메뉴 건너뛰기




Volumn 103, Issue 1, 1999, Pages 107-115

The cytolethal distending toxin from the chancroid bacterium Haemophilus ducreyi induces cell-cycle arrest in the G2 phase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BACTERIAL TOXIN; CYCLIN DEPENDENT KINASE; DNA; GLUCOSYLTRANSFERASE; GUANOSINE TRIPHOSPHATASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; RHO FACTOR; TYROSINE; VIRULENCE FACTOR;

EID: 0032893106     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI3831     Document Type: Article
Times cited : (112)

References (50)
  • 1
    • 0021081927 scopus 로고
    • Epidemiology of chancroid and Haemophilus ducreyi in Nairobi, Kenya
    • Plummer, F.A., et al. 1983. Epidemiology of chancroid and Haemophilus ducreyi in Nairobi, Kenya. Lancet. 2:1293-1295.
    • (1983) Lancet , vol.2 , pp. 1293-1295
    • Plummer, F.A.1
  • 2
    • 0024603397 scopus 로고
    • Chancroid and Haemophilus ducreyi
    • Morse, S.A. 1989. Chancroid and Haemophilus ducreyi. Clin. Microbiol. Rev. 2:137-157.
    • (1989) Clin. Microbiol. Rev. , vol.2 , pp. 137-157
    • Morse, S.A.1
  • 3
    • 0028981507 scopus 로고
    • Chancroid and Haemophilus ducreyi: An update
    • Trees, D.L., and Morse, S.A. 1995. Chancroid and Haemophilus ducreyi: an update. Clin. Microbiol. Rev. 8:357-375.
    • (1995) Clin. Microbiol. Rev. , vol.8 , pp. 357-375
    • Trees, D.L.1    Morse, S.A.2
  • 4
    • 0025601863 scopus 로고
    • Epidemiology of sexually transmitted diseases: The global pictute
    • Schryver, A. De, and Maheus, A. 1990. Epidemiology of sexually transmitted diseases: the global pictute. Bull. World Health Organ. 68:639-654.
    • (1990) Bull. World Health Organ. , vol.68 , pp. 639-654
    • De Schryver, A.1    Maheus, A.2
  • 5
    • 0025826168 scopus 로고
    • Role of lipo-oligosaccharide in experimental dermal lesions caused by Haemophilus ducreyi
    • Campagnari, A.A., et al. 1991. Role of lipo-oligosaccharide in experimental dermal lesions caused by Haemophilus ducreyi. Infect. Immun. 59:2601-2608.
    • (1991) Infect. Immun. , vol.59 , pp. 2601-2608
    • Campagnari, A.A.1
  • 6
    • 0026922150 scopus 로고
    • The role of Haemophilus ducreyi bacteria, cytotoxin, endotoxin and antibodies in animal models for study of chancroid
    • Lagergård, T. 1992. The role of Haemophilus ducreyi bacteria, cytotoxin, endotoxin and antibodies in animal models for study of chancroid. Microb. Pathog. 13:203-217.
    • (1992) Microb. Pathog. , vol.13 , pp. 203-217
    • Lagergård, T.1
  • 7
    • 0029616070 scopus 로고
    • Cloning and characterization of the genes encoding the hemolysin of Haemophilus ducreyi
    • Palmer, L., and Munson, R.S., Jr. 1995. Cloning and characterization of the genes encoding the hemolysin of Haemophilus ducreyi. Mol. Microbiol. 18:821-830.
    • (1995) Mol. Microbiol. , vol.18 , pp. 821-830
    • Palmer, L.1    Munson R.S., Jr.2
  • 8
    • 0028847328 scopus 로고
    • Characterization of the hemolytic activity of Haemophilus ducreyi
    • Totten, P., Norn, D.V., and Stamm, W.E. 1995. Characterization of the hemolytic activity of Haemophilus ducreyi. Infect. Immun. 63:4409-4416.
    • (1995) Infect. Immun. , vol.63 , pp. 4409-4416
    • Totten, P.1    Norn, D.V.2    Stamm, W.E.3
  • 9
    • 0031845347 scopus 로고    scopus 로고
    • Evaluation of a isogenic hemolysin-deficient mutant in the human model of Haemophilus ducreyi infection
    • Palmer, K.L., et al. 1998. Evaluation of a isogenic hemolysin-deficient mutant in the human model of Haemophilus ducreyi infection. J. Infect. Dis. 178:191-199.
    • (1998) J. Infect. Dis. , vol.178 , pp. 191-199
    • Palmer, K.L.1
  • 10
    • 0026521346 scopus 로고
    • Haemophilus ducreyi, a cytotoxin-producing bacterium
    • Purvén, M., and Lagergård, T. 1992. Haemophilus ducreyi, a cytotoxin-producing bacterium. Infect. Immun. 60:1156-1162.
    • (1992) Infect. Immun. , vol.60 , pp. 1156-1162
    • Purvén, M.1    Lagergård, T.2
  • 11
    • 0027469574 scopus 로고
    • Neutralizing antibodies to Haemophilus ducreyi cytotoxin
    • Lagergård, T., and Purvén, M. 1993. Neutralizing antibodies to Haemophilus ducreyi cytotoxin. Infect. Immun. 61:1589-1592.
    • (1993) Infect. Immun. , vol.61 , pp. 1589-1592
    • Lagergård, T.1    Purvén, M.2
  • 12
    • 0030873071 scopus 로고    scopus 로고
    • Purification and identification of Haemophilus ducreyi cytotoxin using a neutralizing monoclonal antibody
    • Purvén, M., Frisk, A., Lönnroth, I., and Lagergård, T. 1997. Purification and identification of Haemophilus ducreyi cytotoxin using a neutralizing monoclonal antibody. Infect. Immun. 65:3496-3499.
    • (1997) Infect. Immun. , vol.65 , pp. 3496-3499
    • Purvén, M.1    Frisk, A.2    Lönnroth, I.3    Lagergård, T.4
  • 13
    • 0028054721 scopus 로고
    • Cloning and sequencing of the genes encoding Escherichia coli cytolethal distending toxins
    • Scott, D.A., and Kaper, J.B. 1994. Cloning and sequencing of the genes encoding Escherichia coli cytolethal distending toxins. Infect. Immun. 62:244-251.
    • (1994) Infect. Immun. , vol.62 , pp. 244-251
    • Scott, D.A.1    Kaper, J.B.2
  • 14
    • 0028045039 scopus 로고
    • Cloning, sequencing, and expression of the Escherichia coli cytolethal distending toxin genes
    • Pickett, C.L., Cottle, D.L., Pesci, E.C., and Bikah, G. 1994. Cloning, sequencing, and expression of the Escherichia coli cytolethal distending toxin genes. Infect. Immun. 62:1046-1051.
    • (1994) Infect. Immun. , vol.62 , pp. 1046-1051
    • Pickett, C.L.1    Cottle, D.L.2    Pesci, E.C.3    Bikah, G.4
  • 15
    • 0030749593 scopus 로고    scopus 로고
    • A new cytolethal distending toxin (CDT) from Escherichia coli producing CNF2 blocks HeLa cell division in G2/M phase
    • Pérès, S.V., et al. 1997. A new cytolethal distending toxin (CDT) from Escherichia coli producing CNF2 blocks HeLa cell division in G2/M phase. Mol. Microb. 24:1095-1107.
    • (1997) Mol. Microb. , vol.24 , pp. 1095-1107
    • Pérès, S.V.1
  • 16
    • 0029008918 scopus 로고
    • Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella and Vibrio and cloning and sequencing of the cdt gene from Shigella dysenteriae
    • Okuda, J., Kurazono, H., and Takeda, Y. 1995. Distribution of the cytolethal distending toxin A gene (cdtA) among species of Shigella and Vibrio and cloning and sequencing of the cdt gene from Shigella dysenteriae. Microb. Pathog. 18:167-172.
    • (1995) Microb. Pathog. , vol.18 , pp. 167-172
    • Okuda, J.1    Kurazono, H.2    Takeda, Y.3
  • 17
    • 0029935822 scopus 로고    scopus 로고
    • Prevalence of cytolethal distending toxin production in Campylobacter jejuni and relatedness of Campylobacter sp cdtB genes
    • Pickett, C.L., et al. 1996. Prevalence of cytolethal distending toxin production in Campylobacter jejuni and relatedness of Campylobacter sp cdtB genes. Infect. Immun. 64:2070-2078.
    • (1996) Infect. Immun. , vol.64 , pp. 2070-2078
    • Pickett, C.L.1
  • 18
    • 0031715028 scopus 로고    scopus 로고
    • The cell cycle-specific growth-inhibitory factor produced by Actinobacillus actinomycetemcomitans is a cytolethal distending toxin
    • Sugai, M., et al. 1998. The cell cycle-specific growth-inhibitory factor produced by Actinobacillus actinomycetemcomitans is a cytolethal distending toxin. Infect. Immun. 66:5008-5019.
    • (1998) Infect. Immun. , vol.66 , pp. 5008-5019
    • Sugai, M.1
  • 19
    • 12644261398 scopus 로고    scopus 로고
    • A diffusible cytocoxin of Haemophilus ducreyi
    • Cope, L.D., et al. 1997. A diffusible cytocoxin of Haemophilus ducreyi. Proc. Natl. Acad. Sci. USA. 94:4056-4061.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 4056-4061
    • Cope, L.D.1
  • 20
    • 0030775355 scopus 로고    scopus 로고
    • 2/M transition by preventing cdc2 protein kinase dephosphorylation and activation
    • 2/M transition by preventing cdc2 protein kinase dephosphorylation and activation. Infect. Immun. 65:5088-5095
    • (1997) Infect. Immun. , vol.65 , pp. 5088-5095
    • Comayras, C.1
  • 21
    • 0031924312 scopus 로고    scopus 로고
    • Campylobacter jejuni cytolethal distending toxin causes a G2-phase cell cycle block
    • Whitehouse, C.A., et al. 1998. Campylobacter jejuni cytolethal distending toxin causes a G2-phase cell cycle block. Infect. Immun. 66:1934-1940.
    • (1998) Infect. Immun. , vol.66 , pp. 1934-1940
    • Whitehouse, C.A.1
  • 23
    • 0023852747 scopus 로고
    • Normal keratinization in a spontaneously immortalised aneuploid human keratinocyte cell line
    • Boukamp, P., et al. 1988. Normal keratinization in a spontaneously immortalised aneuploid human keratinocyte cell line. J. Cell. Biol. 106:761-771.
    • (1988) J. Cell. Biol. , vol.106 , pp. 761-771
    • Boukamp, P.1
  • 24
    • 0029924167 scopus 로고    scopus 로고
    • UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii
    • Chaves-Olarte, E., et al. 1996. UDP-glucose deficiency in a mutant cell line protects against glucosyltransferase toxins from Clostridium difficile and Clostridium sordellii. J. Biol. Chem. 271:6925-6932.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6925-6932
    • Chaves-Olarte, E.1
  • 25
    • 0030931082 scopus 로고    scopus 로고
    • Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells
    • Chaves-Olarte, E., Weidmann, M., Eichel-Streiber, C.V., and Thelestam, M. 1997. Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells. J. Clin. Invest. 100:1734-1741.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1734-1741
    • Chaves-Olarte, E.1    Weidmann, M.2    Eichel-Streiber, C.V.3    Thelestam, M.4
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0030964567 scopus 로고    scopus 로고
    • Effect of cytolethal distending toxin on F-actin assembly and cell division in Chinese hamster ovary cells
    • Aragon, V., Chao, K., and Dreyfus, L.A. 1997. Effect of cytolethal distending toxin on F-actin assembly and cell division in Chinese hamster ovary cells. Infect. Immun. 65:3774-3780.
    • (1997) Infect. Immun. , vol.65 , pp. 3774-3780
    • Aragon, V.1    Chao, K.2    Dreyfus, L.A.3
  • 28
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. 1994. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell. Biol. 10:31-54.
    • (1994) Annu. Rev. Cell. Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 29
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M.F., Ashworth, A., and Hall, A. 1995. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science. 269:1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 30
    • 0031709077 scopus 로고    scopus 로고
    • Antibodies specific to surface antigens are not effective in complement-mediating killing of Haemophilus ducreyi
    • Frisk, A., Ahmed, H.J., Dyck, E. Van, and Lagergård, T. 1998. Antibodies specific to surface antigens are not effective in complement-mediating killing of Haemophilus ducreyi. Microb. Pathog. 25:67-75.
    • (1998) Microb. Pathog. , vol.25 , pp. 67-75
    • Frisk, A.1    Ahmed, H.J.2    Van Dyck, E.3    Lagergård, T.4
  • 31
    • 0030271882 scopus 로고    scopus 로고
    • Large clostridial cytotoxins - A family of glycosyltransferases modifying small GTP-binding proteins
    • Eichel-Streiber, C.v., Boquet, P., Sauerborn, M., and Thelestam, M. 1996. Large clostridial cytotoxins - a family of glycosyltransferases modifying small GTP-binding proteins. Trends Microbiol. 4:375-382.
    • (1996) Trends Microbiol. , vol.4 , pp. 375-382
    • Eichel-Streiber, C.V.1    Boquet, P.2    Sauerborn, M.3    Thelestam, M.4
  • 32
    • 0030567981 scopus 로고    scopus 로고
    • The Ras-related protein Ral is monoglucosylated by Clostridium sordellii lethal toxin
    • Hofmann, F., Rex, G., Aktories, K., and Just, I. 1996. The Ras-related protein Ral is monoglucosylated by Clostridium sordellii lethal toxin. Biochem. Biophys. Res. Commun. 227:77-81.
    • (1996) Biochem. Biophys. Res. Commun. , vol.227 , pp. 77-81
    • Hofmann, F.1    Rex, G.2    Aktories, K.3    Just, I.4
  • 33
    • 0028177598 scopus 로고
    • Clostridium difficile toxin B acts on the GTP-binding protein Rho
    • Just, I., et al. 1994. Clostridium difficile toxin B acts on the GTP-binding protein Rho. J. Biol. Chem. 269:10706-10712.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10706-10712
    • Just, I.1
  • 34
    • 0030610785 scopus 로고    scopus 로고
    • Gln63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1
    • Schmidt, G., et al. 1997. Gln63 of Rho is deamidated by Escherichia coli cytotoxic necrotizing factor-1. Nature. 387:725-729.
    • (1997) Nature , vol.387 , pp. 725-729
    • Schmidt, G.1
  • 35
    • 0030992838 scopus 로고    scopus 로고
    • Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine
    • Flatau, G., et al. 1997. Toxin-induced activation of the G protein p21 Rho by deamidation of glutamine. Nature. 387:729-733.
    • (1997) Nature , vol.387 , pp. 729-733
    • Flatau, G.1
  • 36
    • 0029088441 scopus 로고
    • Escherichia coli cytotoxic necrotizing factor 1: Evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase
    • Fiorentini, C., et al. 1995. Escherichia coli cytotoxic necrotizing factor 1: evidence for induction of actin assembly by constitutive activation of the p21 Rho GTPase. Infect. Immun. 63:3936-3944.
    • (1995) Infect. Immun. , vol.63 , pp. 3936-3944
    • Fiorentini, C.1
  • 37
    • 0028853961 scopus 로고
    • cdc2 activity
    • cdc2 activity. J. Virol. 69:6705-6711.
    • (1995) J. Virol. , vol.69 , pp. 6705-6711
    • He, J.1
  • 39
    • 0029993519 scopus 로고    scopus 로고
    • 2 accumulation by a mechanism which differs from DNA damage checkpoint control
    • 2 accumulation by a mechanism which differs from DNA damage checkpoint control. J. Virol. 70:2324-2331.
    • (1996) J. Virol. , vol.70 , pp. 2324-2331
    • Bartz, S.R.1    Rogel, M.E.2    Emerman, M.3
  • 40
    • 0030951420 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 vpr gene induces phenotypic effects similar to those of the DNA alkylating agent, nitrogen mustard
    • Poon, B., et al. 1997. Human immunodeficiency virus type 1 vpr gene induces phenotypic effects similar to those of the DNA alkylating agent, nitrogen mustard. J. Virol. 71:3961-3971.
    • (1997) J. Virol. , vol.71 , pp. 3961-3971
    • Poon, B.1
  • 41
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: Preventing an identity crisis
    • Elledge, S.J. 1996. Cell cycle checkpoints: preventing an identity crisis. Science. 274:1664-1671.
    • (1996) Science , vol.274 , pp. 1664-1671
    • Elledge, S.J.1
  • 43
    • 0030867582 scopus 로고    scopus 로고
    • Conservation of the Chk1 checkpoint pathway in mammals: Linkage of DNA damage to cdk regulation through Cdc25
    • Sanchez, Y., et al. 1997. Conservation of the Chk1 checkpoint pathway in mammals: linkage of DNA damage to cdk regulation through Cdc25. Science. 277:1497-1501.
    • (1997) Science , vol.277 , pp. 1497-1501
    • Sanchez, Y.1
  • 44
    • 0030665150 scopus 로고    scopus 로고
    • The role of cdc2 feedback loop control in the DNA damage checkpoint in mammalian cells
    • Poon, R.Y., Chau, M.S., Yamashita, K., and Hunter, T. 1997. The role of cdc2 feedback loop control in the DNA damage checkpoint in mammalian cells. Cancer Res. 57:5168-5178.
    • (1997) Cancer Res. , vol.57 , pp. 5168-5178
    • Poon, R.Y.1    Chau, M.S.2    Yamashita, K.3    Hunter, T.4
  • 45
    • 0031036624 scopus 로고    scopus 로고
    • Examination of diarrheageniciry of cytolethal distending toxin: Suckling mouse response to the products of the cdtABC genes of Shigella dysenteriae
    • Okuda, J., Fukumoto, M., Takeda, Y., and Nishibuchi, M. 1997. Examination of diarrheageniciry of cytolethal distending toxin: suckling mouse response to the products of the cdtABC genes of Shigella dysenteriae. Infect. Immun. 65:428-433.
    • (1997) Infect. Immun. , vol.65 , pp. 428-433
    • Okuda, J.1    Fukumoto, M.2    Takeda, Y.3    Nishibuchi, M.4
  • 46
    • 0023891492 scopus 로고
    • A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material
    • Johnson, W.M., and Lior, H. 1988. A new heat-labile cytolethal distending toxin (CLDT) produced by Escherichia coli isolates from clinical material. Microb. Pathog. 4:103-113.
    • (1988) Microb. Pathog. , vol.4 , pp. 103-113
    • Johnson, W.M.1    Lior, H.2
  • 47
    • 0029033806 scopus 로고
    • Cytotoxin production in 100 strains of Haemophilus ducreyi from different geographic locations
    • Purvén, M., Falsen, E., and Lagergård, T. 1995. Cytotoxin production in 100 strains of Haemophilus ducreyi from different geographic locations. FEMS Microbiol. Lett. 129:221-224.
    • (1995) FEMS Microbiol. Lett. , vol.129 , pp. 221-224
    • Purvén, M.1    Falsen, E.2    Lagergård, T.3
  • 48
    • 0027163207 scopus 로고
    • Evidence of Haemophilus ducreyi adherence to and destruction of human epithelial cells
    • Lagergård, T., Purvén, M., and Frisk, A. 1993. Evidence of Haemophilus ducreyi adherence to and destruction of human epithelial cells. Microb. Pathog. 14: 417-431.
    • (1993) Microb. Pathog. , vol.14 , pp. 417-431
    • Lagergård, T.1    Purvén, M.2    Frisk, A.3
  • 49
    • 0028938291 scopus 로고
    • Serum bactericidal activity and phagocytosis in host defence against Haemophilus ducreyi
    • Lagergård, T., Frisk, A., Purvén, M., and Nilsson, L.Å. 1995. Serum bactericidal activity and phagocytosis in host defence against Haemophilus ducreyi. Microb. Pathog. 18:37-51.
    • (1995) Microb. Pathog. , vol.18 , pp. 37-51
    • Lagergård, T.1    Frisk, A.2    Purvén, M.3    Nilsson, L.Å.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.