메뉴 건너뛰기




Volumn 193, Issue 23, 2011, Pages 6461-6470

Surface layers of Clostridium difficile endospores

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; CATALASE; CHITINASE; COAT PROTEIN; COTA PROTEIN; COTB PROTEIN; COTCB PROTEIN; COTD PROTEIN; COTE PROTEIN; MANGANESE; PEROXIDOXIN; UNCLASSIFIED DRUG; PEROXIREDOXIN;

EID: 84855393816     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.05182-11     Document Type: Article
Times cited : (85)

References (38)
  • 1
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers, R. F., Jr., and I. W. Sizer. 1952. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195:133-140.
    • (1952) J. Biol. Chem. , vol.195 , pp. 133-140
    • Beers Jr., R.F.1    Sizer, I.W.2
  • 2
    • 34548486969 scopus 로고    scopus 로고
    • Bacillus anthracis spores of the bclA mutant exhibit increased adherence to epithelial cells, fibroblasts, and endothelial cells but not to macrophages
    • Bozue, J., et al. 2007. Bacillus anthracis spores of the bclA mutant exhibit increased adherence to epithelial cells, fibroblasts, and endothelial cells but not to macrophages. Infect. Immun. 75:4498-4505.
    • (2007) Infect. Immun. , vol.75 , pp. 4498-4505
    • Bozue, J.1
  • 3
    • 77954848009 scopus 로고    scopus 로고
    • The role of toxin A and toxin B in Clostridium difficile-associated disease: past and present perspectives
    • Carter, G. P., J. I. Rood, and D. Lyras. 2010. The role of toxin A and toxin B in Clostridium difficile-associated disease: past and present perspectives. Gut Microbes 1:58-64.
    • (2010) Gut Microbes , vol.1 , pp. 58-64
    • Carter, G.P.1    Rood, J.I.2    Lyras, D.3
  • 4
    • 0034666290 scopus 로고    scopus 로고
    • 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities
    • Chen, J. W., C. Dodia, S. I. Feinstein, M. K. Jain, and A. B. Fisher. 2000. 1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities. J. Biol. Chem. 275:28421-28427.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28421-28427
    • Chen, J.W.1    Dodia, C.2    Feinstein, S.I.3    Jain, M.K.4    Fisher, A.B.5
  • 5
    • 3843062496 scopus 로고    scopus 로고
    • Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium
    • Daubenspeck, J. M., et al. 2004. Novel oligosaccharide side chains of the collagen-like region of BclA, the major glycoprotein of the Bacillus anthracis exosporium. J. Biol. Chem. 279:30945-30953.
    • (2004) J. Biol. Chem. , vol.279 , pp. 30945-30953
    • Daubenspeck, J.M.1
  • 7
    • 33846206774 scopus 로고    scopus 로고
    • Surface appendages of bacterial spores
    • Driks, A. 2007. Surface appendages of bacterial spores. Mol. Microbiol. 63:623-625.
    • (2007) Mol. Microbiol. , vol.63 , pp. 623-625
    • Driks, A.1
  • 8
    • 74249112137 scopus 로고    scopus 로고
    • Potential role of chitinase 3-like-1 in inflammation-associated carcinogenic changes of epithelial cells
    • Eurich, K., M. Segawa, S. Toei-Shimizu, and E. Mizoguchi. 2009. Potential role of chitinase 3-like-1 in inflammation-associated carcinogenic changes of epithelial cells. World J. Gastroenterol. 15:5249-5259.
    • (2009) World J. Gastroenterol. , vol.15 , pp. 5249-5259
    • Eurich, K.1    Segawa, M.2    Toei-Shimizu, S.3    Mizoguchi, E.4
  • 9
    • 39749111479 scopus 로고    scopus 로고
    • Measures to control and prevent Clostridium difficile infection
    • Gerding, D. N., C. A. Muto, and R. C. Owens, Jr. 2008. Measures to control and prevent Clostridium difficile infection. Clin. Infect. Dis. 46(Suppl. 1):S43-S49.
    • (2008) Clin. Infect. Dis. , vol.46 , Issue.SUPPL. 1
    • Gerding, D.N.1    Muto, C.A.2    Owens Jr., R.C.3
  • 10
    • 39749121022 scopus 로고    scopus 로고
    • Treatment of Clostridium difficile infection
    • Gerding, D. N., C. A. Muto, and R. C. Owens, Jr. 2008. Treatment of Clostridium difficile infection. Clin. Infect. Dis. 46(Suppl. 1):S32-S42.
    • (2008) Clin. Infect. Dis. , vol.46 , Issue.SUPPL. 1
    • Gerding, D.N.1    Muto, C.A.2    Owens Jr., R.C.3
  • 11
    • 66349105304 scopus 로고    scopus 로고
    • Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo
    • Greetham, D., and C. M. Grant. 2009. Antioxidant activity of the yeast mitochondrial one-Cys peroxiredoxin is dependent on thioredoxin reductase and glutathione in vivo. Mol. Cell. Biol. 29:3229-3240.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3229-3240
    • Greetham, D.1    Grant, C.M.2
  • 12
    • 0031955996 scopus 로고    scopus 로고
    • Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis
    • Henriques, A. O., L. R. Melsen, and C. P. Moran, Jr. 1998. Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis. J. Bacteriol. 180:2285-2291.
    • (1998) J. Bacteriol. , vol.180 , pp. 2285-2291
    • Henriques, A.O.1    Melsen, L.R.2    Moran Jr., C.P.3
  • 13
    • 34547640042 scopus 로고    scopus 로고
    • Structure, assembly, and function of the spore surface layers
    • Henriques, A. O., and C. P. Moran, Jr. 2007. Structure, assembly, and function of the spore surface layers. Annu. Rev. Microbiol. 61:555-588.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 555-588
    • Henriques, A.O.1    Moran Jr., C.P.2
  • 14
    • 60949087042 scopus 로고    scopus 로고
    • Bacillus subtilis isolated from the human gastrointestinal tract
    • Hong, H. A., et al. 2009. Bacillus subtilis isolated from the human gastrointestinal tract. Res. Microbiol. 160:134-143.
    • (2009) Res. Microbiol. , vol.160 , pp. 134-143
    • Hong, H.A.1
  • 15
  • 16
    • 48749084100 scopus 로고    scopus 로고
    • Chitinase 3-like-1 enhances bacterial adhesion to colonic epithelial cells through the interaction with bacterial chitin-binding protein
    • Kawada, M., et al. 2008. Chitinase 3-like-1 enhances bacterial adhesion to colonic epithelial cells through the interaction with bacterial chitin-binding protein. Lab. Invest. 88:883-895.
    • (2008) Lab. Invest. , vol.88 , pp. 883-895
    • Kawada, M.1
  • 17
    • 34247178358 scopus 로고    scopus 로고
    • Role of mammalian chitinases in inflammatory conditions
    • Kawada, M., Y. Hachiya, A. Arihiro, and E. Mizoguchi. 2007. Role of mammalian chitinases in inflammatory conditions. Keio J. Med. 56:21-27.
    • (2007) Keio J. Med. , vol.56 , pp. 21-27
    • Kawada, M.1    Hachiya, Y.2    Arihiro, A.3    Mizoguchi, E.4
  • 18
    • 69049108796 scopus 로고    scopus 로고
    • Antibiotic treatment of Clostridium difficile carrier mice triggers a supershedder state, spore-mediated transmission, and severe disease in immunocompromised hosts
    • Lawley, T. D., et al. 2009. Antibiotic treatment of Clostridium difficile carrier mice triggers a supershedder state, spore-mediated transmission, and severe disease in immunocompromised hosts. Infect. Immun. 77:3661-3669.
    • (2009) Infect. Immun. , vol.77 , pp. 3661-3669
    • Lawley, T.D.1
  • 19
    • 68949097598 scopus 로고    scopus 로고
    • Proteomic and genomic characterization of highly infectious Clostridium difficile 630 spores
    • Lawley, T. D., et al. 2009. Proteomic and genomic characterization of highly infectious Clostridium difficile 630 spores. J. Bacteriol. 191:5377-5386.
    • (2009) J. Bacteriol. , vol.191 , pp. 5377-5386
    • Lawley, T.D.1
  • 20
    • 0034730630 scopus 로고    scopus 로고
    • Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus
    • Logan, C., and S. G. Mayhew. 2000. Cloning, overexpression, and characterization of peroxiredoxin and NADH peroxiredoxin reductase from Thermus aquaticus. J. Biol. Chem. 275:30019-30028.
    • (2000) J. Biol. Chem. , vol.275 , pp. 30019-30028
    • Logan, C.1    Mayhew, S.G.2
  • 21
    • 33947204162 scopus 로고    scopus 로고
    • Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte
    • Low, F. M., M. B. Hampton, A. V. Peskin, and C. C. Winterbourn. 2007. Peroxiredoxin 2 functions as a noncatalytic scavenger of low-level hydrogen peroxide in the erythrocyte. Blood 109:2611-2617.
    • (2007) Blood , vol.109 , pp. 2611-2617
    • Low, F.M.1    Hampton, M.B.2    Peskin, A.V.3    Winterbourn, C.C.4
  • 22
    • 0042568938 scopus 로고    scopus 로고
    • Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression
    • Neumann, C. A., et al. 2003. Essential role for the peroxiredoxin Prdx1 in erythrocyte antioxidant defence and tumour suppression. Nature 424:561-565.
    • (2003) Nature , vol.424 , pp. 561-565
    • Neumann, C.A.1
  • 23
    • 0001864545 scopus 로고
    • Sporulation, germination and outgrowth
    • C. R. Harwood and S. M. Cutting (ed.), John Wiley & Sons Ltd., Chichester, United Kingdom
    • Nicholson, W. L., and P. Setlow. 1990. Sporulation, germination and outgrowth, p. 391-450. In C. R. Harwood and S. M. Cutting (ed.), Molecular biological methods for Bacillus. John Wiley & Sons Ltd., Chichester, United Kingdom.
    • (1990) Molecular biological methods for Bacillus , pp. 391-450
    • Nicholson, W.L.1    Setlow, P.2
  • 24
    • 0030772660 scopus 로고    scopus 로고
    • Exosporial membrane plasticity of Clostridium sporogenes and Clostridium difficile
    • Panessa-Warren, B. J., G. T. Tortora, and J. B. Warren. 1997. Exosporial membrane plasticity of Clostridium sporogenes and Clostridium difficile. Tissue Cell 29:449-461.
    • (1997) Tissue Cell , vol.29 , pp. 449-461
    • Panessa-Warren, B.J.1    Tortora, G.T.2    Warren, J.B.3
  • 25
    • 51149120361 scopus 로고    scopus 로고
    • Germination of spores of Clostridium difficile strains, including isolates from a hospital outbreak of Clostridium difficile-associated disease (CDAD)
    • Paredes-Sabja, D., C. Bond, R. J. Carman, P. Setlow, and M. R. Sarker. 2008. Germination of spores of Clostridium difficile strains, including isolates from a hospital outbreak of Clostridium difficile-associated disease (CDAD). Microbiology 154:2241-2250.
    • (2008) Microbiology , vol.154 , pp. 2241-2250
    • Paredes-Sabja, D.1    Bond, C.2    Carman, R.J.3    Setlow, P.4    Sarker, M.R.5
  • 26
    • 0033621685 scopus 로고    scopus 로고
    • Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein
    • Poole, L. B., M. Higuchi, M. Shimada, M. L. Calzi, and Y. Kamio. 2000. Streptococcus mutans H2O2-forming NADH oxidase is an alkyl hydroperoxide reductase protein. Free Radic. Biol. Med. 28:108-120.
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 108-120
    • Poole, L.B.1    Higuchi, M.2    Shimada, M.3    Calzi, M.L.4    Kamio, Y.5
  • 27
    • 1242318694 scopus 로고    scopus 로고
    • Identification of proteins in the exosporium of Bacillus anthracis
    • Redmond, C., L. W. Baillie, S. Hibbs, A. J. Moir, and A. Moir. 2004. Identification of proteins in the exosporium of Bacillus anthracis. Microbiology 150:355-363.
    • (2004) Microbiology , vol.150 , pp. 355-363
    • Redmond, C.1    Baillie, L.W.2    Hibbs, S.3    Moir, A.J.4    Moir, A.5
  • 28
    • 76249112140 scopus 로고    scopus 로고
    • Peroxiredoxin 1 stimulates secretion of proinflammatory cytokines by binding to TLR4
    • Riddell, J. R., X. Y. Wang, H. Minderman, and S. O. Gollnick. 2010. Peroxiredoxin 1 stimulates secretion of proinflammatory cytokines by binding to TLR4. J. Immunol. 184:1022-1030.
    • (2010) J. Immunol. , vol.184 , pp. 1022-1030
    • Riddell, J.R.1    Wang, X.Y.2    Minderman, H.3    Gollnick, S.O.4
  • 29
    • 67649391053 scopus 로고    scopus 로고
    • Clostridium difficile infection: new developments in epidemiology and pathogenesis
    • Rupnik, M., M. H. Wilcox, and D. N. Gerding. 2009. Clostridium difficile infection: new developments in epidemiology and pathogenesis. Nat. Rev. Microbiol. 7:526-536.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 526-536
    • Rupnik, M.1    Wilcox, M.H.2    Gerding, D.N.3
  • 30
    • 33745550745 scopus 로고    scopus 로고
    • The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome
    • Sebaihia, M., et al. 2006. The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat. Genet. 38:779-786.
    • (2006) Nat. Genet. , vol.38 , pp. 779-786
    • Sebaihia, M.1
  • 32
    • 28844494379 scopus 로고    scopus 로고
    • Clostridium difficile: an important pathogen of food animals
    • Songer, J. G., and M. A. Anderson. 2006. Clostridium difficile: an important pathogen of food animals. Anaerobe 12:1-4.
    • (2006) Anaerobe , vol.12 , pp. 1-4
    • Songer, J.G.1    Anderson, M.A.2
  • 33
    • 0036042515 scopus 로고    scopus 로고
    • A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium
    • Sylvestre, P., E. Couture-Tosi, and M. Mock. 2002. A collagen-like surface glycoprotein is a structural component of the Bacillus anthracis exosporium. Mol. Microbiol. 45:169-178.
    • (2002) Mol. Microbiol. , vol.45 , pp. 169-178
    • Sylvestre, P.1    Couture-Tosi, E.2    Mock, M.3
  • 35
    • 79953188682 scopus 로고    scopus 로고
    • Current physical and SDS extraction methods do not efficiently remove exosporium proteins from Bacillus anthracis spores
    • Thompson, B. M., J. M. Binkley, and G. C. Stewart. 2011. Current physical and SDS extraction methods do not efficiently remove exosporium proteins from Bacillus anthracis spores. J. Microbiol. Methods 85:143-148.
    • (2011) J. Microbiol. Methods , vol.85 , pp. 143-148
    • Thompson, B.M.1    Binkley, J.M.2    Stewart, G.C.3
  • 36
    • 84855765599 scopus 로고
    • Chemical studies on the spore coat protein of Clostridium perfringens type A
    • Tsuzuki, T., and Y. Ando. 1985. Chemical studies on the spore coat protein of Clostridium perfringens type A. Agric. Biol. Chem. 49:3221-3225.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 3221-3225
    • Tsuzuki, T.1    Ando, Y.2
  • 37
    • 42449133334 scopus 로고    scopus 로고
    • Infection control measures to limit the spread of Clostridium difficile
    • Vonberg, R. P., et al. 2008. Infection control measures to limit the spread of Clostridium difficile. Clin. Microbiol. Infect. 14(Suppl. 5):2-20.
    • (2008) Clin. Microbiol. Infect. , vol.14 , Issue.SUPPL. 5 , pp. 2-20
    • Vonberg, R.P.1
  • 38
    • 0020084325 scopus 로고
    • Use of sodium taurocholate to enhance spore recovery on a medium selective for Clostridium difficile
    • Wilson, K. H., M. J. Kennedy, and F. R. Fekety. 1982. Use of sodium taurocholate to enhance spore recovery on a medium selective for Clostridium difficile. J. Clin. Microbiol. 15:443-446.
    • (1982) J. Clin. Microbiol. , vol.15 , pp. 443-446
    • Wilson, K.H.1    Kennedy, M.J.2    Fekety, F.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.