메뉴 건너뛰기




Volumn 22, Issue 7, 2014, Pages 406-416

Clostridium difficile spore biology: Sporulation, germination, and spore structural proteins

Author keywords

C. difficile spores; Exosporium; Germination; Spore coat; Sporulation

Indexed keywords

PROTEIN COTA; PROTEIN COTCB; PROTEIN COTD; PROTEIN COTE; PROTEIN COTF; PROTEIN SPOIVA; PROTEIN SPOVM; SPORE STRUCTURAL PROTEIN; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN;

EID: 84903612457     PISSN: 0966842X     EISSN: 18784380     Source Type: Journal    
DOI: 10.1016/j.tim.2014.04.003     Document Type: Review
Times cited : (325)

References (75)
  • 1
    • 67649391053 scopus 로고    scopus 로고
    • Clostridium difficile infection: new developments in epidemiology and pathogenesis
    • Rupnik M., et al. Clostridium difficile infection: new developments in epidemiology and pathogenesis. Nat. Rev. Microbiol. 2009, 7:526-536.
    • (2009) Nat. Rev. Microbiol. , vol.7 , pp. 526-536
    • Rupnik, M.1
  • 2
    • 55249105923 scopus 로고    scopus 로고
    • Clostridium difficile - more difficult than ever
    • Kelly C.P., LaMont J.T. Clostridium difficile - more difficult than ever. N. Engl. J. Med. 2008, 359:1932-1940.
    • (2008) N. Engl. J. Med. , vol.359 , pp. 1932-1940
    • Kelly, C.P.1    LaMont, J.T.2
  • 3
    • 0032152205 scopus 로고    scopus 로고
    • Epidemiology, risk factors and treatments for antibiotic-associated diarrhea
    • McFarland L.V. Epidemiology, risk factors and treatments for antibiotic-associated diarrhea. Dig. Dis. 1998, 16:292-307.
    • (1998) Dig. Dis. , vol.16 , pp. 292-307
    • McFarland, L.V.1
  • 4
    • 84866354679 scopus 로고    scopus 로고
    • Infecciones causadas por Clostridium difficile: una visión actualizada
    • Hernández-Rocha C., et al. Infecciones causadas por Clostridium difficile: una visión actualizada. Rev. Chilena Infectol. 2012, 29:434-445.
    • (2012) Rev. Chilena Infectol. , vol.29 , pp. 434-445
    • Hernández-Rocha, C.1
  • 5
    • 79952585695 scopus 로고    scopus 로고
    • Comparison of the burdens of hospital-onset, healthcare facility-associated Clostridium difficile infection and of healthcare-associated infection due to methicillin-resistant Staphylococcus aureus in community hospitals
    • Miller B.A., et al. Comparison of the burdens of hospital-onset, healthcare facility-associated Clostridium difficile infection and of healthcare-associated infection due to methicillin-resistant Staphylococcus aureus in community hospitals. Infect. Control Hosp. Epidemiol. 2011, 32:387-390.
    • (2011) Infect. Control Hosp. Epidemiol. , vol.32 , pp. 387-390
    • Miller, B.A.1
  • 6
    • 34547635096 scopus 로고    scopus 로고
    • Vegetative Clostridium difficile survives in room air on moist surfaces and in gastric contents with reduced acidity: a potential mechanism to explain the association between proton pump inhibitors and C. difficile-associated diarrhea?
    • Jump R.L., et al. Vegetative Clostridium difficile survives in room air on moist surfaces and in gastric contents with reduced acidity: a potential mechanism to explain the association between proton pump inhibitors and C. difficile-associated diarrhea?. Antimicrob. Agents Chemother. 2007, 51:2883-2887.
    • (2007) Antimicrob. Agents Chemother. , vol.51 , pp. 2883-2887
    • Jump, R.L.1
  • 7
    • 84864821482 scopus 로고    scopus 로고
    • Clostridium difficile spo0A gene is a persistence and transmission factor
    • Deakin L.J., et al. Clostridium difficile spo0A gene is a persistence and transmission factor. Infect. Immun. 2012, 80:2704-2711.
    • (2012) Infect. Immun. , vol.80 , pp. 2704-2711
    • Deakin, L.J.1
  • 8
    • 60649089055 scopus 로고    scopus 로고
    • Activity of vancomycin against epidemic Clostridium difficile strains in a human gut model
    • Baines S.D., et al. Activity of vancomycin against epidemic Clostridium difficile strains in a human gut model. J. Antimicrob. Chemother. 2009, 63:520-525.
    • (2009) J. Antimicrob. Chemother. , vol.63 , pp. 520-525
    • Baines, S.D.1
  • 9
    • 84856736130 scopus 로고    scopus 로고
    • Interactions between Clostridium perfringens spores and Raw 264.7 macrophages
    • Paredes-Sabja D., Sarker M.R. Interactions between Clostridium perfringens spores and Raw 264.7 macrophages. Anaerobe 2012, 18:148-156.
    • (2012) Anaerobe , vol.18 , pp. 148-156
    • Paredes-Sabja, D.1    Sarker, M.R.2
  • 10
    • 80051470106 scopus 로고    scopus 로고
    • Spread and persistence of Clostridium difficile spores during and after cleaning with sporicidal disinfectants
    • Ali S., et al. Spread and persistence of Clostridium difficile spores during and after cleaning with sporicidal disinfectants. J. Hosp. Infect. 2011, 79:97-98.
    • (2011) J. Hosp. Infect. , vol.79 , pp. 97-98
    • Ali, S.1
  • 11
    • 34547640042 scopus 로고    scopus 로고
    • Structure, assembly, and function of the spore surface layers
    • Henriques A.O., Moran C.P. Structure, assembly, and function of the spore surface layers. Annu. Rev. Microbiol. 2007, 61:555-588.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 555-588
    • Henriques, A.O.1    Moran, C.P.2
  • 12
    • 79952465087 scopus 로고    scopus 로고
    • Germination of spores of Bacillales and Clostridiales species: mechanisms and proteins involved
    • Paredes-Sabja D., et al. Germination of spores of Bacillales and Clostridiales species: mechanisms and proteins involved. Trends Microbiol. 2011, 19:85-94.
    • (2011) Trends Microbiol. , vol.19 , pp. 85-94
    • Paredes-Sabja, D.1
  • 13
    • 84884601793 scopus 로고    scopus 로고
    • Global analysis of the sporulation pathway of Clostridium difficile
    • Fimlaid K.A., et al. Global analysis of the sporulation pathway of Clostridium difficile. PLoS Genet. 2013, 9:e1003660. 10.1371/journal.pgen.1003660.
    • (2013) PLoS Genet. , vol.9
    • Fimlaid, K.A.1
  • 14
    • 84874760766 scopus 로고    scopus 로고
    • Structural and functional analysis of the CspB protease required for Clostridium spore germination
    • Adams C.M., et al. Structural and functional analysis of the CspB protease required for Clostridium spore germination. PLoS Pathog. 2013, 9:e1003165. 10.1371/journal.ppat.1003165.
    • (2013) PLoS Pathog. , vol.9
    • Adams, C.M.1
  • 15
    • 84878518519 scopus 로고    scopus 로고
    • Bile acid recognition by the Clostridium difficile germinant receptor, CspC, is important for establishing infection
    • Francis M.B., et al. Bile acid recognition by the Clostridium difficile germinant receptor, CspC, is important for establishing infection. PLoS Pathog. 2013, 9:e1003356. 10.1371/journal.ppat.1003356.
    • (2013) PLoS Pathog. , vol.9
    • Francis, M.B.1
  • 16
    • 84887306016 scopus 로고    scopus 로고
    • The spore differentiation pathway in the enteric pathogen Clostridium difficile
    • Pereira F.C., et al. The spore differentiation pathway in the enteric pathogen Clostridium difficile. PLoS Genet. 2013, 9:e1003782. 10.1371/journal.pgen.1003782.
    • (2013) PLoS Genet. , vol.9
    • Pereira, F.C.1
  • 17
    • 84887269162 scopus 로고    scopus 로고
    • Genome-wide analysis of cell type-specific gene transcription during spore formation in Clostridium difficile
    • Saujet L., et al. Genome-wide analysis of cell type-specific gene transcription during spore formation in Clostridium difficile. PLoS Genet. 2013, 9:e1003756. 10.1371/journal.pgen.1003756.
    • (2013) PLoS Genet. , vol.9
    • Saujet, L.1
  • 18
    • 84885217530 scopus 로고    scopus 로고
    • In pursuit of protein targets: proteomic characterization of bacterial spore outer layers
    • Abhyankar W., et al. In pursuit of protein targets: proteomic characterization of bacterial spore outer layers. J. Proteome Res. 2013, 12:4507-4521.
    • (2013) J. Proteome Res. , vol.12 , pp. 4507-4521
    • Abhyankar, W.1
  • 19
    • 84889598919 scopus 로고    scopus 로고
    • Characterization of the collagen-like exosporium protein, BclA1, of Clostridium difficile spores
    • Pizarro-Guajardo M., et al. Characterization of the collagen-like exosporium protein, BclA1, of Clostridium difficile spores. Anaerobe 2014, 25:18-30.
    • (2014) Anaerobe , vol.25 , pp. 18-30
    • Pizarro-Guajardo, M.1
  • 20
    • 68949097598 scopus 로고    scopus 로고
    • Proteomic and genomic characterization of highly infectious Clostridium difficile 630 spores
    • Lawley T.D., et al. Proteomic and genomic characterization of highly infectious Clostridium difficile 630 spores. J. Bacteriol. 2009, 191:5377-5386.
    • (2009) J. Bacteriol. , vol.191 , pp. 5377-5386
    • Lawley, T.D.1
  • 21
    • 84855393816 scopus 로고    scopus 로고
    • Surface layers of Clostridium difficile endospores
    • Permpoonpattana P., et al. Surface layers of Clostridium difficile endospores. J. Bacteriol. 2011, 193:6461-6470.
    • (2011) J. Bacteriol. , vol.193 , pp. 6461-6470
    • Permpoonpattana, P.1
  • 22
    • 84875531755 scopus 로고    scopus 로고
    • Functional characterization of Clostridium difficile spore coat proteins
    • Permpoonpattana P., et al. Functional characterization of Clostridium difficile spore coat proteins. J. Bacteriol. 2013, 195:1492-1503.
    • (2013) J. Bacteriol. , vol.195 , pp. 1492-1503
    • Permpoonpattana, P.1
  • 23
    • 84883515579 scopus 로고    scopus 로고
    • The Clostridium difficile exosporium cystein (CdeC) rich protein is required for exosporium morphogenesis and coat assembly
    • Barra-Carrasco J., et al. The Clostridium difficile exosporium cystein (CdeC) rich protein is required for exosporium morphogenesis and coat assembly. J. Bacteriol. 2013, 195:3863-3875.
    • (2013) J. Bacteriol. , vol.195 , pp. 3863-3875
    • Barra-Carrasco, J.1
  • 24
    • 84884402463 scopus 로고    scopus 로고
    • Insights into the adaptive strategies and pathogenesis of Clostridium difficile from in vivo transcriptomics
    • Janoir C., et al. Insights into the adaptive strategies and pathogenesis of Clostridium difficile from in vivo transcriptomics. Infect. Immun. 2013, 81:3757-3769.
    • (2013) Infect. Immun. , vol.81 , pp. 3757-3769
    • Janoir, C.1
  • 25
    • 84865170905 scopus 로고    scopus 로고
    • Adherence of Clostridium difficile spores to Caco-2 cells in culture
    • Paredes-Sabja D., Sarker M.R. Adherence of Clostridium difficile spores to Caco-2 cells in culture. J. Med. Microbiol. 2012, 61:1208-1218.
    • (2012) J. Med. Microbiol. , vol.61 , pp. 1208-1218
    • Paredes-Sabja, D.1    Sarker, M.R.2
  • 26
    • 83355169571 scopus 로고    scopus 로고
    • Recent progress in Bacillus subtilis sporulation
    • Higgins D., Dworkin J. Recent progress in Bacillus subtilis sporulation. FEMS Microbiol. Rev. 2012, 36:131-148.
    • (2012) FEMS Microbiol. Rev. , vol.36 , pp. 131-148
    • Higgins, D.1    Dworkin, J.2
  • 27
    • 79955011057 scopus 로고    scopus 로고
    • Multiple orphan histidine kinases interact directly with Spo0A to control the initiation of endospore formation in Clostridium acetobutylicum
    • Steiner E., et al. Multiple orphan histidine kinases interact directly with Spo0A to control the initiation of endospore formation in Clostridium acetobutylicum. Mol. Microbiol. 2011, 80:641-654.
    • (2011) Mol. Microbiol. , vol.80 , pp. 641-654
    • Steiner, E.1
  • 28
    • 71749105366 scopus 로고    scopus 로고
    • Characterization of the sporulation initiation pathway of Clostridium difficile and its role in toxin production
    • Underwood S., et al. Characterization of the sporulation initiation pathway of Clostridium difficile and its role in toxin production. J. Bacteriol. 2009, 191:7296-7305.
    • (2009) J. Bacteriol. , vol.191 , pp. 7296-7305
    • Underwood, S.1
  • 29
    • 77956533047 scopus 로고    scopus 로고
    • Hierarchical evolution of the bacterial sporulation network
    • de Hoon M.J., et al. Hierarchical evolution of the bacterial sporulation network. Curr. Biol. 2010, 20:R735-R745. 10.1016/j.cub.2010.06.031.
    • (2010) Curr. Biol. , vol.20
    • de Hoon, M.J.1
  • 30
    • 0038349278 scopus 로고    scopus 로고
    • Efficient sporulation in Clostridium difficile requires disruption of the sigmaK gene
    • Haraldsen J.D., Sonenshein A.L. Efficient sporulation in Clostridium difficile requires disruption of the sigmaK gene. Mol. Microbiol. 2003, 48:811-821.
    • (2003) Mol. Microbiol. , vol.48 , pp. 811-821
    • Haraldsen, J.D.1    Sonenshein, A.L.2
  • 31
    • 84890906688 scopus 로고    scopus 로고
    • SigmaK of Clostridium acetobutylicum is the first known sporulation-specific sigma factor with two developmentally separated roles, one early and one late in sporulation
    • Al-Hinai M.A., et al. sigmaK of Clostridium acetobutylicum is the first known sporulation-specific sigma factor with two developmentally separated roles, one early and one late in sporulation. J. Bacteriol. 2014, 196:287-299.
    • (2014) J. Bacteriol. , vol.196 , pp. 287-299
    • Al-Hinai, M.A.1
  • 32
    • 65249122396 scopus 로고    scopus 로고
    • Sporulation and enterotoxin (CPE) synthesis are controlled by the sporulation-specific sigma factors SigE and SigK in Clostridium perfringens
    • Harry K.H., et al. Sporulation and enterotoxin (CPE) synthesis are controlled by the sporulation-specific sigma factors SigE and SigK in Clostridium perfringens. J. Bacteriol. 2009, 191:2728-2742.
    • (2009) J. Bacteriol. , vol.191 , pp. 2728-2742
    • Harry, K.H.1
  • 33
    • 84885176098 scopus 로고    scopus 로고
    • A genomic update on clostridial phylogeny: Gram-negative spore formers and other misplaced clostridia
    • Yutin N., Galperin M.Y. A genomic update on clostridial phylogeny: Gram-negative spore formers and other misplaced clostridia. Environ. Microbiol. 2013, 15:2631-2641.
    • (2013) Environ. Microbiol. , vol.15 , pp. 2631-2641
    • Yutin, N.1    Galperin, M.Y.2
  • 34
    • 84874406124 scopus 로고    scopus 로고
    • Proteases and sonication specifically remove the exosporium layer of spores of Clostridium difficile strain 630
    • Escobar-Cortes K., et al. Proteases and sonication specifically remove the exosporium layer of spores of Clostridium difficile strain 630. J. Microbiol. Methods 2013, 93:25-31.
    • (2013) J. Microbiol. Methods , vol.93 , pp. 25-31
    • Escobar-Cortes, K.1
  • 35
    • 84868611293 scopus 로고    scopus 로고
    • The contribution of the spore to the ability of Clostridium difficile to adhere to surfaces
    • Joshi L.T., et al. The contribution of the spore to the ability of Clostridium difficile to adhere to surfaces. Appl. Environ. Microbiol. 2012, 78:7671-7679.
    • (2012) Appl. Environ. Microbiol. , vol.78 , pp. 7671-7679
    • Joshi, L.T.1
  • 36
    • 18944408290 scopus 로고    scopus 로고
    • The ExsA protein of Bacillus cereus is required for assembly of coat and exosporium onto the spore surface
    • Bailey-Smith K., et al. The ExsA protein of Bacillus cereus is required for assembly of coat and exosporium onto the spore surface. J. Bacteriol. 2005, 187:3800-3806.
    • (2005) J. Bacteriol. , vol.187 , pp. 3800-3806
    • Bailey-Smith, K.1
  • 37
    • 34247373153 scopus 로고    scopus 로고
    • Non-uniform assembly of the Bacillus anthracis exosporium and a bottle cap model for spore germination and outgrowth
    • Steichen C.T., et al. Non-uniform assembly of the Bacillus anthracis exosporium and a bottle cap model for spore germination and outgrowth. Mol. Microbiol. 2007, 64:359-367.
    • (2007) Mol. Microbiol. , vol.64 , pp. 359-367
    • Steichen, C.T.1
  • 38
    • 33846601807 scopus 로고    scopus 로고
    • Morphogenesis of the Bacillus anthracis spore
    • Giorno R., et al. Morphogenesis of the Bacillus anthracis spore. J. Bacteriol. 2007, 189:691-705.
    • (2007) J. Bacteriol. , vol.189 , pp. 691-705
    • Giorno, R.1
  • 39
    • 84899666921 scopus 로고    scopus 로고
    • Spore formation and toxin production in Clostridium difficile biofilms
    • Semenyuk E.G., et al. Spore formation and toxin production in Clostridium difficile biofilms. PLoS ONE 2014, 9:e87757. 10.1371/journal.pone.0087757.
    • (2014) PLoS ONE , vol.9
    • Semenyuk, E.G.1
  • 40
    • 33846206774 scopus 로고    scopus 로고
    • Surface appendages of bacterial spores
    • Driks A. Surface appendages of bacterial spores. Mol. Microbiol. 2007, 63:623-625.
    • (2007) Mol. Microbiol. , vol.63 , pp. 623-625
    • Driks, A.1
  • 41
    • 84865423020 scopus 로고    scopus 로고
    • Clostridium difficile spore-macrophage interactions: spore survival
    • Paredes-Sabja D., et al. Clostridium difficile spore-macrophage interactions: spore survival. PLoS ONE 2012, 7:e43635. 10.1371/journal.pone.0043635.
    • (2012) PLoS ONE , vol.7
    • Paredes-Sabja, D.1
  • 42
    • 84871292768 scopus 로고    scopus 로고
    • The Bacillus subtilis endospore: assembly and functions of the multilayered coat
    • McKenney P.T., et al. The Bacillus subtilis endospore: assembly and functions of the multilayered coat. Nat. Rev. Microbiol. 2013, 11:33-44.
    • (2013) Nat. Rev. Microbiol. , vol.11 , pp. 33-44
    • McKenney, P.T.1
  • 43
    • 84867988931 scopus 로고    scopus 로고
    • Genomic determinants of sporulation in Bacilli and Clostridia: towards the minimal set of sporulation-specific genes
    • Galperin M.Y., et al. Genomic determinants of sporulation in Bacilli and Clostridia: towards the minimal set of sporulation-specific genes. Environ. Microbiol. 2012, 14:2870-2890.
    • (2012) Environ. Microbiol. , vol.14 , pp. 2870-2890
    • Galperin, M.Y.1
  • 44
    • 84874693324 scopus 로고    scopus 로고
    • SpoIVA and SipL are Clostridium difficile spore morphogenetic proteins
    • Putnam E.E., et al. SpoIVA and SipL are Clostridium difficile spore morphogenetic proteins. J. Bacteriol. 2013, 195:1214-1225.
    • (2013) J. Bacteriol. , vol.195 , pp. 1214-1225
    • Putnam, E.E.1
  • 45
    • 84860593197 scopus 로고    scopus 로고
    • Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis
    • Ebmeier S.E., et al. Small proteins link coat and cortex assembly during sporulation in Bacillus subtilis. Mol. Microbiol. 2012, 84:682-696.
    • (2012) Mol. Microbiol. , vol.84 , pp. 682-696
    • Ebmeier, S.E.1
  • 46
    • 84855804122 scopus 로고    scopus 로고
    • Dynamics of spore coat morphogenesis in Bacillus subtilis
    • McKenney P.T., Eichenberger P. Dynamics of spore coat morphogenesis in Bacillus subtilis. Mol. Microbiol. 2012, 83:245-260.
    • (2012) Mol. Microbiol. , vol.83 , pp. 245-260
    • McKenney, P.T.1    Eichenberger, P.2
  • 47
    • 0035025713 scopus 로고    scopus 로고
    • SpoVID guides SafA to the spore coat in Bacillus subtilis
    • Ozin A.J., et al. SpoVID guides SafA to the spore coat in Bacillus subtilis. J. Bacteriol. 2001, 183:3041-3049.
    • (2001) J. Bacteriol. , vol.183 , pp. 3041-3049
    • Ozin, A.J.1
  • 48
    • 70350432748 scopus 로고    scopus 로고
    • The coat morphogenetic protein SpoVID is necessary for spore encasement in Bacillus subtilis
    • Wang K.H., et al. The coat morphogenetic protein SpoVID is necessary for spore encasement in Bacillus subtilis. Mol. Microbiol. 2009, 74:634-649.
    • (2009) Mol. Microbiol. , vol.74 , pp. 634-649
    • Wang, K.H.1
  • 49
    • 33745550745 scopus 로고    scopus 로고
    • The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome
    • Sebaihia M., et al. The multidrug-resistant human pathogen Clostridium difficile has a highly mobile, mosaic genome. Nat. Genet. 2006, 38:779-786.
    • (2006) Nat. Genet. , vol.38 , pp. 779-786
    • Sebaihia, M.1
  • 50
    • 0031955996 scopus 로고    scopus 로고
    • Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis
    • Henriques A.O., et al. Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis. J. Bacteriol. 1998, 180:2285-2291.
    • (1998) J. Bacteriol. , vol.180 , pp. 2285-2291
    • Henriques, A.O.1
  • 51
    • 79959449569 scopus 로고    scopus 로고
    • Immunization with Bacillus spores expressing toxin A peptide repeats protects against infection with Clostridium difficile strains producing toxins A and B
    • Permpoonpattana P., et al. Immunization with Bacillus spores expressing toxin A peptide repeats protects against infection with Clostridium difficile strains producing toxins A and B. Infect. Immun. 2011, 79:2295-2302.
    • (2011) Infect. Immun. , vol.79 , pp. 2295-2302
    • Permpoonpattana, P.1
  • 52
    • 84876544830 scopus 로고    scopus 로고
    • A new strategy for the prevention of Clostridium difficile infection
    • Howerton A., et al. A new strategy for the prevention of Clostridium difficile infection. J. Infect. Dis. 2013, 207:1498-1504.
    • (2013) J. Infect. Dis. , vol.207 , pp. 1498-1504
    • Howerton, A.1
  • 53
    • 65249186376 scopus 로고    scopus 로고
    • SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens
    • Paredes-Sabja D., et al. SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens. J. Bacteriol. 2009, 191:2711-2720.
    • (2009) J. Bacteriol. , vol.191 , pp. 2711-2720
    • Paredes-Sabja, D.1
  • 54
    • 70349421685 scopus 로고    scopus 로고
    • The protease CspB is essential for initiation of cortex hydrolysis and DPA release during spore germination of Clostridium perfringens type A food poisoning isolates
    • Paredes-Sabja D., et al. The protease CspB is essential for initiation of cortex hydrolysis and DPA release during spore germination of Clostridium perfringens type A food poisoning isolates. Microbiology 2009, 155:3464-3472.
    • (2009) Microbiology , vol.155 , pp. 3464-3472
    • Paredes-Sabja, D.1
  • 55
    • 0034981754 scopus 로고    scopus 로고
    • Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involved in the activity
    • Shimamoto S., et al. Partial characterization of an enzyme fraction with protease activity which converts the spore peptidoglycan hydrolase (SleC) precursor to an active enzyme during germination of Clostridium perfringens S40 spores and analysis of a gene cluster involved in the activity. J. Bacteriol. 2001, 183:3742-3751.
    • (2001) J. Bacteriol. , vol.183 , pp. 3742-3751
    • Shimamoto, S.1
  • 56
    • 41549142775 scopus 로고    scopus 로고
    • Bile salts and glycine as co-germinants for Clostridium difficile spores
    • Sorg J.A., Sonenshein A.L. Bile salts and glycine as co-germinants for Clostridium difficile spores. J. Bacteriol. 2008, 190:2505-2512.
    • (2008) J. Bacteriol. , vol.190 , pp. 2505-2512
    • Sorg, J.A.1    Sonenshein, A.L.2
  • 57
    • 79954578379 scopus 로고    scopus 로고
    • Histidine acts as a co-germinant with glycine and taurocholate for Clostridium difficile spores
    • Wheeldon L.J., et al. Histidine acts as a co-germinant with glycine and taurocholate for Clostridium difficile spores. J. Appl. Microbiol. 2011, 110:987-994.
    • (2011) J. Appl. Microbiol. , vol.110 , pp. 987-994
    • Wheeldon, L.J.1
  • 58
    • 78650157537 scopus 로고    scopus 로고
    • Mapping interactions between germinants and Clostridium difficile spores
    • Howerton A., et al. Mapping interactions between germinants and Clostridium difficile spores. J. Bacteriol. 2011, 193:274-282.
    • (2011) J. Bacteriol. , vol.193 , pp. 274-282
    • Howerton, A.1
  • 59
    • 84857472906 scopus 로고    scopus 로고
    • Spores of Clostridium difficile clinical isolates display a diverse germination response to bile salts
    • Heeg D., et al. Spores of Clostridium difficile clinical isolates display a diverse germination response to bile salts. PLoS ONE 2012, 7:e32381. 10.1371/journal.pone.0032381.
    • (2012) PLoS ONE , vol.7
    • Heeg, D.1
  • 60
    • 63449096364 scopus 로고    scopus 로고
    • Chenodeoxycholate is an inhibitor of Clostridium difficile spore germination
    • Sorg J.A., Sonenshein A.L. Chenodeoxycholate is an inhibitor of Clostridium difficile spore germination. J. Bacteriol. 2009, 191:1115-1117.
    • (2009) J. Bacteriol. , vol.191 , pp. 1115-1117
    • Sorg, J.A.1    Sonenshein, A.L.2
  • 61
    • 76649121515 scopus 로고    scopus 로고
    • A mariner-based transposon system for in vivo random mutagenesis of Clostridium difficile
    • Cartman S.T., Minton N.P. A mariner-based transposon system for in vivo random mutagenesis of Clostridium difficile. Appl. Environ. Microbiol. 2010, 76:1103-1109.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 1103-1109
    • Cartman, S.T.1    Minton, N.P.2
  • 62
    • 75149112859 scopus 로고    scopus 로고
    • SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate
    • Burns D.A., et al. SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate. J. Bacteriol. 2010, 192:657-664.
    • (2010) J. Bacteriol. , vol.192 , pp. 657-664
    • Burns, D.A.1
  • 63
    • 84891621197 scopus 로고    scopus 로고
    • Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination
    • Gutelius D., et al. Functional analysis of SleC from Clostridium difficile: an essential lytic transglycosylase involved in spore germination. Microbiology 2014, 160:209-216.
    • (2014) Microbiology , vol.160 , pp. 209-216
    • Gutelius, D.1
  • 64
    • 0026500823 scopus 로고
    • Crisscross regulation of cell-type-specific gene expression during development in B. subtilis
    • Losick R., Stragier P. Crisscross regulation of cell-type-specific gene expression during development in B. subtilis. Nature 1992, 355:601-604.
    • (1992) Nature , vol.355 , pp. 601-604
    • Losick, R.1    Stragier, P.2
  • 65
    • 0026317041 scopus 로고
    • Establishment of cell type by compartmentalized activation of a transcription factor
    • Margolis P., et al. Establishment of cell type by compartmentalized activation of a transcription factor. Science 1991, 254:562-565.
    • (1991) Science , vol.254 , pp. 562-565
    • Margolis, P.1
  • 66
    • 0028787402 scopus 로고
    • Extracellular signal protein triggering the proteolytic activation of a developmental transcription factor in B. subtilis
    • Hofmeister A.E., et al. Extracellular signal protein triggering the proteolytic activation of a developmental transcription factor in B. subtilis. Cell 1995, 83:219-226.
    • (1995) Cell , vol.83 , pp. 219-226
    • Hofmeister, A.E.1
  • 67
    • 65249114670 scopus 로고    scopus 로고
    • A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis
    • Camp A.H., Losick R. A feeding tube model for activation of a cell-specific transcription factor during sporulation in Bacillus subtilis. Genes Dev. 2009, 23:1014-1024.
    • (2009) Genes Dev. , vol.23 , pp. 1014-1024
    • Camp, A.H.1    Losick, R.2
  • 68
    • 0026029387 scopus 로고
    • Forespore-specific transcription of a gene in the signal transduction pathway that governs pro-sigma K processing in Bacillus subtilis
    • Cutting S., et al. Forespore-specific transcription of a gene in the signal transduction pathway that governs pro-sigma K processing in Bacillus subtilis. Genes Dev. 1991, 5:456-466.
    • (1991) Genes Dev. , vol.5 , pp. 456-466
    • Cutting, S.1
  • 69
    • 34047126471 scopus 로고    scopus 로고
    • I will survive: DNA protection in bacterial spores
    • Setlow P. I will survive: DNA protection in bacterial spores. Trends. Microbiol. 2007, 15:172-180.
    • (2007) Trends. Microbiol. , vol.15 , pp. 172-180
    • Setlow, P.1
  • 70
    • 2442715189 scopus 로고    scopus 로고
    • Lipids in the inner membrane of dormant spores of Bacillus species are largely immobile
    • Cowan A.E., et al. Lipids in the inner membrane of dormant spores of Bacillus species are largely immobile. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:7733-7738.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 7733-7738
    • Cowan, A.E.1
  • 71
    • 33744733251 scopus 로고    scopus 로고
    • Spores of Bacillus subtilis: their resistance to and killing by radiation, heat and chemicals
    • Setlow P. Spores of Bacillus subtilis: their resistance to and killing by radiation, heat and chemicals. J. Appl. Microbiol. 2006, 101:514-525.
    • (2006) J. Appl. Microbiol. , vol.101 , pp. 514-525
    • Setlow, P.1
  • 72
    • 0014585139 scopus 로고
    • Structure of the peptidoglycan of bacterial spores: occurrence of the lactam of muramic acid
    • Warth A.D., Strominger J.L. Structure of the peptidoglycan of bacterial spores: occurrence of the lactam of muramic acid. Proc. Natl. Acad. Sci. U.S.A. 1969, 64:528-535.
    • (1969) Proc. Natl. Acad. Sci. U.S.A. , vol.64 , pp. 528-535
    • Warth, A.D.1    Strominger, J.L.2
  • 73
    • 0015502657 scopus 로고
    • Structure of the peptidoglycan from spores of Bacillus subtilis
    • Warth A.D., Strominger J.L. Structure of the peptidoglycan from spores of Bacillus subtilis. Biochemistry 1972, 11:1389-1396.
    • (1972) Biochemistry , vol.11 , pp. 1389-1396
    • Warth, A.D.1    Strominger, J.L.2
  • 74
    • 79956361126 scopus 로고    scopus 로고
    • Germination response of spores of the pathogenic bacterium Clostridium perfringens and Clostridium difficile to cultured human epithelial cells
    • Paredes-Sabja D., Sarker M.R. Germination response of spores of the pathogenic bacterium Clostridium perfringens and Clostridium difficile to cultured human epithelial cells. Anaerobe 2011, 17:78-84.
    • (2011) Anaerobe , vol.17 , pp. 78-84
    • Paredes-Sabja, D.1    Sarker, M.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.