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Gene Review

colA  -  collagenase

Clostridium perfringens str. 13

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Disease relevance of colA


High impact information on colA

  • We found that the small 3'-portion of VR-RNA was sufficient for the activation of toxin genes, which suggested that VR-RNA itself could act as an RNA regulatory molecule for the plc and colA genes mediating the regulatory information from the VirR/VirS system in C. perfringens [6].
  • The other gene, hyp7, whose transcript was positively regulated by the VirR/VirS system, was shown to activate the transcription of the colA (kappa-toxin) and plc (alpha-toxin) genes, but not the pfoA (theta-toxin) gene in C. perfringens [7].
  • The liver cell suspension, prepared by perfusing the liver with collagenase, was treated with enterotoxin from Clostridium perfringens for 15 min [8].
  • CcpA was also required for maximum synthesis of collagenase (kappa toxin) and acted as a repressor of polysaccharide capsule synthesis in the presence of glucose, but it did not regulate synthesis of the phospholipase PLC (alpha toxin) [9].
  • Both colG and colA have a homologous gene, mscL, at their 3' ends [10].

Biological context of colA

  • Nested deletions were used to define the coding region of colA, and this region was sequenced; from the nucleotide sequence, this gene encodes a protein of 1,104 amino acids (M(r), 125,966) [1].
  • These results suggest that gene duplication and segment duplication have occurred in an ancestor cell common to C. histolyticum and C. perfringens and that further divergence of the parent gene produced colG and colA [10].
  • Southern analysis revealed that the colA gene is located 6.5 kb downstream of the pbg gene in the chromosome of C. perfringens [11].
  • It is suggested that the productivity of theta-toxin in these strains is diverse because of the multiple genetic backgrounds including single deletion of pfoA, large deletion of the pfoA-colA region and the putative point mutations [12].
  • We also identified four other gelatinases (105, 82, 78, and 67 kDa) and determined their N-terminal amino acid sequences, all of which coincided with that of either ColG or ColH [10].

Anatomical context of colA

  • 6. Toxin-induced contraction was diminished by pretreating aorta with collagenase or by rubbing the intimal surface to remove the endothelium [13].
  • Some of these virulence factors, such as the alpha toxin, which is phospholipase C, and the kappa toxin, which is a collagenase, are enzymes that hydrolyze substances essential to the integrity of membranes or other body structures [14].

Associations of colA with chemical compounds

  • The purified enzyme was identified as the major collagenase of the organism, and it cleaved typical collagenase substrates such as azocoll, a synthetic substrate (4-phenylazobenzyloxy-carbonyl-Pro-Leu-Gly-Pro-D-Arg [Pz peptide]), and a type I collagen fibril [1].
  • The 105-kDa protein also showed activity against a typical collagenase substrate, azocoll, and was inhibited by EDTA and 1,10-phenanthroline [15].

Other interactions of colA

  • The colA gene, which encodes the kappa-toxin, had two major promoters, only one of which was virR/virS-dependent [16].

Analytical, diagnostic and therapeutic context of colA

  • Intralesional injection of 3,000 to 12,650 Units of collagenase induced an increase of two- to 10-fold in the IgG levels at one to two months in 88 per cent of patients [5].
  • Pre, 1 and/or 2 month post treatment sera were analyzed in radioimmunoassays for human IgG and IgE antibodies using solid phase purified Cl. histolyticum collagenase to extract antibodies from serum and 125I-Protein A or rabbit anti-human IgE to detect bound IgG and IgE, respectively [5].


  1. Purification and characterization of Clostridium perfringens 120-kilodalton collagenase and nucleotide sequence of the corresponding gene. Matsushita, O., Yoshihara, K., Katayama, S., Minami, J., Okabe, A. J. Bacteriol. (1994) [Pubmed]
  2. Construction and virulence testing of a collagenase mutant of Clostridium perfringens. Awad, M.M., Ellemor, D.M., Bryant, A.E., Matsushita, O., Boyd, R.L., Stevens, D.L., Emmins, J.J., Rood, J.I. Microb. Pathog. (2000) [Pubmed]
  3. Identification of a novel locus that regulates expression of toxin genes in Clostridium perfringens. Ohtani, K., Bhowmik, S.K., Hayashi, H., Shimizu, T. FEMS Microbiol. Lett. (2002) [Pubmed]
  4. The genome sequence of Clostridium tetani, the causative agent of tetanus disease. Bruggemann, H., Baumer, S., Fricke, W.F., Wiezer, A., Liesegang, H., Decker, I., Herzberg, C., Martinez-Arias, R., Merkl, R., Henne, A., Gottschalk, G. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  5. Humoral immune responses in Peyronie's disease patients receiving clostridial collagenase therapy. Hamilton, R.G., Mintz, G.R., Gelbard, M.K. J. Urol. (1986) [Pubmed]
  6. Clostridial VirR/VirS regulon involves a regulatory RNA molecule for expression of toxins. Shimizu, T., Yaguchi, H., Ohtani, K., Banu, S., Hayashi, H. Mol. Microbiol. (2002) [Pubmed]
  7. Identification of novel VirR/VirS-regulated genes in Clostridium perfringens. Banu, S., Ohtani, K., Yaguchi, H., Swe, T., Cole, S.T., Hayashi, H., Shimizu, T. Mol. Microbiol. (2000) [Pubmed]
  8. Preparation of isolated liver endothelial cells and Kupffer cells in high yield by means of an enterotoxin. Blomhoff, R., Smedsrød, B., Eskild, W., Granum, P.E., Berg, T. Exp. Cell Res. (1984) [Pubmed]
  9. The CcpA protein is necessary for efficient sporulation and enterotoxin gene (cpe) regulation in Clostridium perfringens. Varga, J., Stirewalt, V.L., Melville, S.B. J. Bacteriol. (2004) [Pubmed]
  10. Gene duplication and multiplicity of collagenases in Clostridium histolyticum. Matsushita, O., Jung, C.M., Katayama, S., Minami, J., Takahashi, Y., Okabe, A. J. Bacteriol. (1999) [Pubmed]
  11. Collagenase gene (colA) is located in the 3'-flanking region of the perfringolysin O (pfoA) locus in Clostridium perfringens. Ohtani, K., Bando, M., Swe, T., Banu, S., Oe, M., Hayashi, H., Shimizu, T. FEMS Microbiol. Lett. (1997) [Pubmed]
  12. Genomic diversity in the pfoA region of the theta-toxin-deficient strains of Clostridium perfringens. Ba-Thein, W., Inui, S., Shimizu, T., Swe, T., Banu, S., Ohtani, K., Oe, M., Sakurai, N., Nakamura, S., Hayashi, H. Microbiol. Immunol. (1997) [Pubmed]
  13. Contraction of the rat isolated aorta caused by Clostridium perfringens alpha toxin (phospholipase C): evidence for the involvement of arachidonic acid metabolism. Fujii, Y., Sakurai, J. Br. J. Pharmacol. (1989) [Pubmed]
  14. Virulence factors of Clostridium perfringens. Smith, L.D. Rev. Infect. Dis. (1979) [Pubmed]
  15. The 105-kDa protein component of Bacillus cereus non-haemolytic enterotoxin (Nhe) is a metalloprotease with gelatinolytic and collagenolytic activity. Lund, T., Granum, P.E. FEMS Microbiol. Lett. (1999) [Pubmed]
  16. The virR/virS locus regulates the transcription of genes encoding extracellular toxin production in Clostridium perfringens. Ba-Thein, W., Lyristis, M., Ohtani, K., Nisbet, I.T., Hayashi, H., Rood, J.I., Shimizu, T. J. Bacteriol. (1996) [Pubmed]
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