MAJOR VIRULENCE FACTORS AND PATHOGENICITY ISLANDS IN PATHOGENIC CLOSTRIDIUM SPECIES
Asian Journal of Microbiology and Biotechnology,
Page 1-16
DOI:
10.56557/ajmab/2022/v7i17564
Abstract
Clostridia are obligately anaerobic, spore-forming bacilli that, at least in the early stages of growth, stain gramme positive. Clostridia produce greater toxins than any other bacterium genus, and pathogenic clostridia are typically diagnosed by their unique toxins. Clostridium spp. has been found to have more than 20 toxins and other extracellular proteins that contribute to virulence, such as spread factors and proteolytic enzymes. Botulinum and tetanus toxins are the most potent poisons ever discovered. Clostridium botulinum neurotoxins are the most potent acute toxins identified, and they are the cause of the neuroparalytic illness botulism. Such toxins work by inhibiting presynaptic nerve terminal neurotransmission in the peripheral and central nervous systems. Other clostridia toxins have different modes of action, such as tissue destruction, hemolysis, diarrhoea, or generating an overactive immunological response in the recipient. On non-integrative lysogenic bacteriophages or plasmids, the genes coding for numerous clostridial toxins are found. Protein secretory processes in Clostridia are poorly understood. It has remained a mystery as to how the tetanus toxin, which lacks a normal N-terminal signal peptide, is exported until today. Typical PAI are DNA segments that are found in pathogenic bacteria's genomes but not in nonpathogenic strains of the same or similar species.
Keywords:
- Clostridia
- genes
- neurotoxin
- secretory systems
- virulence
How to Cite
YIMER, L. (2022). MAJOR VIRULENCE FACTORS AND PATHOGENICITY ISLANDS IN PATHOGENIC CLOSTRIDIUM SPECIES. Asian Journal of Microbiology and Biotechnology, 7(1), 1-16. https://doi.org/10.56557/ajmab/2022/v7i17564
References
Wilson JW, Schurr MJ, LeBlanc CL, Ramamurthy R, Buchanan KL, Nickerson CA. Mechanisms of bacterial pathogenicity. Postgrad. Med. J. 2002;78:216–224.
Casadevall A, Pirofski L. Host–pathogen interactions: redefining the basic concepts of virulence and pathogenicity. Infect. Immun. 1999;67:3703–3713.
Casadevall A, Pirofski LA. Virulence factors and their mechanisms of action: The view from a damage-response framework. J. Water Health. 2009;7:2–18. Available:https://doi.org/10.2166/wh.2009.036
Sparling PF. Bacterial virulence and pathogenesis: an overview. Rev. Infect. Dis. 1983;5:S637–S646.
Popoff MR. Toxins of histotoxic clostridia: Clostridium chauvoei, Clostridium septicum, Clostridium novyi, and Clostridium sordellii. Clostridial Dis. Anim. 2016;23.
Prescott JF, MacInnes JI, Wu AKK, Uzal FA, Songer JG, Popoff MR. Taxonomic relationships among the clostridia. Clostridial Dis. Anim. 2016;1–5.
Collins MD, et al. The phylogeny of the genus Clostridium: proposal of five new genera and eleven new species combinations. Int J Syst Bacteriol. 1994;44(4):812–826.
Rood JI, McClane BA, Songer JG, Titball RW. The clostridia: molecular biology and pathogenesis. Academic Press; 1997.
Hatheway CL. Toxigenic clostridia. Clin. Microbiol. Rev. 1990;3:66–98.
Rood JI. Virulence genes of Clostridium perfringens. Annu. Rev. Microbiol. 1998;52: 333– 360.
Myers GSA, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, et al. Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006;16:1031– 1040. Available:https://doi.org/10.1101/gr.5238106
Smith LDS. Virulence factors of Clostridium perfringens. Rev. Infect. Dis. 1979;1:254–262.
Johnson EA. Extrachromosomal virulence determinants in the Clostridia. In The Clostridia. Molecular biology and pathogenesis (eds. J.I. Rood, et al.). Academic Press, London. 1997;35–48.
Rood JI, Cole ST. Molecular genetics and pathogenesis of Clostridium perfringens. Microbiol. Rev. 1991;55:621–648.
Li J, Sayeed S, Robertson S, Chen J, Mcclane BA. Sialidases Affect the Host Cell Adherence and Epsilon Toxin-Induced Cytotoxicity of Clostridium perfringens Type D Strain CN3718 7; 2011. Available:https://doi.org/10.1371/journal.ppat.1002429
Walters DM, Stirewalt VL, Melville SB. Cloning, sequence, and transcriptional regulation of the operon encoding a putative N-acetylmannosamine-6-phosphate epimerase (nanE) and sialic acid lyase (nanA) in Clostridium perfringens. J. Bacteriol. 1999;181:4526–4532.
Adams JJ, Gregg K, Bayer EA, Boraston AB, Smith SP. Structural basis of Clostridium perfringens toxin complex formation; 2008.
Smyth CJ, Arbuthnott JP. Properties of Clostridium Perfringens (Welch II) Type-A α- Toxin (Phospholipase c) Purified By Electrofocusing. J. Med. Microbiol. 1974;7: 41–66.
Pivnick H, Hauschild AHW, Gorenstein B, Ha- Beeb AFSA. Effect of controlled pH on toxino- genesis by Clostridium periringens type D. Can. J. Microbiol. 1965;11:45-55.
Habeeb AFSA. Studies on e-prototoxin of Clos-tridium periringens type D. Physicochemical and chemical properties of e-prototoxin. Biochim. Bio- phys. Acta. 1975;412:62-69.
Porter CJ, Bantwal R, Bannam TL, Rosado CJ, Pearce MC, Adams V, Lyras D, Whisstock JC, Rood JI. The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram‐ negative bacteria. Mol. Microbiol. 2012;83:275–288. Available:https://doi.org/10.1111/j.1365- 2958.2011.07930.x
Rupnik M, Wilcox MH, Gerding DN. Clostridium difficile infection: new developments in epidemiology and pathogenesis. Nat. Rev. Microbiol. 2009;7: 526.
Poxton IR, Mccoubrey J, Blair G. The pathogenicity of Clostridium difficile; 2001.
Vedantam G, Clark A, Chu M, McQuade R, Mallozzi M, Viswanathan VK. Clostridium difficile infection: toxins and non-toxin virulence factors, and their contributions to disease establishment and host response. Gut Microbes. 2012;3:121–134.
Carter GP, Rood JI, Lyras D. The role of toxin A and toxin B in the virulence of Clostridium difficile. Trends Microbiol. 2012;20:21–29.
Shen A. Clostridium difficile toxins: mediators of inflammation. J. Innate Immun. 2012;4: 149–158.
Thelestam M, Chaves-Olarte E. Cytotoxic effects of the Clostridium difficile toxins. Curr Topics Microbiol Immunol. 2000;250:85–96.
Dillon ST, Rubin EJ, Yakubovich M et al. Involvement of Ras-related proteins in the mechanism of action of Clostridium difficile toxin A and toxin B. Infect Immun. 1995;63: 1421–6.
Zhang W, Cheng Y, Du P, Zhang Y, Jia H, Li X, Wang J, Han N, Qiang Y, Chen C. Genomic study of the Type IVC secretion system in Clostridium difficile: understanding C. difficile evolution via horizontal gene transfer. Genome. 2016;60:8–16.
Oguma K, Fujinaga Y, Inoue K. Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 1995;39:161–168.
Franciosa G, Ferreira JL, Hatheway CL. Detection of type A, B, and E botulism neurotoxin genes in Clostridium botulinum and other Clostridium species by PCR: evidence of unexpressed type B toxin genes in type A toxigenic organisms. J. Clin. Microbiol. 1994; 32:1911–1917.
Cathey, John. "Re: Tetanus." Tetanus. Madsci Network, 27 Feb. 1998. Web. 23 April. 2018.
Montecucco C, Schiavo G. Mechanism of action of tetanus and botulinum neurotoxins. Mol. Microbiol. 1994;13:1–8.
Helting TB, Parschat S, Engelhardt H. Structure of tetanus toxin. Demonstration and separation of a specific enzyme converting intracellular tetanus toxin to the extracellular form. J. Biol. Chem. 1979;254:10728–10733.
Schiavo GG, Benfenati F, Poulain B, Rossetto O, de Laureto PP, DasGupta BR, Montecucco C. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 1992;359: 832.
Mukherjee K, Karlsson S, Burman LG, Åkerlund T. Proteins released during high toxin production in Clostridium difficile. Microbiology. 2002;148:2245–2253.
Driessen AJM, Fekkes P, van der Wolk JPW. The sec system. Curr. Opin. Microbiol. 1998; 1:216–222.
Nouwen N, Driessen AJM. SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 2002;44:1397–1405.
Brüggemann H, Bäumer S, Fricke WF, Wiezer A, Liesegang H, Decker I, Herzberg C, Martinez-Arias R, Merkl R, Henne A. The genome sequence of Clostridium tetani, the causative agent of tetanus disease. Proc. Natl. Acad. Sci. 2003;100:1316–1321.
Willis AT. Clostridia of wound infection. Clostridia wound Infect; 1969.
Al-Khatib G. Beitrage zur Clostridien differenzierung. Zur Differenzierung von Cl. septicum and Cl. chauvoei. Arch Exp Vet. 1969;23:963–970.
Princewill TJ, Oakley CL. Deoxyribonucleases and hyaluronidases of Clostridium septicum and Clostridium chauvoei. III. Relationship between the two organisms. Med. Lab. Sci. 1976;33:10–118.
Moussa RS. Complexity of toxins from Clostridium septicum and Clostridium chauvoei. J. Bacteriol. 1958;76:538.
Gadalla MSA, Collee JG. The relationship of the neuraminidase of Clostridium septicum to the haemagglutinin and other soluble products of the organism. J. Pathol. 1968;96: 169–184.
Hacker J, Bender L, Ott M, Wingender J, Lund B, Marre R, Goebel W. Deletions of chromosomal regions coding for fimbriae and hemolysins occur in vitro and in vivo in various extraintestinal Escherichiacoli isolates. Microb. Pathog. 1990;8:213–225.
Herbert Schmidt and Michael Hensel. Pathogenicity Islands in Bacterial Pathogenesis. Clinical Microbiology Reviews. 2004;17(1):14–56.
Smith TJ, Hill KK, Foley BT, Detter JC, Munk AC, Bruce DC, et al. Analysis of the Neurotoxin Complex Genes in Clostridium botulinum A1-A4 and B1 Strains : BoNT / A3 , / Ba4 and / B1 Clusters Are Located within Plasmids; 2007. Available:https://doi.org/10.1371/journal.pone.0001271
Casadevall A, Pirofski L. Host–pathogen interactions: redefining the basic concepts of virulence and pathogenicity. Infect. Immun. 1999;67:3703–3713.
Casadevall A, Pirofski LA. Virulence factors and their mechanisms of action: The view from a damage-response framework. J. Water Health. 2009;7:2–18. Available:https://doi.org/10.2166/wh.2009.036
Sparling PF. Bacterial virulence and pathogenesis: an overview. Rev. Infect. Dis. 1983;5:S637–S646.
Popoff MR. Toxins of histotoxic clostridia: Clostridium chauvoei, Clostridium septicum, Clostridium novyi, and Clostridium sordellii. Clostridial Dis. Anim. 2016;23.
Prescott JF, MacInnes JI, Wu AKK, Uzal FA, Songer JG, Popoff MR. Taxonomic relationships among the clostridia. Clostridial Dis. Anim. 2016;1–5.
Collins MD, et al. The phylogeny of the genus Clostridium: proposal of five new genera and eleven new species combinations. Int J Syst Bacteriol. 1994;44(4):812–826.
Rood JI, McClane BA, Songer JG, Titball RW. The clostridia: molecular biology and pathogenesis. Academic Press; 1997.
Hatheway CL. Toxigenic clostridia. Clin. Microbiol. Rev. 1990;3:66–98.
Rood JI. Virulence genes of Clostridium perfringens. Annu. Rev. Microbiol. 1998;52: 333– 360.
Myers GSA, Rasko DA, Cheung JK, Ravel J, Seshadri R, DeBoy RT, Ren Q, Varga J, et al. Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens. Genome Res. 2006;16:1031– 1040. Available:https://doi.org/10.1101/gr.5238106
Smith LDS. Virulence factors of Clostridium perfringens. Rev. Infect. Dis. 1979;1:254–262.
Johnson EA. Extrachromosomal virulence determinants in the Clostridia. In The Clostridia. Molecular biology and pathogenesis (eds. J.I. Rood, et al.). Academic Press, London. 1997;35–48.
Rood JI, Cole ST. Molecular genetics and pathogenesis of Clostridium perfringens. Microbiol. Rev. 1991;55:621–648.
Li J, Sayeed S, Robertson S, Chen J, Mcclane BA. Sialidases Affect the Host Cell Adherence and Epsilon Toxin-Induced Cytotoxicity of Clostridium perfringens Type D Strain CN3718 7; 2011. Available:https://doi.org/10.1371/journal.ppat.1002429
Walters DM, Stirewalt VL, Melville SB. Cloning, sequence, and transcriptional regulation of the operon encoding a putative N-acetylmannosamine-6-phosphate epimerase (nanE) and sialic acid lyase (nanA) in Clostridium perfringens. J. Bacteriol. 1999;181:4526–4532.
Adams JJ, Gregg K, Bayer EA, Boraston AB, Smith SP. Structural basis of Clostridium perfringens toxin complex formation; 2008.
Smyth CJ, Arbuthnott JP. Properties of Clostridium Perfringens (Welch II) Type-A α- Toxin (Phospholipase c) Purified By Electrofocusing. J. Med. Microbiol. 1974;7: 41–66.
Pivnick H, Hauschild AHW, Gorenstein B, Ha- Beeb AFSA. Effect of controlled pH on toxino- genesis by Clostridium periringens type D. Can. J. Microbiol. 1965;11:45-55.
Habeeb AFSA. Studies on e-prototoxin of Clos-tridium periringens type D. Physicochemical and chemical properties of e-prototoxin. Biochim. Bio- phys. Acta. 1975;412:62-69.
Porter CJ, Bantwal R, Bannam TL, Rosado CJ, Pearce MC, Adams V, Lyras D, Whisstock JC, Rood JI. The conjugation protein TcpC from Clostridium perfringens is structurally related to the type IV secretion system protein VirB8 from Gram‐ negative bacteria. Mol. Microbiol. 2012;83:275–288. Available:https://doi.org/10.1111/j.1365- 2958.2011.07930.x
Rupnik M, Wilcox MH, Gerding DN. Clostridium difficile infection: new developments in epidemiology and pathogenesis. Nat. Rev. Microbiol. 2009;7: 526.
Poxton IR, Mccoubrey J, Blair G. The pathogenicity of Clostridium difficile; 2001.
Vedantam G, Clark A, Chu M, McQuade R, Mallozzi M, Viswanathan VK. Clostridium difficile infection: toxins and non-toxin virulence factors, and their contributions to disease establishment and host response. Gut Microbes. 2012;3:121–134.
Carter GP, Rood JI, Lyras D. The role of toxin A and toxin B in the virulence of Clostridium difficile. Trends Microbiol. 2012;20:21–29.
Shen A. Clostridium difficile toxins: mediators of inflammation. J. Innate Immun. 2012;4: 149–158.
Thelestam M, Chaves-Olarte E. Cytotoxic effects of the Clostridium difficile toxins. Curr Topics Microbiol Immunol. 2000;250:85–96.
Dillon ST, Rubin EJ, Yakubovich M et al. Involvement of Ras-related proteins in the mechanism of action of Clostridium difficile toxin A and toxin B. Infect Immun. 1995;63: 1421–6.
Zhang W, Cheng Y, Du P, Zhang Y, Jia H, Li X, Wang J, Han N, Qiang Y, Chen C. Genomic study of the Type IVC secretion system in Clostridium difficile: understanding C. difficile evolution via horizontal gene transfer. Genome. 2016;60:8–16.
Oguma K, Fujinaga Y, Inoue K. Structure and function of Clostridium botulinum toxins. Microbiol. Immunol. 1995;39:161–168.
Franciosa G, Ferreira JL, Hatheway CL. Detection of type A, B, and E botulism neurotoxin genes in Clostridium botulinum and other Clostridium species by PCR: evidence of unexpressed type B toxin genes in type A toxigenic organisms. J. Clin. Microbiol. 1994; 32:1911–1917.
Cathey, John. "Re: Tetanus." Tetanus. Madsci Network, 27 Feb. 1998. Web. 23 April. 2018.
Montecucco C, Schiavo G. Mechanism of action of tetanus and botulinum neurotoxins. Mol. Microbiol. 1994;13:1–8.
Helting TB, Parschat S, Engelhardt H. Structure of tetanus toxin. Demonstration and separation of a specific enzyme converting intracellular tetanus toxin to the extracellular form. J. Biol. Chem. 1979;254:10728–10733.
Schiavo GG, Benfenati F, Poulain B, Rossetto O, de Laureto PP, DasGupta BR, Montecucco C. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin. Nature 1992;359: 832.
Mukherjee K, Karlsson S, Burman LG, Åkerlund T. Proteins released during high toxin production in Clostridium difficile. Microbiology. 2002;148:2245–2253.
Driessen AJM, Fekkes P, van der Wolk JPW. The sec system. Curr. Opin. Microbiol. 1998; 1:216–222.
Nouwen N, Driessen AJM. SecDFyajC forms a heterotetrameric complex with YidC. Mol. Microbiol. 2002;44:1397–1405.
Brüggemann H, Bäumer S, Fricke WF, Wiezer A, Liesegang H, Decker I, Herzberg C, Martinez-Arias R, Merkl R, Henne A. The genome sequence of Clostridium tetani, the causative agent of tetanus disease. Proc. Natl. Acad. Sci. 2003;100:1316–1321.
Willis AT. Clostridia of wound infection. Clostridia wound Infect; 1969.
Al-Khatib G. Beitrage zur Clostridien differenzierung. Zur Differenzierung von Cl. septicum and Cl. chauvoei. Arch Exp Vet. 1969;23:963–970.
Princewill TJ, Oakley CL. Deoxyribonucleases and hyaluronidases of Clostridium septicum and Clostridium chauvoei. III. Relationship between the two organisms. Med. Lab. Sci. 1976;33:10–118.
Moussa RS. Complexity of toxins from Clostridium septicum and Clostridium chauvoei. J. Bacteriol. 1958;76:538.
Gadalla MSA, Collee JG. The relationship of the neuraminidase of Clostridium septicum to the haemagglutinin and other soluble products of the organism. J. Pathol. 1968;96: 169–184.
Hacker J, Bender L, Ott M, Wingender J, Lund B, Marre R, Goebel W. Deletions of chromosomal regions coding for fimbriae and hemolysins occur in vitro and in vivo in various extraintestinal Escherichiacoli isolates. Microb. Pathog. 1990;8:213–225.
Herbert Schmidt and Michael Hensel. Pathogenicity Islands in Bacterial Pathogenesis. Clinical Microbiology Reviews. 2004;17(1):14–56.
Smith TJ, Hill KK, Foley BT, Detter JC, Munk AC, Bruce DC, et al. Analysis of the Neurotoxin Complex Genes in Clostridium botulinum A1-A4 and B1 Strains : BoNT / A3 , / Ba4 and / B1 Clusters Are Located within Plasmids; 2007. Available:https://doi.org/10.1371/journal.pone.0001271
-
Abstract View: 298 times
PDF Download: 4 times
Download Statistics
Downloads
Download data is not yet available.
Subscription
Login to access subscriber-only resources.
Information
Current Issue
