1887
No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.

Physiology and Sporulation in

MyBook is a cheap paperback edition of the original book and will be sold at uniform, low price.
  • PDF
    441.26 Kb
  • XML
    138.01 Kb
  • HTML
    139.64 Kb
  • Author: Peter Dürre1
  • Editors: Patrick Eichenberger2, Adam Driks3
  • VIEW AFFILIATIONS HIDE AFFILIATIONS
    Affiliations: 1: Institut für Mikrobiologie und Biotechnologie, Universität Ulm, 89069 Ulm, Germany; 2: New York University, New York, NY; 3: Loyola University Medical Center, Maywood, IL
    • Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.TBS-0010-2012
  • Received 12 October 2012 Accepted 31 March 2014 Published 08 August 2014
  • P. Dürre, [email protected]
image of Physiology and Sporulation in <span class="jp-italic">Clostridium</span>
    Preview this microbiology spectrum article:
    Preview Magnify
    Zoom in
    Zoomout

    Physiology and Sporulation in , Page 1 of 2

    | /docserver/preview/fulltext/microbiolspec/2/4/TBS-0010-2012-1.gif /docserver/preview/fulltext/microbiolspec/2/4/TBS-0010-2012-2.gif

  • Abstract:

    Clostridia are Gram-positive, anaerobic, endospore-forming bacteria, incapable of dissimilatory sulfate reduction. Comprising approximately 180 species, the genus is one of the largest bacterial genera. Physiology is mostly devoted to acid production. Numerous pathways are known, such as the homoacetate fermentation by acetogens, the propionate fermentation by , and the butyrate/butanol fermentation by , a well-known solvent producer. Clostridia degrade sugars, alcohols, amino acids, purines, pyrimidines, and polymers such as starch and cellulose. Energy conservation can be performed by substrate-level phosphorylation as well as by the generation of ion gradients. Endospore formation resembles the mechanism elucidated in . Morphology, contents, and properties of spores are very similar to bacilli endospores. Sporulating clostridia usually form swollen mother cells and accumulate the storage substance granulose. However, clostridial sporulation differs by not employing the so-called phosphorelay. Initiation starts by direct phosphorylation of the master regulator Spo0A. The cascade of sporulation-specific sigma factors is again identical to what is known from . The onset of sporulation is coupled in some species to either solvent (acetone, butanol) or toxin (e.g., enterotoxin) formation. The germination of spores is often induced by various amino acids, often in combination with phosphate and sodium ions. In medical applications, spores are used as a prophylaxis and as treatment against diarrhea. Recombinant spores are currently under investigation and testing as antitumor agents, because they germinate only in hypoxic tissues (i.e., tumor tissue), allowing precise targeting and direct killing of tumor cells.

  • Citation: Dürre P. 2014. Physiology and Sporulation in . Microbiol Spectrum 2(4):TBS-0010-2012. doi:10.1128/microbiolspec.TBS-0010-2012.

References

1. Bahl H, Dürre P. 2001. Clostridia: Biotechnology and Medical Applications. Wiley-VCH, Weinheim, Germany. [CrossRef]
2. Dürre P. 2005. Handbook on Clostridia. CRC Press-Taylor and Francis Group, Boca Raton, FL. [CrossRef]
3. Dürre P. 2007. Clostridia. Encyclopedia of Life Sciences. doi:10.1002/9780470015902.a0020370. [CrossRef]
4. Dürre P. 2009. The genus Clostridium, p 339–353. In Goldman E, Green LH (ed), Practical Handbook of Microbiology, 2nd ed. CRC Press-Taylor and Francis Group, Boca Raton, FL.
5. Rood JI, McClane BA, Songer JG, Titball RW. 1997. The Clostridia: Molecular Biology and Pathogenesis. Academic Press, San Diego, CA.
6. Schiel B, Dürre P. 2010. Clostridium, p 1701–1715. In Flickinger MC (ed), Encyclopedia of Industrial Biotechnology, Bioprocess, Bioseparation, and Cell Technology, vol. 3. John Wiley & Sons, Hoboken, NJ. doi:10.1002/9780470054581.eib236 [CrossRef]
7. Wilde E, Hippe H, Tosunoglu N, Schallehn G, Herwig K, Gottschalk G. 1989. Clostridium tetanomorphum sp. nov., nom. rev. Int J Syst Bacteriol 39:127–134. [CrossRef]
8. Brüggemann H, Gottschalk G. 2004. Insights in metabolism and toxin production from the complete genome sequence of Clostridium tetani. Anaerobe 10:53–68. [PubMed][CrossRef]
9. Wieringa KT. 1936. Over het verdwijnen van waterstof en koolzuur onder anaerobe voorwaarden. Antonie van Leeuwenhoek 3:263–273. [CrossRef]
10. Braun M, Mayer F, Gottschalk G. 1981. Clostridium aceticum (Wieringa), a microorganism producing acetic acid from molecular hydrogen and carbon dioxide. Arch Microbiol 128:288–293. [PubMed][CrossRef]
11. Braun M. 1981. Charakterisierung von anaeroben autotrophen Essigsäurebildnern and Untersuchungen zur Essigsäurebildung aus Wasserstoff and Kohlendioxid durch Clostridium aceticum. Ph.D. dissertation. University of Göttingen, Germany.
12. Das A, Ljungdahl LG. 2003. Electron-transport system in acetogens, p 191–204. In Ljungdahl LG, Adams MW, Barton LL, Ferry JG (ed), Biochemistry and Physiology of Anaerobic Bacteria. Springer, New York, NY. [CrossRef]
13. Huang H, Wang S, Moll J, Thauer RK. 2012. Electron bifurcation involved in the energy metabolism of the acetogenic bacterium Moorella thermoacetica growing on glucose or H 2 plus CO 2. J Bacteriol 194:3689–3699. [PubMed][CrossRef]
14. Balch WE, Schoberth S, Tanner RS, Wolfe RS. 1977. Acetobacterium, a new genus of hydrogen-oxidizing, carbon dioxide-reducing anaerobic bacteria. Int J Syst Bacteriol 27:355–361. [CrossRef]
15. Schmehl M, Jahn A, Meyer zu Vilsendorf A, Hennecke S, Masepohl B, Schuppler M, Marxer M, Oelze J, Klipp W. 1993. Identification of a new class of nitrogen fixation genes in Rhodobacter capsulatus: a putative membrane complex involved in electron transport to nitrogenase. Mol Gen Genet 241:602–615. [PubMed][CrossRef]
16. Biegel E, Müller V. 2010. Bacterial Na +-translocating ferredoxin:NAD + oxidoreductase. Proc Natl Acad Sci USA 107:18138–18142. [PubMed][CrossRef]
17. Poehlein A, Schmidt S, Kaster A-K, Goenreich M, Vollmers J, Thürmer A, Bertsch J, Schuchmann K, Voigt B, Hecker M, Daniel R, Thauer RK, Gottschalk G, Müller V. 2012. An ancient pathway combining carbon dioxide fixation with the generation and utilization of a sodium ion gradient for ATP synthesis. PLoS One. 7(3) :e33439. doi:10.1371/journal.pone.0033439 [CrossRef]
18. Müller V. 2003. Energy conservation in acetogenic bacteria. Appl Environ Microbiol 69:6345–6353. [PubMed][CrossRef]
19. Köpke M, Held C, Hujer S, Liesegang H, Wiezer A, Wollherr A, Ehrenreich A, Liebl W, Gottschalk G, Dürre P. 2010. Clostridium ljungdahlii represents a microbial production platform based on syngas. Proc Natl Acad Sci USA 107:13087–13092. [PubMed][CrossRef]
20. Köpke M, Mihalcea C, Bromley JC, Simpson SD. 2011. Fermentative production of ethanol from carbon monoxide. Curr Opin Biotechnol 22:320–325. [PubMed][CrossRef]
21. Schiel-Bengelsdorf B, Dürre P. 2012. Pathway engineering and synthetic biology using acetogenic clostridia. FEBS Lett 586:2191–2198. [PubMed][CrossRef]
22. Hilpert W, Schink B, Dimroth P. 1984. Life by a new decarboxylation-dependent energy conservation mechanism with Na + as coupling ion. EMBO J 3:1665–1670. [PubMed]
23. Kane MB, Brauman A, Breznak JA. 1991. Clostridium mayombei sp. nov., an H 2/CO 2 acetogenic bacterium from the gut of the African soil-feeding termite, Cubitermes speciosus. Arch Microbiol 156:99–104. [CrossRef]
24. Charrier C, Duncan GJ, Reid MD, Rucklidge GJ, Henderson D, Young P, Russell VJ, Aminov RI, Flint HJ, Louis P. 2006. A novel class of CoA-transferase involved in shortchain fatty acid metabolism in butyrate-producing human colonic bacteria. Microbiology 152:179–182. [PubMed][CrossRef]
25. Louis P, Duncan SH, McCrae SI, Millar J, Jackson MS, Flint HJ. 2004. Restricted distribution of the butyrate kinase pathway among butyrate-producing bacteria from the human colon. J Bacteriol 186:2099–2106. [PubMed][CrossRef]
26. Herrmann G, Jayamani E, Mai G, Buckel W. 2008. Energy conservation via electron-transferring flavoprotein in anaerobic bacteria. J Bacteriol 190:784–791. [PubMed][CrossRef]
27. Dürre P, Bahl H, Gottschalk G. 1988. Membrane processes and product formation in anaerobes, p 187–220. In Erickson LE, Fung DY-C (ed), Handbook on Anaerobic Fermentations. Marcel Dekker Inc., New York, NY.
28. Dürre P. 2005. Formation of solvents in clostridia, p 671–693. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
29. Dürre P. 2009. Metabolic networks in Clostridium acetobutylicum: interaction of sporulation, solventogenesis and toxin formation, p 215–227. In Brüggemann H, Gottschalk G (ed), Clostridia. Molecular Biology in the Post-genomic Era. Caister Academic Press, Norfolk, United Kingdom.
30. Dürre P. 2007. Biobutanol: an attractive biofuel. Biotechnol J 2:1525–1534. [PubMed][CrossRef]
31. Dürre P. 2011. Fermentative production of butanol – the academic perspective. Curr Opin Biotechnol 22:331–336. [PubMed][CrossRef]
32. Green EM. 2011. Fermentative production of butanol – the industrial perspective. Curr Opin Biotechnol 22:337–343. [PubMed][CrossRef]
33. Lütke-Eversloh T, Bahl H. 2011. Metabolic engineering of Clostridium acetobutylicum: recent advances to improve butanol production. Curr Opin Biotechnol 22:634–647. [PubMed][CrossRef]
34. Kenealy WR, Waselefsky DM. 1985. Studies on the substrate range of Clostridium kluyveri: the use of propanol and succinate. Arch Microbiol 141:187–194. [CrossRef]
35. Gaston LW, Stadtman ER. 1963. Fermentation of ethylene glycol by Clostridium glycolicum, sp. n. J Bacteriol 85:356–362. [PubMed]
36. Schink B. 1984. Clostridium magnum sp. nov., a non-autotrophic homoacetogenic bacterium. Arch Microbiol 137:250–255. [CrossRef]
37. Forsberg, CW. 1987. Production of 1,3-propanediol from glycerol by Clostridium acetobutylicum and other Clostridium species. Appl Environ Microbiol 53:639–643. [PubMed]
38. Li F, Hinderberger J, Seedorf H, Zhang J, Buckel W, Thauer RK. 2008. Coupled ferredoxin and crotonyl coenzyme A (CoA) reduction with NADH catalyzed by the butyryl-CoA dehydrogenase/Etf complex from Clostridium kluyveri. J Bacteriol 190:843–850. [PubMed][CrossRef]
39. Seedorf H, Fricke WF, Veith B, Brüggemann H, Liesegang H, Strittmatter A, Miethke M, Buckel W, Hinderberger J, Li F, Hagemeier C, Thauer RK, Gottschalk G. 2008. The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features. Proc Natl Acad Sci USA 105:2128–2133. [PubMed][CrossRef]
40. Buckel W. 1990. Amino acid fermentations: coenzyme B 12-dependent and –independent pathways, p 21–30. In Hauska G, Thauer RK (ed), The Molecular Basis of Bacterial Metabolism. Springer-Verlag, Heidelberg, Germany. [CrossRef]
41. Buckel W. 1991. Ungewöhnliche Chemie bei der Fermentation von Aminosäuren durch anaerobe Bakterien. Bioforum 14:7–19.
42. Buckel W. 2005. Special clostridial enzymes and fermentation pathways, p 177–220. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
43. Dürre P, Andersch W, Andreesen JR. 1981. Isolation and characterization of an adenine-utilizing, anaerobic sporeformer, Clostridium purinolyticum sp. nov. Int J Syst Bacteriol 31:184–194. [CrossRef]
44. Dürre P, Andreesen JR. 1982. Selenium-dependent growth and glycine fermentation by Clostridium purinolyticum. J Gen Microbiol 128:1457–1466. [PubMed]
45. Dürre P, Andreesen JR. 1983. Purine and glycine metabolism by purinolytic clostridia. J Bacteriol 154:192–199. [PubMed]
46. Dürre P, Andreesen JR. 1982. Anaerobic degradation of uric acid via pyrimidine derivatives by selenium-starved cells of Clostridium purinolyticum. Arch Microbiol 131:255–260. [PubMed][CrossRef]
47. Andreesen JR. 2005. Degradation of heterocyclic compounds, p 221–237. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
48. Vogels GD, van der Drift C. 1976. Degradation of purines and pyrimidines by microorganisms. Bacteriol Rev 40:403–468. [PubMed]
49. Minton NP, Clarke DJ. 1989. Clostridia. Plenum Press, New York, NY. [CrossRef]
50. Bahl H, Dürre P. 1993. Clostridia, p 285–323. In Rehm H-J, Reed G, Pühler A, Stadler P (ed), Biotechnology, vol 1. Sahm H (ed), Biological Fundamentals. VCH Verlagsgesellschaft mbH, Weinheim, Germany.
51. Labbé RG. 2005. Sporulation (morphology) of clostridia, p 647–658. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
52. Reysenbach AL, Ravenscroft N, Long S, Jones DT, Woods DR. 1986. Characterization, biosynthesis, and regulation of granulose in Clostridium acetobutylicum. Appl Environ Microbiol 52:185–190. [PubMed]
53. Bergère JL, Rousseau M, Mercier C. 1975. Polyoside intracellulaire impliqué dans la sporulation de Clostridium butyricum. I. Cytologie, production et analyse enzymatique préliminaire. Ann Inst Pasteur Microbiol 126:295–314.
54. Brown RG, Lindberg B, Laishley EJ. 1975. Characterization of two reserve glucans from Clostridium pasteurianum. Can J Microbiol 21:1136–1138. [PubMed][CrossRef]
55. Darvill AG, Hall MA, Fish JP, Morris JG. 1977. The intracellular reserve polysaccharide of Clostridium pasteurianum. Can J Microbiol 23:947–953. [PubMed][CrossRef]
56. Hobson PN, Nasr H. 1951. An amylopectin-type polysaccharide synthesized from sucrose by C. butyricum. J Chem Soc 1951:1855–1857. [CrossRef]
57. Whyte JNC, Strasdine GA. 1972. An intracellular α-D-glucan from Clostridium botulinum, type E. Carbohydr Res 25:435–441. [PubMed][CrossRef]
58. McCoy E, Fred EB, Peterson WH, Hastings EG. 1926. A cultural study of the acetone butyl alcohol organism. J Infect Dis 39:457–483. [CrossRef]
59. Spray RS. 1948. The granulose reaction of certain anaerobes of the "butyric" group. J Bacteriol 55:79–84. [PubMed]
60. Orsburn BC, Melville SB, Popham DL. 2010. EtfA catalyses the formation of dipicolinic acid in Clostridium perfringens. Mol Microbiol 75:178–186. [PubMed][CrossRef]
61. Cabrera-Martinez RM, Mason JM, Setlow B, Waites WM, Setlow P. 1989. Purification and amino acid sequence of two small, acid-soluble proteins from Clostridium bifermentans spores. FEMS Microbiol Lett 52:139–143. [PubMed][CrossRef]
62. Cabrera-Martinez RM, Setlow P. 1991. Cloning and nucleotide sequence of three genes coding for small, acid-soluble proteins of Clostridium perfringens spores. FEMS Microbiol Lett 61:127–131. [PubMed][CrossRef]
63. Huang I-H, Raju D, Paredes-Sabja D, Sarker MR. 2007. Clostridium perfringens: sporulation, spore resistance and germination. Bangladesh J Microbiol 24:1–8.
64. Paredes-Sabja D, Raju D, Torres JA, Sarker MR. 2008. Role of small, acid-soluble spore proteins in the resistance of Clostridium perfringens spores to chemicals. Int J Food Microbiol 122:333–335. [PubMed][CrossRef]
65. Raju D, Waters M, Setlow P, Sarker MR. 2006. Investigating the role of small, acid-soluble spore proteins (SASPs) in the resistance of Clostridium perfringens spores to heat. BMC Microbiol 6:50. doi:10.1186/1471-2180-6-50 [CrossRef]
66. Raju D, Setlow P, Sarker MR. 2007. Antisense-RNA-mediated decreased synthesis of small, acid-soluble spore proteins leads to decreased resistance of Clostridium perfringens spores to moist heat and UV radiation. Appl Environ Microbiol 73:2048–2053. [PubMed][CrossRef]
67. Carpenter CE, Reddy DSA, Cornforth DP. 1987. Inactivation of clostridial ferredoxin and pyruvate-ferredoxin oxidoreductase by sodium nitrite. Appl Environ Microbiol 53:549–552. [PubMed]
68. Reddy D, Lancaster LR, Jr, Cornforth DP. 1983. Nitrite inhibition of Clostridium botulinum: electron spin resonance detection of iron-nitric oxide complexes. Science 221:769–770. [PubMed][CrossRef]
69. Scheeff ED, Axelrod HL, Miller MD, Chiu H-J, Deacon AM, Wilson IA, Manning G. 2010. Genomics, evolution, and crystal structure of a new family of bacterial spore kinases. Proteins 78:1470–1482. [PubMed][CrossRef]
70. Dalla Vecchia E, Veeramani H, Suvorova EI, Wigginton NS, Bargar JR, Bernier-Latmani R. 2010. U(VI) reduction by spores of Clostridium acetobutylicum. Res Microbiol 161:765–771. [PubMed][CrossRef]
71. Permpoonpattana P, Tolls EH, Nadem R, Tan S, Brisson A, Cutting SM. 2011. Surface layers of Clostridium difficile endospores. J Bacteriol 193:6461–6470. [PubMed][CrossRef]
72. Dürre P, Hollergschwandner C. 2004. Initiation of endospore formation in Clostridium acetobutylicum. Anaerobe 10:69–74. [PubMed][CrossRef]
73. Dürre P. 2005. Sporulation in clostridia (genetics), p 659–669. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
74. Stragier P. 2002. A gene odyssey: exploring the genomes of endospore-forming bacteria, p 519–525. In Sonenshein AL, Hoch JA, Losick R (ed), Bacillus subtilis and its closest relatives: From Genes to Cells. American Society for Microbiology, Washington, DC. [CrossRef]
75. Paredes CJ, Alsaker KV, Papoutsakis ET. 2005. A comparative genomic view of clostridial sporulation and physiology. Nat Rev Microbiol 3:969–978. [PubMed][CrossRef]
76. Stephenson K, Lewis RJ. 2005. Molecular insights into the initiation of sporulation in Gram-positive bacteria: new technologies for an old phenomenon. FEMS Microbiol Lett 29:281–301. [PubMed][CrossRef]
77. Brown DP, Ganova-Raeva L, Green BD, Wilkinson SR, Young M, Youngman P. 1994. Characterization of spo0A homologs in diverse Bacillus and Clostridium species reveals regions of high conservation within the effector domain. Mol Microbiol 14:411–426. [PubMed][CrossRef]
78. Gutierrez Escobar AJ, Montoya Castaño D. 2009. Evolutionary analysis for the functional divergence of the Spo0A protein: the key sporulation control element. In Silico Biol 9:149–162. [PubMed]
79. Hilbert DW, Piggot PJ. 2004. Compartmentalization of gene expression during Bacillus subtilis spore formation. Microbiol Mol Biol Rev 68:234–262. [PubMed][CrossRef]
80. Nölling J, Breton G, Omelchenko MV, Makarova KS, Zeng Q, Gibson R, Lee HM, Dubois J, Qiu D, Hitti J, GTC Sequencing Center Production, Finishing, and Bioinformatics Teams, Wolf YI, Tatusov RL, Sabathe F, Doucette-Stamm L, Soucaille P, Daly MJ, Bennett GN, Koonin EV, Smith DR. 2001. Genome sequence and comparative analysis of the solvent-producing bacterium Clostridium acetobutylicum. J Bacteriol 183:4823–4838. [PubMed][CrossRef]
81. Sauer U, Treuner A, Buchholz M, Santangelo JD, Dürre P. 1994. Sporulation and primary sigma factor homologous genes in Clostridium acetobutylicum. J Bacteriol 176:6572–6582. [PubMed]
82. Santangelo JD, Kuhn A, Treuner-Lange A, Dürre P. 1998. Sporulation and time course expression of sigma-factor homologous genes in Clostridium acetobutylicum. FEMS Microbiol Lett 161:157–164. [PubMed][CrossRef]
83. Jones SW, Tracy BP, Gaida SM, Papoutsakis ET. 2011. Inactivation of σ F in Clostridium acetobutylicum ATCC 824 blocks sporulation prior to asymmetric division and abolishes σ E and σ G protein expression but does not block solvent formation. J Bacteriol 193:242–2440. [PubMed][CrossRef]
84. Li J, McClane BA. 2010. Evaluating the involvement of alternative sigma factors SigF and SigG in Clostridium perfringens sporulation and enterotoxin synthesis. Infect Immun 78:4286–4293. [PubMed][CrossRef]
85. Scotcher MC, Bennett GN. 2005. SpoIIE regulates sporulation but does not directly affect solventogenesis in Clostridium acetobutylicum ATCC 824. J Bacteriol 187:1930–1936. [PubMed][CrossRef]
86. Bi C, Jones SW, Hess DR, Tracy BP, Papoutsakis ET. 2011. SpoIIE is necessary for asymmetric division, sporulation, and expression of σ F, σ E, and σ G but does not control solvent production in Clostridium acetobutylicum ATCC 824. J Bacteriol 193:5130–5137. [PubMed][CrossRef]
87. Tracy BP, Jones AW, Papoutsakis ET. 2011. Inactivation of σ E and σ G in Clostridium acetobutylicum illuminates their roles in clostridial-cell-form biogenesis, granulose synthesis, solventogenesis, and spore morphogenesis. J Bacteriol 193:1414–1426. [PubMed][CrossRef]
88. Harry KH, Zhou R, Kroos L, Melville SB. 2009. Sporulation and enterotoxin (CPE) synthesis are controlled by the sporulation-specific sigma factors SigE and SigK in Clostridium perfringens. J Bacteriol 191:2728–2742. [PubMed][CrossRef]
89. Jones SW, Paredes CJ, Tracy B, Cheng N, Sillers R, Senger RS, Papoutsakis ET. 2008. The transcriptional program underlying the physiology of clostridial sporulation. Genome Biol 9:R114. doi:10.1186/gb-2008-9-7-r114. [PubMed][CrossRef]
90. Haraldsen JD, Sonenshein AL. 2003. Efficient sporulation in Clostridium difficile requires disruption of the σ K gene. Mol Microbiol 48:811–821. [PubMed][CrossRef]
91. Kirk DG, Dahlsten E, Zhang Z, Korkeala H, Lindström M. 2012. Clostridium botulinum ATCC 3502 sigma factor K is involved with early stage sporulation. Appl Environ Microbiol 78:4590–4596. [PubMed][CrossRef]
92. Saujet L, Monot M, Dupuy B, Soutourina O, Martin-Verstraete I. 2011. The key sigma factor of transition phase, SigH, controls sporulation, metabolism, and virulence factor expression in Clostridium difficile. J Bacteriol 193:3186–3196. [PubMed][CrossRef]
93. Burns DA, Minton NP. 2011. Sporulation studies in Clostridium difficile. J Microbiol Methods 87:133–138. [PubMed][CrossRef]
94. Burns DA, Heeg D, Cartman ST, Minton NP. 2011. Reconsidering the sporulation characteristics of hypervirulent Clostridium difficile BI/NAP1/027. PLoS One. 6(9) :e24894. doi:10.1371/journal.pone.0024894. [PubMed][CrossRef]
95. Doß S, Gröger C, Knauber T, Whitworth DE, Treuner-Lange A. 2005. Comparative genomic analysis of signal transduction proteins in clostridia, p 561–582. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
96. Steiner E, Dago AE, Young DI, Heap JT, Minton NP, Hoch JA, Young M. 2011. Multiple orphan histidine kinases interact directly with Spo0A to control initiation of endospore formation in Clostridium acetobutylicum. Mol Microbiol 80:641–654. [PubMed][CrossRef]
97. Dürre P. 2011. Ancestral sporulation initiation. Mol Microbiol 80:584–587. [PubMed][CrossRef]
98. Harris LM, Welker NE, Papoutsakis ET. 2002. Northern, morphological, and fermentation analysis of spo0A inactivation and overexpression in Clostridium acetobutylicum ATCC 824. J Bacteriol 184:3586–3597. [PubMed][CrossRef]
99. Köpke M, Dürre P. 2010. Biochemical production of biobutanol, p 221–257. In Luque R, Campelo J, Clark J (ed), Handbook of Biofuels Production. Woodhead Publishing Ltd, Abington, Cambridge, UK.
100. Ravagnani A, Jennert KCB, Steiner E, Grünberg R, Jefferies JR, Wilkinson SR, Young DI, Tidswell EC, Brown DP, Youngman P, Morris JG, Young M. 2000. Spo0A directly controls the switch from acid to solvent production in solvent-forming clostridia. Mol Microbiol 37:1172–1185. [PubMed][CrossRef]
101. Paredes-Sabja D, Sarker N, Sarker MR. 2011. Clostridium perfringen stpeL is expressed during sporulation. Microbial Pathogen 51: 384–388. [PubMed][CrossRef]
102. Popoff M R, Stiles BG. 2005. Clostridial toxins vs. other bacterial toxins, p 323–383. In Dürre P (ed), Handbook on Clostridia. CRC Press, Taylor & Francis Group, Boca Raton, FL.
103. Carter GP, Douce GR, Govind R, Howarth PM, Mackin KE, Spencer J, Buckley AM, Antunes A, Kotsanas D, Jenkin GA, Dupuy B, Rood JI, Lyras D. 2011. The anti-sigma factor TcdC modulates hypervirulence in an epidemic BI/NAP1/027 clinical isolate of Clostridium difficile. PLoS Pathog 7(10) :e1002317. doi:10.1371/journal.ppat.1002317. [PubMed][CrossRef]
104. Underwood S, Guan S, Vijayasubhash V, Baines SD, Graham L, Lewis RJ, Wilcox MH, Stephenson K. 2009. Characterization of the sporulation initiation pathway of Clostridium difficile and its role in toxin production. J Bacteriol 191:7296–7305. [PubMed][CrossRef]
105. Deakin LJ, Clare S, Fagan RP, Dawson LF, Pickard DJ, West MR, Wren BW, Fairweather NF, Dougan G, Lawley TD. 2012. Clostridium difficile spo0A gene is a persistence and transmission factor. Infect Immun 80:2704–2711. [PubMed][CrossRef]
106. Lyras D, O’Connor JR, Howarth PM, Sambol SP, Carter GP, Phumoonna T, Poon R, Adams V, Vedantam G, Johnson S, Gerding DN, Rood JI. 2009. Toxin B is essential for virulence of Clostridium difficile.Nature 458:1176–1179. [PubMed][CrossRef]
107. Kuehne SA, Cartman ST, Heap JT, Kelly ML, Cockayne A, Minton NP. 2010. The role of toxin A and toxin B in Clostridium difficile infection. Nature 467:711–713. [PubMed][CrossRef]
108. Nakamura S, Serikawa T, Yamakawa K, Nishida S, Kozaki S, Sakaguchi G. 1978. Sporulation and C2 toxin production by Clostridium botulinum type C strains producing no C1 toxin. Microbiol Immunol 22:591–596. [PubMed][CrossRef]
109. Cooksley CM, Davis IJ, Winzer K, Chan WC, Peck MW, Minton NP. 2010. Regulation of neurotoxin production and sporulation by a putative agrBD signaling system in proteolytic Clostridium botulinum. Appl Environ Microbiol 76:4448–4460. [CrossRef]
110. Li J, Chen J, Vidal JE, McClane BA. 2011. The Agr-like quorum-sensing system regulates sporulation and production of enterotoxin and beta2 toxin by Clostridium perfringens type A non-food-borne human gastrointestinal disease strain F5603. Infect Immun 79:2451–2459. [PubMed][CrossRef]
111. Steiner E, Scott J, Minton NP, Winzer K. 2012. An agr quorum sensing system that regulates granulose formation and sporulation in Clostridium acetobutylicum. Appl Environ Microbiol 78:1113–1122. [PubMed][CrossRef]
112. Marchais A, Duperrier S, Durand S, Gautheret D, Stragier P. 2011. CsfG, a sporulation-specific, small non-coding RNA highly conserved in endospore formers. RNA Biol 8:358–364. [PubMed][CrossRef]
113. Brousolle V, Alberto F, Shearman CA, Mason DR, Botella L, Nguyen-The C, Peck MW, Carlin F. 2002. Molecular and physiological characterization of spore germination in Clostridium botulinum and C. sporogenes. Anaerobe 8:89–100. [CrossRef]
114. Paredes-Sabja D, Torres JA, Setlow P, Sarker MR. 2008. Clostridium perfringens spore germination: characterization of germinants and their receptors. J Bacteriol 190:1190–1201. [PubMed][CrossRef]
115. Paredes-Sabja D, Udompijitkul P, Sarker MR. 2009. Inorganic phosphate and sodium ions are cogerminants for spores of Clostridium perfringens type A food poisoning-related isolates. Appl Environ Microbiol 75:6299–6305. [PubMed][CrossRef]
116. Heeg D, Burns DA, Cartman ST, Minton NP. 2012. Spores of Clostridium difficile clinical isolates display a diverse germination response to bile salts. PLoS One 7(2) :e32381. doi:10.1371/journal.pone.0032381. [PubMed][CrossRef]
117. Paredes-Sabja D, Bond C, Carman RJ, Setlow P, Sarker MR. 2008. Germination of spores of Clostridium difficile strains, including isolates from a hospital outbreak of Clostridium difficile-associated disease (CDAD). Microbiology 154:2241–2250. [PubMed][CrossRef]
118. Sorg JA, Sonenshein AL. 2008. Bile salts and glycine as cogerminants for Clostridium difficile spores. J Bacteriol 190:2505–2512. [PubMed][CrossRef]
119. Paredes-Sabja D, Setlow P, Sarker MR. 2009. Role of GerKB in germination and outgrowth of Clostridium perfringens spores. Appl Environ Microbiol 75:3813–3817. [PubMed][CrossRef]
120. Paredes-Sabja D, Setlow P, Sarker MR. 2009. GerO, a putative Na +/H +-K + antiporter, is essential for normal germination of spores of the pathogenic bacterium Clostridium perfringens. J Bacteriol 191:3822–3831. [PubMed][CrossRef]
121. Makino S, Moriyama R. 2002. Hydrolysis of cortex peptidoglycan during bacterial spore germination. Med Sci Monit 8:RA119–127. [PubMed]
122. Miyata S, Kozuka S, Yasuda Y, Chen Y, Moriyama R, Tochikubo K, Makino S. 1997. Localization of germination-specific spore-lytic enzymes in Clostridium perfringens S40 spores detected by immunoelectron microscopy. FEMS Microbiol Lett 152:243–247. [PubMed][CrossRef]
123. Kumazawa T, Masayama A, Fukuoka S, Makino S, Yoshimura T, Moriyama R. 2007. Mode of action of a germination-specific cortex-lytic enzyme, SleC, of Clostridium perfringens S40. Biosci Biotechnol Biochem 71:884–892. [PubMed][CrossRef]
124. Paredes-Sabja D, Setlow P, Sarker MR. 2009. SleC is essential for cortex peptidoglycan hydrolysis during germination of spores of the pathogenic bacterium Clostridium perfringens. J Bacteriol 191: 2711–2720. [PubMed][CrossRef]
125. Burns DA, Heap JT, Minton NP. 2010. SleC is essential for germination of Clostridium difficile spores in nutrient-rich medium supplemented with the bile salt taurocholate. J Bacteriol 192: 657–664. [PubMed][CrossRef]
126. Xiao Y, Francke C, Abee T, Wells-Bennik MHJ. 2011. Clostridial spore germination versus bacilli: genome mining and current insights. Food Microbiol 28:266–274. [PubMed][CrossRef]
127. Bader J, Albin A, Stahl U. 2012. Spore-forming bacteria and their utilisation as probiotics. Benef Microbes 3:67–75. [PubMed][CrossRef]
128. Okamoto T, Sasaki M, Tsujikawa T, Fujiyama Y, Bamba T, Kusunoki M. 2000. Preventive efficacy of butyrate enemas and oral administration of Clostridium butyricum M588 in dextran sodium sulfate-induced colitis in rats. J Gastroenterol 35:341–346. [PubMed][CrossRef]
129. Takahashi M, Taguchi H, Yamaguchi H, Osaki T, Komatsu A, Kamiya S. 2004. The effect of probiotic treatment with Clostridium butyricum on enterohemorrhagic Escherichia coli O157:H7 infection in mice. FEMS Immunol Med Microbiol 41:219–226. [PubMed][CrossRef]
130. Mengesha A, Wie JZ, Zhou S-F, Wie MQ. 2010. Clostridial spores to treat solid tumours – potential for a new therapeutic model. Curr Gene Ther 10:15–26. [PubMed]
131. Minton NP, Mauchline ML, Lemmon MJ, Brehm JK, Fox M, Michael NP, Giaccia A, Brown JM. 1995. Chemotherapeutic tumour targeting using clostridial spores. FEMS Microbiol Rev 17:357–364. [PubMed][CrossRef]
132. Minton NP. 2003. Clostridia in cancer therapy. Nat Rev Microbiol 1:237–242. [PubMed][CrossRef]
133. Brown JM, Liu S-C. 2004. Use of anaerobic bacteria for cancer therapy, p 211–219. In Nakano MM, Zuber P (ed), Strict and Facultative Anaerobes. Medical and Environmental Aspects. Horizon Bioscience, Wymondham, UK.
134. Lambin P, Theys J, Landuyt W, Rijken P, van der Kogel A, van der Schueren E, Hodgkiss R, Fowler J, Nuyts S, de Bruijn E, van Mellaert L, Anné J. 1998. Colonization of Clostridium in the body is restricted to hypoxic and necrotic areas of tumours. Anaerobe 4:183–188. [PubMed][CrossRef]
135. Barbé S, van Mellaert L, Theys J, Geukens N, Lammertyn E, Lambin P, Anné J. 2005. Secretory production of biologically active rat interleukin-2 by Clostridium acetobutylicum DSM792 as a tool for anti-tumor treatment. FEMS Microbiol Lett 246:67–73. [PubMed][CrossRef]
136. Theys J, Nuyts S, Landuyt W, van Mellaert L, Dillen C, Böhringer M, Dürre P, Lambin P, Anné J. 1999. Stable Escherichia coli-Clostridium acetobutylicum shuttle vector for secretion of murine tumor necrosis factor alpha. Appl Environ Microbiol 65:4295–4300. [PubMed]
137. Dang LH, Bettegowda C, Huso DL, Kinzler KW, Vogelstein B. 2001. Combination bacteriolytic therapy for the treatment of experimental tumors. Proc Natl Acad Sci USA 98:15155–15160. [PubMed][CrossRef]
Loading

Article metrics loading...

/content/journal/microbiolspec/10.1128/microbiolspec.TBS-0010-2012
2014-08-08
2021-01-26

Abstract:

Clostridia are Gram-positive, anaerobic, endospore-forming bacteria, incapable of dissimilatory sulfate reduction. Comprising approximately 180 species, the genus is one of the largest bacterial genera. Physiology is mostly devoted to acid production. Numerous pathways are known, such as the homoacetate fermentation by acetogens, the propionate fermentation by , and the butyrate/butanol fermentation by , a well-known solvent producer. Clostridia degrade sugars, alcohols, amino acids, purines, pyrimidines, and polymers such as starch and cellulose. Energy conservation can be performed by substrate-level phosphorylation as well as by the generation of ion gradients. Endospore formation resembles the mechanism elucidated in . Morphology, contents, and properties of spores are very similar to bacilli endospores. Sporulating clostridia usually form swollen mother cells and accumulate the storage substance granulose. However, clostridial sporulation differs by not employing the so-called phosphorelay. Initiation starts by direct phosphorylation of the master regulator Spo0A. The cascade of sporulation-specific sigma factors is again identical to what is known from . The onset of sporulation is coupled in some species to either solvent (acetone, butanol) or toxin (e.g., enterotoxin) formation. The germination of spores is often induced by various amino acids, often in combination with phosphate and sodium ions. In medical applications, spores are used as a prophylaxis and as treatment against diarrhea. Recombinant spores are currently under investigation and testing as antitumor agents, because they germinate only in hypoxic tissues (i.e., tumor tissue), allowing precise targeting and direct killing of tumor cells.

Highlighted Text: Show | Hide
Loading full text...

Full text loading...

/deliver/fulltext/microbiolspec/2/4/TBS-0010-2012.html?itemId=/content/journal/microbiolspec/10.1128/microbiolspec.TBS-0010-2012&mimeType=html&fmt=ahah

Figures

Physiology and Sporulation in
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.TBS-0010-2012-1,webId=/content/author/microbiolspec/10.1128/microbiolspec.TBS-0010-2012-1,properties={foaf_givenname=Peter, foaf_name=Peter Dürre, foaf_surname=Dürre, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.TBS-0010-2012-aff1]]}]]
Citation: Dürre P. 2014. Physiology and sporulation in . microbiolspec 2(4): doi:10.1128/microbiolspec.TBS-0010-2012
/content/microbiolspec/10.1128/microbiolspec.TBS-0010-2012.fig1
FIGURE 1
Vegetative growth and sporulation/germination cycle in clostridia. During normal growth, cells (shown is ) divide and multiply (left). During this period, acids, carbon dioxide, and hydrogen are formed. Upon signals not yet determined, cells start to differentiate into "clostridial forms" with granulose as a storage material (solventogenic species produce at this time acetone, butanol, or isopropanol), then form endospores, which finally will germinate into vegetative cells again.
microbiolspec/2/4/TBS-0010-2012-fig1_thmb.gif
microbiolspec/2/4/TBS-0010-2012-fig1.gif
Image of FIGURE 1

Click to view

FIGURE 1

Vegetative growth and sporulation/germination cycle in clostridia. During normal growth, cells (shown is ) divide and multiply (left). During this period, acids, carbon dioxide, and hydrogen are formed. Upon signals not yet determined, cells start to differentiate into "clostridial forms" with granulose as a storage material (solventogenic species produce at this time acetone, butanol, or isopropanol), then form endospores, which finally will germinate into vegetative cells again.

Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.TBS-0010-2012
Permissions and Reprints Request Permissions
Download as Powerpoint
/content/microbiolspec/10.1128/microbiolspec.TBS-0010-2012.fig2
FIGURE 2
Signal transduction in and leading to the onset of sporulation. (A) In , three sensor kinases autophosphorylate at a histidine residue and transfer the phosphoryl group to an aspartate residue of the response regulator Spo0A. Cac0323 acts alone, while Cac0903 and Cac3319 act in concert. Cac0437 is a protein masquerading as a kinase, but acting as a phosphatase. (B) In , five different kinases channel the phosphoryl group to Spo0A via a phosphorelay consisting of Spo0F and Spo0B.
microbiolspec/2/4/TBS-0010-2012-fig2_thmb.gif
microbiolspec/2/4/TBS-0010-2012-fig2.gif
Image of FIGURE 2

Click to view

FIGURE 2

Signal transduction in and leading to the onset of sporulation. (A) In , three sensor kinases autophosphorylate at a histidine residue and transfer the phosphoryl group to an aspartate residue of the response regulator Spo0A. Cac0323 acts alone, while Cac0903 and Cac3319 act in concert. Cac0437 is a protein masquerading as a kinase, but acting as a phosphatase. (B) In , five different kinases channel the phosphoryl group to Spo0A via a phosphorelay consisting of Spo0F and Spo0B.

Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.TBS-0010-2012
Permissions and Reprints Request Permissions
Download as Powerpoint

Tables

Physiology and Sporulation in
[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/author/microbiolspec/10.1128/microbiolspec.TBS-0010-2012-1,webId=/content/author/microbiolspec/10.1128/microbiolspec.TBS-0010-2012-1,properties={foaf_givenname=Peter, foaf_name=Peter Dürre, foaf_surname=Dürre, pub_isAffiliatedWith=[com.pub2web.rdf.cci.facet.ContentItem[id=http://asm.metastore.ingenta.com/content/affiliation/microbiolspec/10.1128/microbiolspec.TBS-0010-2012-aff1]]}]]
Citation: Dürre P. 2014. Physiology and sporulation in . microbiolspec 2(4): doi:10.1128/microbiolspec.TBS-0010-2012
/content/microbiolspec/10.1128/microbiolspec.TBS-0010-2012.T1
TABLE 1
Major metabolic features of
Generic image for table

Click to view

TABLE 1

Major metabolic features of

Source: microbiolspec August 2014 vol. 2 no. 4 doi:10.1128/microbiolspec.TBS-0010-2012

Supplemental Material

No supplementary material available for this content.

Back to top
This is a required field
Please enter a valid email address
Please check the format of the address you have entered.
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error