Skip to main content
NCBI home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1992 Oct;174(20):6707–6710. doi: 10.1128/jb.174.20.6707-6710.1992

Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus mutans glucosyltransferases.

C von Eichel-Streiber 1, M Sauerborn 1, H K Kuramitsu 1
PMCID: PMC207659  PMID: 1307487

Abstract

The homologous C-terminal repeats of Clostridium difficile toxins (ToxA and ToxB) and streptococcal glucosyltransferases appear to mediate protein-carbohydrate interactions at cellular binding sites with sugar moieties as substrates. A consensus sequence of 134 repeating units from gram-positive bacteria indicates that these repeats have a modular design with (i) a stretch of aromatic amino acids proposed to be involved in the primary carbohydrate-protein interaction, (ii) an amplification of this interaction by repetition of the respective sequences, and (iii) a second domain, not characterized, that is responsible for carbohydrate specificity.

Full text

PDF
6710

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Banas J. A., Russell R. R., Ferretti J. J. Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt. Infect Immun. 1990 Mar;58(3):667–673. doi: 10.1128/iai.58.3.667-673.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Ferretti J. J., Gilpin M. L., Russell R. R. Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus MFe28. J Bacteriol. 1987 Sep;169(9):4271–4278. doi: 10.1128/jb.169.9.4271-4278.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. García E., García J. L., García P., Arrarás A., Sánchez-Puelles J. M., López R. Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Proc Natl Acad Sci U S A. 1988 Feb;85(3):914–918. doi: 10.1073/pnas.85.3.914. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. García P., García J. L., García E., López R. Nucleotide sequence and expression of the pneumococcal autolysin gene from its own promoter in Escherichia coli. Gene. 1986;43(3):265–272. doi: 10.1016/0378-1119(86)90215-5. [DOI] [PubMed] [Google Scholar]
  5. Gilmore K. S., Russell R. R., Ferretti J. J. Analysis of the Streptococcus downei gtfS gene, which specifies a glucosyltransferase that synthesizes soluble glucans. Infect Immun. 1990 Aug;58(8):2452–2458. doi: 10.1128/iai.58.8.2452-2458.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Johnson L. N., Cheetham J., McLaughlin P. J., Acharya K. R., Barford D., Phillips D. C. Protein-oligosaccharide interactions: lysozyme, phosphorylase, amylases. Curr Top Microbiol Immunol. 1988;139:81–134. doi: 10.1007/978-3-642-46641-0_4. [DOI] [PubMed] [Google Scholar]
  7. Kato C., Kuramitsu H. K. Carboxyl-terminal deletion analysis of the Streptococcus mutans glucosyltransferase-I enzyme. FEMS Microbiol Lett. 1990 Nov;60(3):299–302. doi: 10.1016/0378-1097(90)90321-g. [DOI] [PubMed] [Google Scholar]
  8. Loesche W. J. Role of Streptococcus mutans in human dental decay. Microbiol Rev. 1986 Dec;50(4):353–380. doi: 10.1128/mr.50.4.353-380.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lyerly D. M., Krivan H. C., Wilkins T. D. Clostridium difficile: its disease and toxins. Clin Microbiol Rev. 1988 Jan;1(1):1–18. doi: 10.1128/cmr.1.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Mooser G., Hefta S. A., Paxton R. J., Shively J. E., Lee T. D. Isolation and sequence of an active-site peptide containing a catalytic aspartic acid from two Streptococcus sobrinus alpha-glucosyltransferases. J Biol Chem. 1991 May 15;266(14):8916–8922. [PubMed] [Google Scholar]
  11. Quiocho F. A. Molecular features and basic understanding of protein-carbohydrate interactions: the arabinose-binding protein-sugar complex. Curr Top Microbiol Immunol. 1988;139:135–148. doi: 10.1007/978-3-642-46641-0_5. [DOI] [PubMed] [Google Scholar]
  12. Shiroza T., Ueda S., Kuramitsu H. K. Sequence analysis of the gtfB gene from Streptococcus mutans. J Bacteriol. 1987 Sep;169(9):4263–4270. doi: 10.1128/jb.169.9.4263-4270.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Sixma T. K., Pronk S. E., Kalk K. H., van Zanten B. A., Berghuis A. M., Hol W. G. Lactose binding to heat-labile enterotoxin revealed by X-ray crystallography. Nature. 1992 Feb 6;355(6360):561–564. doi: 10.1038/355561a0. [DOI] [PubMed] [Google Scholar]
  14. Tucker K. D., Wilkins T. D. Toxin A of Clostridium difficile binds to the human carbohydrate antigens I, X, and Y. Infect Immun. 1991 Jan;59(1):73–78. doi: 10.1128/iai.59.1.73-78.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Ueda S., Shiroza T., Kuramitsu H. K. Sequence analysis of the gtfC gene from Streptococcus mutans GS-5. Gene. 1988 Sep 15;69(1):101–109. doi: 10.1016/0378-1119(88)90382-4. [DOI] [PubMed] [Google Scholar]
  16. Wren B. W., Russell R. R., Tabaqchali S. Antigenic cross-reactivity and functional inhibition by antibodies to Clostridium difficile toxin A, Streptococcus mutans glucan-binding protein, and a synthetic peptide. Infect Immun. 1991 Sep;59(9):3151–3155. doi: 10.1128/iai.59.9.3151-3155.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Wright C. S. 2.2 A resolution structure analysis of two refined N-acetylneuraminyl-lactose--wheat germ agglutinin isolectin complexes. J Mol Biol. 1990 Oct 20;215(4):635–651. doi: 10.1016/S0022-2836(05)80174-3. [DOI] [PubMed] [Google Scholar]
  18. von Eichel-Streiber C., Laufenberg-Feldmann R., Sartingen S., Schulze J., Sauerborn M. Comparative sequence analysis of the Clostridium difficile toxins A and B. Mol Gen Genet. 1992 May;233(1-2):260–268. doi: 10.1007/BF00587587. [DOI] [PubMed] [Google Scholar]
  19. von Eichel-Streiber C., Sauerborn M. Clostridium difficile toxin A carries a C-terminal repetitive structure homologous to the carbohydrate binding region of streptococcal glycosyltransferases. Gene. 1990 Nov 30;96(1):107–113. doi: 10.1016/0378-1119(90)90348-u. [DOI] [PubMed] [Google Scholar]

Articles from Journal of Bacteriology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES