protein InlB of Listeria monocytogenes and lipoteichoic acid: a novel mechanism of protein association at the surface of gram-positive bacteria. Mol Microbiol 34: 902-914.
    • (1999) Mol Microbiol , vol.34 , pp. 902-914
    • Jonquieres, R.1    Bierne, H.2    Fiedler, F.3    Gounon, P.4    Cossart, P.5
  • 31
    • 0035171383 scopus 로고    scopus 로고
    • Synergy between the N-and C-terminal domains of InlB for efficient invasion of non-phagocytic cells by Listeria monocytogenes
    • Jonquieres R, Pizarro-Cerda J, Cossart P (2001) Synergy between the N-and C-terminal domains of InlB for efficient invasion of non-phagocytic cells by Listeria monocytogenes. Mol Microbiol 42: 955-965.
    • (2001) Mol Microbiol , vol.42 , pp. 955-965
    • Jonquieres, R.1    Pizarro-Cerda, J.2    Cossart, P.3
  • 32
    • 0036845352 scopus 로고    scopus 로고
    • GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands
    • Marino M, Banerjee M, Jonquieres R, Cossart P, Ghosh P (2002) GW domains of the Listeria monocytogenes invasion protein InlB are SH3-like and mediate binding to host ligands. EMBO J 21: 5623-5634.
    • (2002) EMBO J , vol.21 , pp. 5623-5634
    • Marino, M.1    Banerjee, M.2    Jonquieres, R.3    Cossart, P.4    Ghosh, P.5
  • 34
    • 34548516176 scopus 로고    scopus 로고
    • Molecular mechanisms exploited by Listeria monocytogenes during host cell invasion
    • Seveau S, Pizarro-Cerda J, Cossart P (2007) Molecular mechanisms exploited by Listeria monocytogenes during host cell invasion. Microbes Infect 9: 1167-1175.
    • (2007) Microbes Infect , vol.9 , pp. 1167-1175
    • Seveau, S.1    Pizarro-Cerda, J.2    Cossart, P.3
  • 35
    • 0023189876 scopus 로고
    • Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes
    • Geoffroy C, Gaillard JL, Alouf JE, Berche P (1987) Purification, characterization, and toxicity of the sulfhydryl-activated hemolysin listeriolysin O from Listeria monocytogenes. Infect Immun 55: 1641-1646.
    • (1987) Infect Immun , vol.55 , pp. 1641-1646
    • Geoffroy, C.1    Gaillard, J.L.2    Alouf, J.E.3    Berche, P.4
  • 36
    • 0024519896 scopus 로고
    • Production of thiol-dependent haemolysins by Listeria monocytogenes and related species
    • Geoffroy C, Gaillard JL, Alouf JE, Berche P (1989) Production of thiol-dependent haemolysins by Listeria monocytogenes and related species. J Gen Microbiol 135: 481-487.
    • (1989) J Gen Microbiol , vol.135 , pp. 481-487
    • Geoffroy, C.1    Gaillard, J.L.2    Alouf, J.E.3    Berche, P.4
  • 37
    • 0023898917 scopus 로고
    • Role of hemolysin for the intracellular growth of Listeria monocytogenes
    • Portnoy DA, Jacks PS, Hinrichs DJ (1988) Role of hemolysin for the intracellular growth of Listeria monocytogenes. J Exp Med 167: 1459-1471.
    • (1988) J Exp Med , vol.167 , pp. 1459-1471
    • Portnoy, D.A.1    Jacks, P.S.2    Hinrichs, D.J.3
  • 38
    • 0024464468 scopus 로고
    • Listeriolysin O is essential for virulence of Listeria monocytogenes: Direct evidence obtained by gene complementation
    • Cossart P, Vicente MF, Mengaud J, Baquero F, Perez-Diaz JC, Berche P (1989) Listeriolysin O is essential for virulence of Listeria monocytogenes: direct evidence obtained by gene complementation. Infect Immun 57: 3629-3636.
    • (1989) Infect Immun , vol.57 , pp. 3629-3636
    • Cossart, P.1    Vicente, M.F.2    Mengaud, J.3    Baquero, F.4    Perez-Diaz, J.C.5    Berche, P.6
  • 39
    • 0022628814 scopus 로고
    • Transposon mutagenesis as a tool to study the role of hemolysin in the virulence of Listeria monocytogenes
    • Gaillard JL, Berche P, Sansonetti P (1986) Transposon mutagenesis as a tool to study the role of hemolysin in the virulence of Listeria monocytogenes. Infect Immun 52: 50-55.
    • (1986) Infect Immun , vol.52 , pp. 50-55
    • Gaillard, J.L.1    Berche, P.2    Sansonetti, P.3
  • 40
    • 0023138737 scopus 로고
    • Tn916-induced mutations in the hemolysin determinant affecting virulence of Listeria monocytogenes
    • Kathariou S, Metz P, Hof H, Goebel W (1987) Tn916-induced mutations in the hemolysin determinant affecting virulence of Listeria monocytogenes. J Bacteriol 169: 1291-1297.
    • (1987) J Bacteriol , vol.169 , pp. 1291-1297
    • Kathariou, S.1    Metz, P.2    Hof, H.3    Goebel, W.4
  • 41
    • 0023515533 scopus 로고
    • Identification of the structural gene encoding the SH-activated hemolysin of Listeria monocytogenes: Listeriolysin O is homologous to streptolysin O and pneumolysin
    • Mengaud J, Chenevert J, Geoffroy C, Gaillard JL, Cossart P (1987) Identification of the structural gene encoding the SH-activated hemolysin of Listeria monocytogenes: listeriolysin O is homologous to streptolysin O and pneumolysin. Infect Immun 55: 3225-3227.
    • (1987) Infect Immun , vol.55 , pp. 3225-3227
    • Mengaud, J.1    Chenevert, J.2    Geoffroy, C.3    Gaillard, J.L.4    Cossart, P.5
  • 42
    • 0026515440 scopus 로고
    • L. monocytogenesinduced actin assembly requires the actA gene product, a surface protein
    • Kocks C, Gouin E, Tabouret M, Berche P, Ohayon H, Cossart P (1992) L. monocytogenesinduced actin assembly requires the actA gene product, a surface protein. Cell 68: 521-531.
    • (1992) Cell , vol.68 , pp. 521-531
    • Kocks, C.1    Gouin, E.2    Tabouret, M.3    Berche, P.4    Ohayon, H.5    Cossart, P.6
  • 43
    • 0032479578 scopus 로고    scopus 로고
    • Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation
    • Welch MD, Rosenblatt J, Skoble J, Portnoy DA, Mitchison TJ (1998) Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281: 105-108.
    • (1998) Science , vol.281 , pp. 105-108
    • Welch, M.D.1    Rosenblatt, J.2    Skoble, J.3    Portnoy, D.A.4    Mitchison, T.J.5
  • 44
    • 0025239739 scopus 로고
    • Intracellular and cell-to-cell spread of Listeria monocytogenes involves interaction with F-actin in the enterocytelike cell line Caco-2
    • Mounier J, Ryter A, Coquis-Rondon M, Sansonetti PJ (1990) Intracellular and cell-to-cell spread of Listeria monocytogenes involves interaction with F-actin in the enterocytelike cell line Caco-2. Infect Immun 58: 1048-1058.
    • (1990) Infect Immun , vol.58 , pp. 1048-1058
    • Mounier, J.1    Ryter, A.2    Coquis-Rondon, M.3    Sansonetti, P.J.4
  • 45
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney LG, Portnoy DA (1989) Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 109: 1597-1608.
    • (1989) J Cell Biol , vol.109 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 46
    • 0033977538 scopus 로고    scopus 로고
    • Role of listeriolysin O in cell-tocell spread of Listeria monocytogenes
    • Gedde MM, Higgins DE, Tilney LG, Portnoy DA (2000) Role of listeriolysin O in cell-tocell spread of Listeria monocytogenes. Infect Immun 68: 999-1003.
    • (2000) Infect Immun , vol.68 , pp. 999-1003
    • Gedde, M.M.1    Higgins, D.E.2    Tilney, L.G.3    Portnoy, D.A.4
  • 47
    • 0025016446 scopus 로고
    • Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread
    • Sun AN, Camilli A, Portnoy DA (1990) Isolation of Listeria monocytogenes small-plaque mutants defective for intracellular growth and cell-to-cell spread. Infect Immun 58: 3770-3778.
    • (1990) Infect Immun , vol.58 , pp. 3770-3778
    • Sun, A.N.1    Camilli, A.2    Portnoy, D.A.3
  • 48
    • 0028828198 scopus 로고
    • The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread
    • Smith GA, Marquis H, Jones S, Johnston NC, Portnoy DA, Goldfine H (1995) The two distinct phospholipases C of Listeria monocytogenes have overlapping roles in escape from a vacuole and cell-to-cell spread. Infect Immun 63: 4231-4237.
    • (1995) Infect Immun , vol.63 , pp. 4231-4237
    • Smith, G.A.1    Marquis, H.2    Jones, S.3    Johnston, N.C.4    Portnoy, D.A.5    Goldfine, H.6
  • 53
    • 0025015538 scopus 로고
    • Identification of a gene that positively regulates expression of listeriolysin, the major virulence factor of listeria monocytogenes
    • Leimeister-Wachter M, Haffner C, Domann E, Goebel W, Chakraborty T (1990) Identification of a gene that positively regulates expression of listeriolysin, the major virulence factor of listeria monocytogenes. Proc Natl Acad Sci USA 87: 8336-8340.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 8336-8340
    • Leimeister-Wachter, M.1    Haffner, C.2    Domann, E.3    Goebel, W.4    Chakraborty, T.5
  • 54
    • 0026599832 scopus 로고
    • Transcriptional activation of the Listeria monocytogenes hemolysin gene in Bacillus subtilis
    • Freitag NE, Youngman P, Portnoy DA (1992) Transcriptional activation of the Listeria monocytogenes hemolysin gene in Bacillus subtilis. J Bacteriol 174: 1293-1298.
    • (1992) J Bacteriol , vol.174 , pp. 1293-1298
    • Freitag, N.E.1    Youngman, P.2    Portnoy, D.A.3
  • 55
    • 0031848306 scopus 로고    scopus 로고
    • Regulation of hly expression in Listeria monocytogenes by carbon sources and pH occurs through separate mechanisms mediated by PrfA
    • Behari J, Youngman P (1998) Regulation of hly expression in Listeria monocytogenes by carbon sources and pH occurs through separate mechanisms mediated by PrfA. Infect Immun 66: 3635-3642.
    • (1998) Infect Immun , vol.66 , pp. 3635-3642
    • Behari, J.1    Youngman, P.2
  • 56
    • 0027490303 scopus 로고
    • Effects of glucose, growth temperature, and pH on listeriolysin O production in Listeria monocytogenes
    • Datta AR, Kothary MH (1993) Effects of glucose, growth temperature, and pH on listeriolysin O production in Listeria monocytogenes. Appl Environ Microbiol 59: 3495-3497.
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3495-3497
    • Datta, A.R.1    Kothary, M.H.2
  • 57
    • 0031024403 scopus 로고    scopus 로고
    • Carbon-source regulation of virulence gene expression in Listeria monocytogenes
    • Milenbachs AA, Brown DP, Moors M, Youngman P (1997) Carbon-source regulation of virulence gene expression in Listeria monocytogenes. Mol Microbiol 23: 1075-1085.
    • (1997) Mol Microbiol , vol.23 , pp. 1075-1085
    • Milenbachs, A.A.1    Brown, D.P.2    Moors, M.3    Youngman, P.4
  • 58
    • 0037031594 scopus 로고    scopus 로고
    • An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes
    • Johansson J, Mandin P, Renzoni A, Chiaruttini C, Springer M, Cossart P (2002) An RNA thermosensor controls expression of virulence genes in Listeria monocytogenes. Cell 110: 551-561.
    • (2002) Cell , vol.110 , pp. 551-561
    • Johansson, J.1    Mandin, P.2    Renzoni, A.3    Chiaruttini, C.4    Springer, M.5    Cossart, P.6
  • 59
    • 0026541096 scopus 로고
    • The expression of virulence genes in Listeria monocytogenes is thermoregulated
    • Leimeister-Wachter M, Domann E, Chakraborty T (1992) The expression of virulence genes in Listeria monocytogenes is thermoregulated. J Bacteriol 174: 947-952.
    • (1992) J Bacteriol , vol.174 , pp. 947-952
    • Leimeister-Wachter, M.1    Domann, E.2    Chakraborty, T.3
  • 60
    • 0033036962 scopus 로고    scopus 로고
    • Differential expression of Listeria monocytogenes virulence genes in mammalian host cells
    • Bubert A, Sokolovic Z, Chun SK, Papatheodorou L, Simm A, Goebel W (1999) Differential expression of Listeria monocytogenes virulence genes in mammalian host cells. Mol Gen Genet 261: 323-336.
    • (1999) Mol Gen Genet , vol.261 , pp. 323-336
    • Bubert, A.1    Sokolovic, Z.2    Chun, S.K.3    Papatheodorou, L.4    Simm, A.5    Goebel, W.6
  • 61
    • 23844522843 scopus 로고    scopus 로고
    • The 5' untranslated region-mediated enhancement of intracellular listeriolysin O production is required for Listeria monocytogenes pathogenicity
    • Shen A, Higgins DE (2005) The 5' untranslated region-mediated enhancement of intracellular listeriolysin O production is required for Listeria monocytogenes pathogenicity. Mol Microbiol 57: 1460-1473.
    • (2005) Mol Microbiol , vol.57 , pp. 1460-1473
    • Shen, A.1    Higgins, D.E.2
  • 62
    • 33644819006 scopus 로고    scopus 로고
    • Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: Role of the PEST-like sequence
    • Schnupf P, Portnoy DA, Decatur AL (2006) Phosphorylation, ubiquitination and degradation of listeriolysin O in mammalian cells: role of the PEST-like sequence. Cell Microbiol 8: 353-364.
    • (2006) Cell Microbiol , vol.8 , pp. 353-364
    • Schnupf, P.1    Portnoy, D.A.2    Decatur, A.L.3
  • 64
    • 79952651258 scopus 로고    scopus 로고
    • Defensins enable macrophages to inhibit the intracellular proliferation of Listeria monocytogenes
    • Arnett E, Lehrer RI, Pratikhya P, Lu W, Seveau S (2011) Defensins enable macrophages to inhibit the intracellular proliferation of Listeria monocytogenes. Cell Microbiol 13: 635-651.
    • (2011) Cell Microbiol , vol.13 , pp. 635-651
    • Arnett, E.1    Lehrer, R.I.2    Pratikhya, P.3    Lu, W.4    Seveau, S.5
  • 66
    • 84861307350 scopus 로고    scopus 로고
    • The multifaceted activities of mammalian defensins
    • Arnett E, Seveau S (2011) The multifaceted activities of mammalian defensins. Curr Pharm Des 17: 4254-4269.
    • (2011) Curr Pharm Des , vol.17 , pp. 4254-4269
    • Arnett, E.1    Seveau, S.2
  • 67
    • 84887313008 scopus 로고    scopus 로고
    • Crystallization and X-ray crystallographic analysis of the cholesterol-dependent cytolysin listeriolysin O from Listeria monocytogenes
    • Koster S, Hudel M, Chakraborty T, Yildiz O (2013) Crystallization and X-ray crystallographic analysis of the cholesterol-dependent cytolysin listeriolysin O from Listeria monocytogenes. Acta Crystallogr, Sect F: Struct Biol Cryst Commun 69: 1212-1215.
    • (2013) Acta Crystallogr, Sect F: Struct Biol Cryst Commun , vol.69 , pp. 1212-1215
    • Koster, S.1    Hudel, M.2    Chakraborty, T.3    Yildiz, O.4
  • 68
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: The mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • Dunstone MA, Tweten RK (2012) Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr Opin Struct Biol 22: 342-349.
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 69
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, Parker MW (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89: 685-692.
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 70
    • 77952302993 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin family of gram-positive bacterial toxins
    • Heuck AP, Moe PC, Johnson BB (2010) The cholesterol-dependent cytolysin family of gram-positive bacterial toxins. Subcell Biochem 51: 551-577.
    • (2010) Subcell Biochem , vol.51 , pp. 551-577
    • Heuck, A.P.1    Moe, P.C.2    Johnson, B.B.3
  • 71
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • Hotze EM, Tweten RK (2012) Membrane assembly of the cholesterol-dependent cytolysin pore complex. Biochim Biophys Acta 1818: 1028-1038.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 72
    • 0036830653 scopus 로고    scopus 로고
    • Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin
    • Ramachandran R, Heuck AP, Tweten RK, Johnson AE (2002) Structural insights into the membrane-anchoring mechanism of a cholesterol-dependent cytolysin. Nat Struct Biol 9: 823-827.
    • (2002) Nat Struct Biol , vol.9 , pp. 823-827
    • Ramachandran, R.1    Heuck, A.P.2    Tweten, R.K.3    Johnson, A.E.4
  • 73
    • 3042855150 scopus 로고    scopus 로고
    • The solution structure and oligomerization behavior of two bacterial toxins: Pneumolysin and perfringolysin O
    • Solovyova AS, Nollmann M, Mitchell TJ, Byron O (2004) The solution structure and oligomerization behavior of two bacterial toxins: pneumolysin and perfringolysin O. Biophys J 87: 540-552.
    • (2004) Biophys J , vol.87 , pp. 540-552
    • Solovyova, A.S.1    Nollmann, M.2    Mitchell, T.J.3    Byron, O.4
  • 74
    • 0032536856 scopus 로고    scopus 로고
    • Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
    • Palmer M, Harris R, Freytag C, Kehoe M, Tranum-Jensen J, Bhakdi S (1998) Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization. EMBO J 17: 1598-1605.
    • (1998) EMBO J , vol.17 , pp. 1598-1605
    • Palmer, M.1    Harris, R.2    Freytag, C.3    Kehoe, M.4    Tranum-Jensen, J.5    Bhakdi, S.6
  • 76
    • 33645553471 scopus 로고    scopus 로고
    • Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles
    • Shaughnessy LM, Hoppe AD, Christensen KA, Swanson JA (2006) Membrane perforations inhibit lysosome fusion by altering pH and calcium in Listeria monocytogenes vacuoles. Cell Microbiol 8: 781-792.
    • (2006) Cell Microbiol , vol.8 , pp. 781-792
    • Shaughnessy, L.M.1    Hoppe, A.D.2    Christensen, K.A.3    Swanson, J.A.4
  • 77
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit betastrand alignment
    • Ramachandran R, Tweten RK, Johnson AE (2004) Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit betastrand alignment. Nat Struct Mol Biol 11: 697-705.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 78
    • 34447536854 scopus 로고    scopus 로고
    • Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin
    • Soltani CE, Hotze EM, Johnson AE, Tweten RK (2007) Specific protein-membrane contacts are required for prepore and pore assembly by a cholesterol-dependent cytolysin. J Biol Chem 282: 15709-15716.
    • (2007) J Biol Chem , vol.282 , pp. 15709-15716
    • Soltani, C.E.1    Hotze, E.M.2    Johnson, A.E.3    Tweten, R.K.4
  • 79
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • Farrand AJ, LaChapelle S, Hotze EM, Johnson AE, Tweten RK (2010) Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface. Proc Natl Acad Sci USA 107: 4341-4346.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    LaChapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 81
    • 0034523543 scopus 로고    scopus 로고
    • Listeriolysin O-induced stimulation of mucin exocytosis in polarized intestinal mucin-secreting cells: Evidence for toxin recognition of membrane-associated lipids and subsequent toxin internalization through caveolae
    • Coconnier MH, Lorrot M, Barbat A, Laboisse C, Servin AL (2000) Listeriolysin O-induced stimulation of mucin exocytosis in polarized intestinal mucin-secreting cells: evidence for toxin recognition of membrane-associated lipids and subsequent toxin internalization through caveolae. Cell Microbiol 2: 487-504.
    • (2000) Cell Microbiol , vol.2 , pp. 487-504
    • Coconnier, M.H.1    Lorrot, M.2    Barbat, A.3    Laboisse, C.4    Servin, A.L.5
  • 82
    • 44349190402 scopus 로고    scopus 로고
    • Functional and phylogenetic characterization of Vaginolysin, the human-specific cytolysin from Gardnerella vaginalis
    • Gelber SE, Aguilar JL, Lewis KL, Ratner AJ (2008) Functional and phylogenetic characterization of Vaginolysin, the human-specific cytolysin from Gardnerella vaginalis. J Bacteriol 190: 3896-3903.
    • (2008) J Bacteriol , vol.190 , pp. 3896-3903
    • Gelber, S.E.1    Aguilar, J.L.2    Lewis, K.L.3    Ratner, A.J.4
  • 83
    • 16544370492 scopus 로고    scopus 로고
    • Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin
    • Giddings KS, Zhao J, Sims PJ, Tweten RK (2004) Human CD59 is a receptor for the cholesterol-dependent cytolysin intermedilysin. Nat Struct Mol Biol 11: 1173-1178.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1173-1178
    • Giddings, K.S.1    Zhao, J.2    Sims, P.J.3    Tweten, R.K.4
  • 85
    • 84864593970 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin signature motif: A critical element in the allosteric pathway that couples membrane binding to pore assembly
    • Dowd KJ, Tweten RK (2012) The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly. PLoS Pathog 8: e1002787.
    • (2012) PLoS Pathog , vol.8
    • Dowd, K.J.1    Tweten, R.K.2
  • 86
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99: 293-299.
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 87
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • Shepard LA, Heuck AP, Hamman BD, Rossjohn J, Parker MW, Ryan KR, Johnson AE, Tweten RK (1998) Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37: 14563-14574.
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 88
    • 0035896507 scopus 로고    scopus 로고
    • Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate
    • Hotze EM, Wilson-Kubalek EM, Rossjohn J, Parker MW, Johnson AE, Tweten RK (2001) Arresting pore formation of a cholesterol-dependent cytolysin by disulfide trapping synchronizes the insertion of the transmembrane beta-sheet from a prepore intermediate. J Biol Chem 276: 8261-8268.
    • (2001) J Biol Chem , vol.276 , pp. 8261-8268
    • Hotze, E.M.1    Wilson-Kubalek, E.M.2    Rossjohn, J.3    Parker, M.W.4    Johnson, A.E.5    Tweten, R.K.6
  • 89
    • 81755183022 scopus 로고    scopus 로고
    • The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes
    • Vadia S, Arnett E, Haghighat AC, Wilson-Kubalek EM, Tweten RK, Seveau S (2011) The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes. PLoS Pathog 7: e1002356.
    • (2011) PLoS Pathog , vol.7
    • Vadia, S.1    Arnett, E.2    Haghighat, A.C.3    Wilson-Kubalek, E.M.4    Tweten, R.K.5    Seveau, S.6
  • 90
    • 34548490518 scopus 로고    scopus 로고
    • Listeriolysin O: A phagosome-specific lysin
    • Schnupf P, Portnoy DA (2007) Listeriolysin O: a phagosome-specific lysin. Microbes Infect 9: 1176-1187.
    • (2007) Microbes Infect , vol.9 , pp. 1176-1187
    • Schnupf, P.1    Portnoy, D.A.2
  • 94
  • 95
    • 0037128936 scopus 로고    scopus 로고
    • The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells
    • Glomski IJ, Gedde MM, Tsang AW, Swanson JA, Portnoy DA (2002) The Listeria monocytogenes hemolysin has an acidic pH optimum to compartmentalize activity and prevent damage to infected host cells. J Cell Biol 156: 1029-1038.
    • (2002) J Cell Biol , vol.156 , pp. 1029-1038
    • Glomski, I.J.1    Gedde, M.M.2    Tsang, A.W.3    Swanson, J.A.4    Portnoy, D.A.5
  • 96
    • 0025685253 scopus 로고
    • Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O
    • Michel E, Reich KA, Favier R, Berche P, Cossart P (1990) Attenuated mutants of the intracellular bacterium Listeria monocytogenes obtained by single amino acid substitutions in listeriolysin O. Mol Microbiol 4: 2167-2178.
    • (1990) Mol Microbiol , vol.4 , pp. 2167-2178
    • Michel, E.1    Reich, K.A.2    Favier, R.3    Berche, P.4    Cossart, P.5
  • 97
    • 55249111793 scopus 로고    scopus 로고
    • GILT is a critical host factor for Listeria monocytogenes infection
    • Singh R, Jamieson A, Cresswell P (2008) GILT is a critical host factor for Listeria monocytogenes infection. Nature 455: 1244-1247.
    • (2008) Nature , vol.455 , pp. 1244-1247
    • Singh, R.1    Jamieson, A.2    Cresswell, P.3
  • 98
    • 70349904566 scopus 로고    scopus 로고
    • Perturbation of vacuolar maturation promotes listeriolysin O-independent vacuolar escape during Listeria monocytogenes infection of human cells
    • Burrack LS, Harper JW, Higgins DE (2009) Perturbation of vacuolar maturation promotes listeriolysin O-independent vacuolar escape during Listeria monocytogenes infection of human cells. Cell Microbiol 11: 1382-1398.
    • (2009) Cell Microbiol , vol.11 , pp. 1382-1398
    • Burrack, L.S.1    Harper, J.W.2    Higgins, D.E.3
  • 99
    • 10744224174 scopus 로고    scopus 로고
    • Requirement of the Listeria monocytogenes broad-range phospholipase PC-PLC during infection of human epithelial cells
    • Grundling A, Gonzalez MD, Higgins DE (2003) Requirement of the Listeria monocytogenes broad-range phospholipase PC-PLC during infection of human epithelial cells. J Bacteriol 185: 6295-6307.
    • (2003) J Bacteriol , vol.185 , pp. 6295-6307
    • Grundling, A.1    Gonzalez, M.D.2    Higgins, D.E.3
  • 100
    • 0028822997 scopus 로고
    • The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells
    • Marquis H, Doshi V, Portnoy DA (1995) The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells. Infect Immun 63: 4531-4534.
    • (1995) Infect Immun , vol.63 , pp. 4531-4534
    • Marquis, H.1    Doshi, V.2    Portnoy, D.A.3
  • 101
    • 0027476804 scopus 로고
    • Dual roles of plcA in Listeria monocytogenes pathogenesis
    • Camilli A, Tilney LG, Portnoy DA (1993) Dual roles of plcA in Listeria monocytogenes pathogenesis. Mol Microbiol 8: 143-157.
    • (1993) Mol Microbiol , vol.8 , pp. 143-157
    • Camilli, A.1    Tilney, L.G.2    Portnoy, D.A.3
  • 102
    • 0036073612 scopus 로고    scopus 로고
    • Mobilization of protein kinase C in macrophages induced by Listeria monocytogenes affects its internalization and escape from the phagosome
    • Wadsworth SJ, Goldfine H (2002) Mobilization of protein kinase C in macrophages induced by Listeria monocytogenes affects its internalization and escape from the phagosome. Infect Immun 70: 4650-4660.
    • (2002) Infect Immun , vol.70 , pp. 4650-4660
    • Wadsworth, S.J.1    Goldfine, H.2
  • 103
    • 0030828008 scopus 로고    scopus 로고
    • pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes
    • Beauregard KE, Lee KD, Collier RJ, Swanson JA (1997) pH-dependent perforation of macrophage phagosomes by listeriolysin O from Listeria monocytogenes. J Exp Med 186: 1159-1163.
    • (1997) J Exp Med , vol.186 , pp. 1159-1163
    • Beauregard, K.E.1    Lee, K.D.2    Collier, R.J.3    Swanson, J.A.4
  • 106
    • 83655190735 scopus 로고    scopus 로고
    • Listeriolysin O suppresses phospholipase C-mediated activation of the microbicidal NADPH oxidase to promote Listeria monocytogenes infection
    • Lam GY, Fattouh R, Muise AM, Grinstein S, Higgins DE, Brumell JH (2011) Listeriolysin O suppresses phospholipase C-mediated activation of the microbicidal NADPH oxidase to promote Listeria monocytogenes infection. Cell Host Microbe 10: 627-634.
    • (2011) Cell Host Microbe , vol.10 , pp. 627-634
    • Lam, G.Y.1    Fattouh, R.2    Muise, A.M.3    Grinstein, S.4    Higgins, D.E.5    Brumell, J.H.6
  • 107
    • 0035846909 scopus 로고    scopus 로고
    • Cytolysin-mediated translocation (CMT): A functional equivalent of type III secretion in gram-positive bacteria
    • Madden JC, Ruiz N, Caparon M (2001) Cytolysin-mediated translocation (CMT): a functional equivalent of type III secretion in gram-positive bacteria. Cell 104: 143-152.
    • (2001) Cell , vol.104 , pp. 143-152
    • Madden, J.C.1    Ruiz, N.2    Caparon, M.3
  • 108
    • 36048965750 scopus 로고    scopus 로고
    • The role of the activated macrophage in clearing Listeria monocytogenes infection
    • Shaughnessy LM, Swanson JA (2007) The role of the activated macrophage in clearing Listeria monocytogenes infection. Front Biosci 12: 2683-2692.
    • (2007) Front Biosci , vol.12 , pp. 2683-2692
    • Shaughnessy, L.M.1    Swanson, J.A.2
  • 109
    • 84891118285 scopus 로고    scopus 로고
    • The pore-forming toxin listeriolysin O is degraded by neutrophil metalloproteiase-8 and is fails to mediate Listeria monocytogenes intracellular survival in neutrophils
    • (in press)
    • Arnett E, Vadia S, Nackerman CC, Oghumu S, Satoskar AR, McLeish KR, Uriarte SM, Seveau S (2014) The pore-forming toxin listeriolysin O is degraded by neutrophil metalloproteiase-8 and is fails to mediate Listeria monocytogenes intracellular survival in neutrophils. J Immunol. doi: 10. 4049/jimmunol. 1301302 (in press).
    • (2014) J Immunol
    • Arnett, E.1    Vadia, S.2    Nackerman, C.C.3    Oghumu, S.4    Satoskar, A.R.5    McLeish, K.R.6    Uriarte, S.M.7    Seveau, S.8
  • 110
    • 0242494307 scopus 로고    scopus 로고
    • Localized reactive oxygen and nitrogen intermediates inhibit escape of Listeria monocytogenes from vacuoles in activated macrophages
    • Myers JT, Tsang AW, Swanson JA (2003) Localized reactive oxygen and nitrogen intermediates inhibit escape of Listeria monocytogenes from vacuoles in activated macrophages. J Immunol 171: 5447-5453.
    • (2003) J Immunol , vol.171 , pp. 5447-5453
    • Myers, J.T.1    Tsang, A.W.2    Swanson, J.A.3
  • 112
    • 84867905124 scopus 로고    scopus 로고
    • Inducible renitence limits Listeria monocytogenes escape from vacuoles in macrophages
    • Davis MJ, Gregorka B, Gestwicki JE, Swanson JA (2012) Inducible renitence limits Listeria monocytogenes escape from vacuoles in macrophages. J Immunol 189: 4488-4495.
    • (2012) J Immunol , vol.189 , pp. 4488-4495
    • Davis, M.J.1    Gregorka, B.2    Gestwicki, J.E.3    Swanson, J.A.4
  • 114
    • 33947416152 scopus 로고    scopus 로고
    • Autophagy limits Listeria monocytogenes intracellular growth in the early phase of primary infection
    • Py BF, Lipinski MM, Yuan J (2007) Autophagy limits Listeria monocytogenes intracellular growth in the early phase of primary infection. Autophagy 3: 117-125.
    • (2007) Autophagy , vol.3 , pp. 117-125
    • Py, B.F.1    Lipinski, M.M.2    Yuan, J.3
  • 117
    • 33845424970 scopus 로고    scopus 로고
    • Differential function of Listeria monocytogenes listeriolysin O and phospholipases C in vacuolar dissolution following cell-to-cell spread
    • Alberti-Segui C, Goeden KR, Higgins DE (2007) Differential function of Listeria monocytogenes listeriolysin O and phospholipases C in vacuolar dissolution following cell-to-cell spread. Cell Microbiol 9: 179-195.
    • (2007) Cell Microbiol , vol.9 , pp. 179-195
    • Alberti-Segui, C.1    Goeden, K.R.2    Higgins, D.E.3
  • 118
    • 0036838013 scopus 로고    scopus 로고
    • Inducible control of virulence gene expression in Listeria monocytogenes: Temporal requirement of listeriolysin O during intracellular infection
    • Dancz CE, Haraga A, Portnoy DA, Higgins DE (2002) Inducible control of virulence gene expression in Listeria monocytogenes: temporal requirement of listeriolysin O during intracellular infection. J Bacteriol 184: 5935-5945.
    • (2002) J Bacteriol , vol.184 , pp. 5935-5945
    • Dancz, C.E.1    Haraga, A.2    Portnoy, D.A.3    Higgins, D.E.4
  • 119
    • 0028853674 scopus 로고
    • Listeriolysin is processed efficiently into an MHC class I-associated epitope in Listeria monocytogenes-infected cells
    • Villanueva MS, Sijts AJ, Pamer EG (1995) Listeriolysin is processed efficiently into an MHC class I-associated epitope in Listeria monocytogenes-infected cells. J Immunol 155: 5227-5233.
    • (1995) J Immunol , vol.155 , pp. 5227-5233
    • Villanueva, M.S.1    Sijts, A.J.2    Pamer, E.G.3
  • 120
    • 0034602312 scopus 로고    scopus 로고
    • A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity
    • Decatur AL, Portnoy DA (2000) A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity. Science 290: 992-995.
    • (2000) Science , vol.290 , pp. 992-995
    • Decatur, A.L.1    Portnoy, D.A.2
  • 121
    • 0344851711 scopus 로고    scopus 로고
    • Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses
    • Glomski IJ, Decatur AL, Portnoy DA (2003) Listeria monocytogenes mutants that fail to compartmentalize listerolysin O activity are cytotoxic, avirulent, and unable to evade host extracellular defenses. Infect Immun 71: 6754-6765.
    • (2003) Infect Immun , vol.71 , pp. 6754-6765
    • Glomski, I.J.1    Decatur, A.L.2    Portnoy, D.A.3
  • 122
    • 0037348466 scopus 로고    scopus 로고
    • Capacity of ivanolysin O to replace listeriolysin O in phagosomal escape and in vivo survival of Listeria monocytogenes
    • Frehel C, Lety MA, Autret N, Beretti JL, Berche P, Charbit A (2003) Capacity of ivanolysin O to replace listeriolysin O in phagosomal escape and in vivo survival of Listeria monocytogenes. Microbiology 149: 611-620.
    • (2003) Microbiology , vol.149 , pp. 611-620
    • Frehel, C.1    Lety, M.A.2    Autret, N.3    Beretti, J.L.4    Berche, P.5    Charbit, A.6
  • 123
    • 0028072474 scopus 로고
    • Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O
    • Jones S, Portnoy DA (1994) Characterization of Listeria monocytogenes pathogenesis in a strain expressing perfringolysin O in place of listeriolysin O. Infect Immun 62: 5608-5613.
    • (1994) Infect Immun , vol.62 , pp. 5608-5613
    • Jones, S.1    Portnoy, D.A.2
  • 124
    • 25444457508 scopus 로고    scopus 로고
    • Characterization of Listeria monocytogenes expressing anthrolysin O and phosphatidylinositol-specific phospholipase C from Bacillus anthracis
    • Wei Z, Schnupf P, Poussin MA, Zenewicz LA, Shen H, Goldfine H (2005) Characterization of Listeria monocytogenes expressing anthrolysin O and phosphatidylinositol-specific phospholipase C from Bacillus anthracis. Infect Immun 73: 6639-6646.
    • (2005) Infect Immun , vol.73 , pp. 6639-6646
    • Wei, Z.1    Schnupf, P.2    Poussin, M.A.3    Zenewicz, L.A.4    Shen, H.5    Goldfine, H.6
  • 125
    • 1842529256 scopus 로고    scopus 로고
    • Listeriolysin O from Listeria monocytogenes is a lymphocyte apoptogenic molecule
    • Carrero JA, Calderon B, Unanue ER (2004) Listeriolysin O from Listeria monocytogenes is a lymphocyte apoptogenic molecule. J Immunol 172: 4866-4874.
    • (2004) J Immunol , vol.172 , pp. 4866-4874
    • Carrero, J.A.1    Calderon, B.2    Unanue, E.R.3
  • 126
    • 0035100596 scopus 로고    scopus 로고
    • Identification of a PEST-like motif in listeriolysin O required for phagosomal escape and for virulence in Listeria monocytogenes
    • Lety MA, Frehel C, Dubail I, Beretti JL, Kayal S, Berche P, Charbit A (2001) Identification of a PEST-like motif in listeriolysin O required for phagosomal escape and for virulence in Listeria monocytogenes. Mol Microbiol 39: 1124-1139.
    • (2001) Mol Microbiol , vol.39 , pp. 1124-1139
    • Lety, M.A.1    Frehel, C.2    Dubail, I.3    Beretti, J.L.4    Kayal, S.5    Berche, P.6    Charbit, A.7
  • 127
    • 35648954603 scopus 로고    scopus 로고
    • Listeriolysin O secreted by Listeria monocytogenes into the host cell cytosol is degraded by the N-end rule pathway
    • Schnupf P, Zhou J, Varshavsky A, Portnoy DA (2007) Listeriolysin O secreted by Listeria monocytogenes into the host cell cytosol is degraded by the N-end rule pathway. Infect Immun 75: 5135-5147.
    • (2007) Infect Immun , vol.75 , pp. 5135-5147
    • Schnupf, P.1    Zhou, J.2    Varshavsky, A.3    Portnoy, D.A.4
  • 128
    • 40749138262 scopus 로고    scopus 로고
    • A bacterial pore-forming toxin forms aggregates in cells that resemble those associated with neurodegenerative diseases
    • Viala JP, Mochegova SN, Meyer-Morse N, Portnoy DA (2008) A bacterial pore-forming toxin forms aggregates in cells that resemble those associated with neurodegenerative diseases. Cell Microbiol 10: 985-993.
    • (2008) Cell Microbiol , vol.10 , pp. 985-993
    • Viala, J.P.1    Mochegova, S.N.2    Meyer-Morse, N.3    Portnoy, D.A.4
  • 129
    • 21544450007 scopus 로고    scopus 로고
    • Listeriolysin O-induced membrane permeation mediates persistent interleukin-6 production in Caco-2 cells during Listeria monocytogenes infection in vitro
    • Tsuchiya K, Kawamura I, Takahashi A, Nomura T, Kohda C, Mitsuyama M (2005) Listeriolysin O-induced membrane permeation mediates persistent interleukin-6 production in Caco-2 cells during Listeria monocytogenes infection in vitro. Infect Immun 73: 3869-3877.
    • (2005) Infect Immun , vol.73 , pp. 3869-3877
    • Tsuchiya, K.1    Kawamura, I.2    Takahashi, A.3    Nomura, T.4    Kohda, C.5    Mitsuyama, M.6
  • 130
    • 84864629840 scopus 로고    scopus 로고
    • Membrane damage during Listeria monocytogenes infection triggers a caspase-7 dependent cytoprotective response
    • Cassidy SK, Hagar JA, Kanneganti TD, Franchi L, Nunez G, O'Riordan MX (2012) Membrane damage during Listeria monocytogenes infection triggers a caspase-7 dependent cytoprotective response. PLoS Pathog 8: e1002628.
    • (2012) PLoS Pathog , vol.8
    • Cassidy, S.K.1    Hagar, J.A.2    Kanneganti, T.D.3    Franchi, L.4    Nunez, G.5    O’Riordan, M.X.6
  • 131
    • 84894279109 scopus 로고    scopus 로고
    • Fluxes of Ca2+ and K+ are required for the LLO-dependent internalization pathway of Listeria monocytogenes
    • (in press)
    • Vadia S, Seveau S (2014) Fluxes of Ca2+ and K+ are required for the LLO-dependent internalization pathway of Listeria monocytogenes. Infect Immun (in press).
    • (2014) Infect Immun
    • Vadia, S.1    Seveau, S.2
  • 132
  • 133
    • 0036500836 scopus 로고    scopus 로고
    • Repairing a torn cell surface: Make way, lysosomes to the rescue
    • McNeil PL (2002) Repairing a torn cell surface: make way, lysosomes to the rescue. J Cell Sci 115: 873-879.
    • (2002) J Cell Sci , vol.115 , pp. 873-879
    • McNeil, P.L.1
  • 134
    • 33749058798 scopus 로고    scopus 로고
    • The mechanisms of cell membrane repair: A tutorial guide to key experiments
    • Steinhardt RA (2005) The mechanisms of cell membrane repair: a tutorial guide to key experiments. Ann N Y Acad Sci 1066: 152-165.
    • (2005) Ann N Y Acad Sci , vol.1066 , pp. 152-165
    • Steinhardt, R.A.1
  • 135
    • 79951952737 scopus 로고    scopus 로고
    • Plasma membrane repair and cellular damage control: The annexin survival kit
    • Draeger A, Monastyrskaya K, Babiychuk EB (2011) Plasma membrane repair and cellular damage control: the annexin survival kit. Biochem Pharmacol 81: 703-712.
    • (2011) Biochem Pharmacol , vol.81 , pp. 703-712
    • Draeger, A.1    Monastyrskaya, K.2    Babiychuk, E.B.3
  • 137
    • 0030615262 scopus 로고    scopus 로고
    • Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells
    • Rodriguez A, Webster P, Ortego J, Andrews NW (1997) Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells. J Cell Biol 137: 93-104.
    • (1997) J Cell Biol , vol.137 , pp. 93-104
    • Rodriguez, A.1    Webster, P.2    Ortego, J.3    Andrews, N.W.4
  • 138
    • 0028014529 scopus 로고
    • Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release
    • Steinhardt RA, Bi G, Alderton JM (1994) Cell membrane resealing by a vesicular mechanism similar to neurotransmitter release. Science 263: 390-393.
    • (1994) Science , vol.263 , pp. 390-393
    • Steinhardt, R.A.1    Bi, G.2    Alderton, J.M.3
  • 141
    • 84856787672 scopus 로고    scopus 로고
    • Toxin pores endocytosed during plasma membrane repair traffic into the lumen of MVBs for degradation
    • Corrotte M, Fernandes MC, Tam C, Andrews NW (2012) Toxin pores endocytosed during plasma membrane repair traffic into the lumen of MVBs for degradation. Traffic 13: 483-494.
    • (2012) Traffic , vol.13 , pp. 483-494
    • Corrotte, M.1    Fernandes, M.C.2    Tam, C.3    Andrews, N.W.4
  • 144
    • 8744310905 scopus 로고    scopus 로고
    • Lipid rafts clustering and signalling by listeriolysin O
    • Gekara NO, Weiss S (2004) Lipid rafts clustering and signalling by listeriolysin O. Biochem Soc Trans 32: 712-714.
    • (2004) Biochem Soc Trans , vol.32 , pp. 712-714
    • Gekara, N.O.1    Weiss, S.2
  • 145
    • 0038780809 scopus 로고    scopus 로고
    • Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line
    • Dramsi S, Cossart P (2003) Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line. Infect Immun 71: 3614-3618.
    • (2003) Infect Immun , vol.71 , pp. 3614-3618
    • Dramsi, S.1    Cossart, P.2
  • 146
    • 34447619164 scopus 로고    scopus 로고
    • The multiple mechanisms of Ca2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes
    • Gekara NO, Westphal K, Ma B, Rohde M, Groebe L, Weiss S (2007) The multiple mechanisms of Ca2+ signalling by listeriolysin O, the cholesterol-dependent cytolysin of Listeria monocytogenes. Cell Microbiol 9: 2008-2021.
    • (2007) Cell Microbiol , vol.9 , pp. 2008-2021
    • Gekara, N.O.1    Westphal, K.2    Ma, B.3    Rohde, M.4    Groebe, L.5    Weiss, S.6
  • 148
    • 0033040621 scopus 로고    scopus 로고
    • Listeria monocytogenes phospholipase C-dependent calcium signaling modulates bacterial entry into J774 macrophage-like cells
    • Wadsworth SJ, Goldfine H (1999) Listeria monocytogenes phospholipase C-dependent calcium signaling modulates bacterial entry into J774 macrophage-like cells. Infect Immun 67: 1770-1778.
    • (1999) Infect Immun , vol.67 , pp. 1770-1778
    • Wadsworth, S.J.1    Goldfine, H.2
  • 150
    • 84883199752 scopus 로고    scopus 로고
    • Mitogen-activated protein kinases in innate immunity
    • Arthur JS, Ley SC (2013) Mitogen-activated protein kinases in innate immunity. Nat Rev Immunol 13: 679-692.
    • (2013) Nat Rev Immunol , vol.13 , pp. 679-692
    • Arthur, J.S.1    Ley, S.C.2
  • 151
    • 0031912786 scopus 로고    scopus 로고
    • Listeria monocytogenes invasion of epithelial cells requires the MEK-1/ERK-2 mitogen-activated protein kinase pathway
    • Tang P, Sutherland CL, Gold MR, Finlay BB (1998) Listeria monocytogenes invasion of epithelial cells requires the MEK-1/ERK-2 mitogen-activated protein kinase pathway. Infect Immun 66: 1106-1112.
    • (1998) Infect Immun , vol.66 , pp. 1106-1112
    • Tang, P.1    Sutherland, C.L.2    Gold, M.R.3    Finlay, B.B.4
  • 152
    • 0030970226 scopus 로고    scopus 로고
    • Listeria monocytogenes infection of HeLa cells results in listeriolysin O-mediated transient activation of the Raf-MEK-MAP kinase pathway
    • Weiglein I, Goebel W, Troppmair J, Rapp UR, Demuth A, Kuhn M (1997) Listeria monocytogenes infection of HeLa cells results in listeriolysin O-mediated transient activation of the Raf-MEK-MAP kinase pathway. FEMS Microbiol Lett 148: 189-195.
    • (1997) FEMS Microbiol Lett , vol.148 , pp. 189-195
    • Weiglein, I.1    Goebel, W.2    Troppmair, J.3    Rapp, U.R.4    Demuth, A.5    Kuhn, M.6
  • 153
    • 84878944582 scopus 로고    scopus 로고
    • Sumoylation: A regulatory protein modification in health and disease
    • Flotho A, Melchior F (2013) Sumoylation: a regulatory protein modification in health and disease. Annu Rev Biochem 82: 357-385.
    • (2013) Annu Rev Biochem , vol.82 , pp. 357-385
    • Flotho, A.1    Melchior, F.2
  • 154
    • 79251518045 scopus 로고    scopus 로고
    • SUMOylation and bacterial pathogens
    • Ribet D, Cossart P (2010) SUMOylation and bacterial pathogens. Virulence 1: 532-534.
    • (2010) Virulence , vol.1 , pp. 532-534
    • Ribet, D.1    Cossart, P.2
  • 155
    • 4444329588 scopus 로고    scopus 로고
    • Role of lipid rafts in Ecadherin-and HGF-R/Met-mediated entry of Listeria monocytogenes into host cells
    • Seveau S, Bierne H, Giroux S, Prevost MC, Cossart P (2004) Role of lipid rafts in Ecadherin-and HGF-R/Met-mediated entry of Listeria monocytogenes into host cells. J Cell Biol 166: 743-753.
    • (2004) J Cell Biol , vol.166 , pp. 743-753
    • Seveau, S.1    Bierne, H.2    Giroux, S.3    Prevost, M.C.4    Cossart, P.5
  • 156
    • 33846933508 scopus 로고    scopus 로고
    • A FRET analysis to unravel the role of cholesterol in Rac1 and PI 3-kinase activation in the InlB/Met signalling pathway
    • Seveau S, Tham TN, Payrastre B, Hoppe AD, Swanson JA, Cossart P (2007) A FRET analysis to unravel the role of cholesterol in Rac1 and PI 3-kinase activation in the InlB/Met signalling pathway. Cell Microbiol 9: 790-803.
    • (2007) Cell Microbiol , vol.9 , pp. 790-803
    • Seveau, S.1    Tham, T.N.2    Payrastre, B.3    Hoppe, A.D.4    Swanson, J.A.5    Cossart, P.6
  • 157
    • 79956075012 scopus 로고    scopus 로고
    • Trypanosoma cruzi subverts the sphingomyelinase-mediated plasma membrane repair pathway for cell invasion
    • Fernandes MC, Cortez M, Flannery AR, Tam C, Mortara RA, Andrews NW (2011) Trypanosoma cruzi subverts the sphingomyelinase-mediated plasma membrane repair pathway for cell invasion. J Exp Med 208: 909-921.
    • (2011) J Exp Med , vol.208 , pp. 909-921
    • Fernandes, M.C.1    Cortez, M.2    Flannery, A.R.3    Tam, C.4    Mortara, R.A.5    Andrews, N.W.6
  • 158
    • 79955082658 scopus 로고    scopus 로고
    • Streptolysin o inhibits clathrindependent internalization of group a streptococcus
    • Logsdon LK, Hakansson AP, Cortes G, Wessels MR (2011) Streptolysin o inhibits clathrindependent internalization of group a streptococcus. MBio 2: e00332-e00310.
    • (2011) MBio , vol.2 , pp. e00310-e00332
    • Logsdon, L.K.1    Hakansson, A.P.2    Cortes, G.3    Wessels, M.R.4
  • 160
    • 84890411602 scopus 로고    scopus 로고
    • Stressed to death-mechanisms of ER stress-induced cell death
    • Sovolyova N, Healy S, Samali A, Logue SE (2014) Stressed to death-mechanisms of ER stress-induced cell death. Biol Chem 395: 1-13.
    • (2014) Biol Chem , vol.395 , pp. 1-13
    • Sovolyova, N.1    Healy, S.2    Samali, A.3    Logue, S.E.4
  • 161
    • 84875534184 scopus 로고    scopus 로고
    • UPR signal activation by luminal sensor domains
    • Carrara M, Prischi F, Ali MM (2013) UPR signal activation by luminal sensor domains. Int J Mol Sci 14: 6454-6466.
    • (2013) Int J Mol Sci , vol.14 , pp. 6454-6466
    • Carrara, M.1    Prischi, F.2    Ali, M.M.3
  • 162
    • 84861193171 scopus 로고    scopus 로고
    • Activation of the unfolded protein response by Listeria monocytogenes
    • Pillich H, Loose M, Zimmer KP, Chakraborty T (2012) Activation of the unfolded protein response by Listeria monocytogenes. Cell Microbiol 14: 949-964.
    • (2012) Cell Microbiol , vol.14 , pp. 949-964
    • Pillich, H.1    Loose, M.2    Zimmer, K.P.3    Chakraborty, T.4
  • 163
    • 39149112798 scopus 로고    scopus 로고
    • Listeria monocytogenes desensitizes immune cells to subsequent Ca2+ signaling via listeriolysin O-induced depletion of intracellular Ca2+ stores
    • Gekara NO, Groebe L, Viegas N, Weiss S (2008) Listeria monocytogenes desensitizes immune cells to subsequent Ca2+ signaling via listeriolysin O-induced depletion of intracellular Ca2+ stores. Infect Immun 76: 857-862.
    • (2008) Infect Immun , vol.76 , pp. 857-862
    • Gekara, N.O.1    Groebe, L.2    Viegas, N.3    Weiss, S.4
  • 164
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M, Kaufman RJ (2005) The mammalian unfolded protein response. Annu Rev Biochem 74: 739-789.
    • (2005) Annu Rev Biochem , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 166
    • 77955824765 scopus 로고    scopus 로고
    • An intimate liaison: Spatial organization of the endoplasmic reticulum-mitochondria relationship
    • de Brito OM, Scorrano L (2010) An intimate liaison: spatial organization of the endoplasmic reticulum-mitochondria relationship. EMBO J 29: 2715-2723.
    • (2010) EMBO J , vol.29 , pp. 2715-2723
    • de Brito, O.M.1    Scorrano, L.2
  • 168
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister AJ, Kouzarides T (2011) Regulation of chromatin by histone modifications. Cell Res 21: 381-395.
    • (2011) Cell Res , vol.21 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 169
    • 79959431647 scopus 로고    scopus 로고
    • K+ efflux is required for histone H3 dephosphorylation by Listeria monocytogenes listeriolysin O and other pore-forming toxins
    • Hamon MA, Cossart P (2011) K+ efflux is required for histone H3 dephosphorylation by Listeria monocytogenes listeriolysin O and other pore-forming toxins. Infect Immun 79: 2839-2846.
    • (2011) Infect Immun , vol.79 , pp. 2839-2846
    • Hamon, M.A.1    Cossart, P.2
  • 170
    • 84869237413 scopus 로고    scopus 로고
    • Innate immune recognition and inflammasome activation in listeria monocytogenes infection
    • Eitel J, Suttorp N, Opitz B (2010) Innate immune recognition and inflammasome activation in listeria monocytogenes infection. Front Microbiol 1: 149.
    • (2010) Front Microbiol , vol.1
    • Eitel, J.1    Suttorp, N.2    Opitz, B.3
  • 172
    • 29644434743 scopus 로고    scopus 로고
    • Listeria monocytogenes activated p38 MAPK and induced IL-8 secretion in a nucleotide-binding oligomerization domain 1-dependent manner in endothelial cells
    • Opitz B, Puschel A, Beermann W, Hocke AC, Forster S, Schmeck B, van Laak V, Chakraborty T, Suttorp N, Hippenstiel S (2006) Listeria monocytogenes activated p38 MAPK and induced IL-8 secretion in a nucleotide-binding oligomerization domain 1-dependent manner in endothelial cells. J Immunol 176: 484-490.
    • (2006) J Immunol , vol.176 , pp. 484-490
    • Opitz, B.1    Puschel, A.2    Beermann, W.3    Hocke, A.C.4    Forster, S.5    Schmeck, B.6    van Laak, V.7    Chakraborty, T.8    Suttorp, N.9    Hippenstiel, S.10
  • 173
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L, Abrami L, Girardin S, Tschopp J, van der Goot FG (2006) Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126: 1135-1145.
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    van der Goot, F.G.5
  • 175
    • 84864024031 scopus 로고    scopus 로고
    • Protection from bacterial-toxin-induced apoptosis in macrophages requires the lipogenic transcription factor sterol regulatory element binding protein 1a
    • Im SS, Osborne TF (2012) Protection from bacterial-toxin-induced apoptosis in macrophages requires the lipogenic transcription factor sterol regulatory element binding protein 1a. Mol Cell Biol 32: 2196-2202.
    • (2012) Mol Cell Biol , vol.32 , pp. 2196-2202
    • Im, S.S.1    Osborne, T.F.2
  • 176
    • 0033033378 scopus 로고    scopus 로고
    • Listeriolysin Odependent activation of endothelial cells during infection with Listeria monocytogenes: Activation of NF-kappa B and upregulation of adhesion molecules and chemokines
    • Kayal S, Lilienbaum A, Poyart C, Memet S, Israel A, Berche P (1999) Listeriolysin Odependent activation of endothelial cells during infection with Listeria monocytogenes: activation of NF-kappa B and upregulation of adhesion molecules and chemokines. Mol Microbiol 31: 1709-1722.
    • (1999) Mol Microbiol , vol.31 , pp. 1709-1722
    • Kayal, S.1    Lilienbaum, A.2    Poyart, C.3    Memet, S.4    Israel, A.5    Berche, P.6
  • 177
    • 11844262784 scopus 로고    scopus 로고
    • Anthrolysin O and other gram-positive cytolysins are toll-like receptor 4 agonists
    • Park JM, Ng VH, Maeda S, Rest RF, Karin M (2004) Anthrolysin O and other gram-positive cytolysins are toll-like receptor 4 agonists. J Exp Med 200: 1647-1655.
    • (2004) J Exp Med , vol.200 , pp. 1647-1655
    • Park, J.M.1    Ng, V.H.2    Maeda, S.3    Rest, R.F.4    Karin, M.5
  • 178
    • 84878787539 scopus 로고    scopus 로고
    • Listeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccines
    • Sun R, Liu Y (2013) Listeriolysin O as a strong immunogenic molecule for the development of new anti-tumor vaccines. Hum Vaccin Immunother 9: 1058-1068.
    • (2013) Hum Vaccin Immunother , vol.9 , pp. 1058-1068
    • Sun, R.1    Liu, Y.2
  • 179
    • 84872258754 scopus 로고    scopus 로고
    • Listeria monocytogenes-derived listeriolysin O has pathogen-associated molecular pattern-like properties independent of its hemolytic ability
    • Wallecha A, Wood L, Pan ZK, Maciag PC, Shahabi V, Paterson Y (2013) Listeria monocytogenes-derived listeriolysin O has pathogen-associated molecular pattern-like properties independent of its hemolytic ability. Clin Vaccine Immunol 20: 77-84.
    • (2013) Clin Vaccine Immunol , vol.20 , pp. 77-84
    • Wallecha, A.1    Wood, L.2    Pan, Z.K.3    Maciag, P.C.4    Shahabi, V.5    Paterson, Y.6
  • 180
    • 84855882985 scopus 로고    scopus 로고
    • Mechanisms and immunological effects of apoptosis caused by Listeria monocytogenes
    • Carrero JA, Unanue ER (2012) Mechanisms and immunological effects of apoptosis caused by Listeria monocytogenes. Adv Immunol 113: 157-174.
    • (2012) Adv Immunol , vol.113 , pp. 157-174
    • Carrero, J.A.1    Unanue, E.R.2
  • 181
    • 0030070367 scopus 로고    scopus 로고
    • Listeria monocytogenes induces apoptosis of infected hepatocytes
    • Rogers HW, Callery MP, Deck B, Unanue ER (1996) Listeria monocytogenes induces apoptosis of infected hepatocytes. J Immunol 156: 679-684.
    • (1996) J Immunol , vol.156 , pp. 679-684
    • Rogers, H.W.1    Callery, M.P.2    Deck, B.3    Unanue, E.R.4
  • 182
    • 70349413075 scopus 로고    scopus 로고
    • Recombinant Listeria monocytogenes expressing a cell wall-associated listeriolysin O is weakly virulent but immunogenic
    • Carrero JA, Calderon B, Vivanco-Cid H, Unanue ER (2009) Recombinant Listeria monocytogenes expressing a cell wall-associated listeriolysin O is weakly virulent but immunogenic. Infect Immun 77: 4371-4382.
    • (2009) Infect Immun , vol.77 , pp. 4371-4382
    • Carrero, J.A.1    Calderon, B.2    Vivanco-Cid, H.3    Unanue, E.R.4
  • 183
    • 0032876692 scopus 로고    scopus 로고
    • Cutting edge: Paradigm revisited: Antibody provides resistance to Listeria infection
    • Edelson BT, Cossart P, Unanue ER (1999) Cutting edge: paradigm revisited: antibody provides resistance to Listeria infection. J Immunol 163: 4087-4090.
    • (1999) J Immunol , vol.163 , pp. 4087-4090
    • Edelson, B.T.1    Cossart, P.2    Unanue, E.R.3
  • 184
    • 0035003647 scopus 로고    scopus 로고
    • Intracellular antibody neutralizes Listeria growth
    • Edelson BT, Unanue ER (2001) Intracellular antibody neutralizes Listeria growth. Immunity 14: 503-512.
    • (2001) Immunity , vol.14 , pp. 503-512
    • Edelson, B.T.1    Unanue, E.R.2
  • 185
    • 49049094694 scopus 로고    scopus 로고
    • Granzymes drive a rapid listeriolysin Oinduced T cell apoptosis
    • Carrero JA, Vivanco-Cid H, Unanue ER (2008) Granzymes drive a rapid listeriolysin Oinduced T cell apoptosis. J Immunol 181: 1365-1374.
    • (2008) J Immunol , vol.181 , pp. 1365-1374
    • Carrero, J.A.1    Vivanco-Cid, H.2    Unanue, E.R.3
  • 186
    • 4344572356 scopus 로고    scopus 로고
    • Type I interferon sensitizes lymphocytes to apoptosis and reduces resistance to Listeria infection
    • Carrero JA, Calderon B, Unanue ER (2004) Type I interferon sensitizes lymphocytes to apoptosis and reduces resistance to Listeria infection. J Exp Med 200: 535-540.
    • (2004) J Exp Med , vol.200 , pp. 535-540
    • Carrero, J.A.1    Calderon, B.2    Unanue, E.R.3
  • 187
    • 35348839575 scopus 로고    scopus 로고
    • Impact of lymphocyte apoptosis on the innate immune stages of infection
    • Carrero JA, Unanue ER (2007) Impact of lymphocyte apoptosis on the innate immune stages of infection. Immunol Res 38: 333-341.
    • (2007) Immunol Res , vol.38 , pp. 333-341
    • Carrero, J.A.1    Unanue, E.R.2
  • 188
    • 83755177932 scopus 로고    scopus 로고
    • Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes
    • Cossart P (2011) Illuminating the landscape of host-pathogen interactions with the bacterium Listeria monocytogenes. Proc Natl Acad Sci USA 108: 19484-19491.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 19484-19491
    • Cossart, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.