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. 1985 Aug;49(2):414–416. doi: 10.1128/iai.49.2.414-416.1985

Cloning and expression of two Streptococcus mutans glucosyltransferases in Escherichia coli K-12.

M L Gilpin, R R Russell, P Morrissey
PMCID: PMC262032  PMID: 3160662

Abstract

Chromosomal DNA from Streptococcus mutans strain MFe28 (serotype h) was cloned in the bacteriophage vector lambda L47.1. Two classes of recombinants were found which expressed glucosyltransferase activity in phage plaques: (i) gtfS, which expressed a glucosyltransferase synthesizing a water-soluble, dextranase-sensitive glucan, and (ii) gtfI, which expressed a primer-dependent glucosyltransferase synthesizing an insoluble glucan.

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Selected References

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  1. Beighton D., Russell R. R., Hayday H. The isolation of characterization of Streptococcus mutans serotype h from dental plaque of monkeys (Macaca fascicularis). J Gen Microbiol. 1981 Jun;124(2):271–279. doi: 10.1099/00221287-124-2-271. [DOI] [PubMed] [Google Scholar]
  2. Ciardi J. E., Beaman A. J., Wittenberger C. L. Purification, resolution, and interaction of the glucosyltransferases of Streptococcus mutans 6715. Infect Immun. 1977 Oct;18(1):237–246. doi: 10.1128/iai.18.1.237-246.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fukui K., Moriyama T., Miyake Y., Mizutani K., Tanaka O. Purification and properties of glucosyltransferase responsible for water-insoluble glucan synthesis from Streptococcus mutans. Infect Immun. 1982 Jul;37(1):1–9. doi: 10.1128/iai.37.1.1-9.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Fukushima K., Motoda R., Takada K., Ikeda T. Resolution of Streptococcus mutans glycosyltransferases into two components essential to water-insoluble glucan synthesis. FEBS Lett. 1981 Jun 15;128(2):213–216. doi: 10.1016/0014-5793(81)80083-x. [DOI] [PubMed] [Google Scholar]
  5. Furuta T., Nisizawa T., Chiba J., Hamada S. Production of monoclonal antibody against a glucosyltransferase of Streptococcus mutans 6715. Infect Immun. 1983 Aug;41(2):872–875. doi: 10.1128/iai.41.2.872-875.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gibbons R. J., Houte J. V. Bacterial adherence in oral microbial ecology. Annu Rev Microbiol. 1975;29:19–44. doi: 10.1146/annurev.mi.29.100175.000315. [DOI] [PubMed] [Google Scholar]
  7. Grahame D. A., Mayer R. M. The origin and composition of multiple forms of dextransucrase from Streptococcus sanguis. Biochim Biophys Acta. 1984 Apr 27;786(1-2):42–48. doi: 10.1016/0167-4838(84)90151-1. [DOI] [PubMed] [Google Scholar]
  8. Hamada S., Slade H. D. Biology, immunology, and cariogenicity of Streptococcus mutans. Microbiol Rev. 1980 Jun;44(2):331–384. doi: 10.1128/mr.44.2.331-384.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Jagusztyn-Krynicka E. K., Smorawinska M., Curtiss R., 3rd Expression of Streptococcus mutans aspartate-semialdehyde dehydrogenase gene cloned into plasmid pBR322. J Gen Microbiol. 1982 May;128(5):1135–1145. doi: 10.1099/00221287-128-5-1135. [DOI] [PubMed] [Google Scholar]
  10. Kehoe M., Duncan J., Foster T., Fairweather N., Dougan G. Cloning, expression, and mapping of the Staphylococcus aureus alpha-hemolysin determinant in Escherichia coli K-12. Infect Immun. 1983 Sep;41(3):1105–1111. doi: 10.1128/iai.41.3.1105-1111.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Kuramitsu H. K. Characterization of extracellular glucosyltransferase activity of Steptococcus mutans. Infect Immun. 1975 Oct;12(4):738–749. doi: 10.1128/iai.12.4.738-749.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Loenen W. A., Brammar W. J. A bacteriophage lambda vector for cloning large DNA fragments made with several restriction enzymes. Gene. 1980 Aug;10(3):249–259. doi: 10.1016/0378-1119(80)90054-2. [DOI] [PubMed] [Google Scholar]
  13. Okahashi N., Nishida Y., Koga T., Hamada S. Immunochemical characteristics of Streptococcus mutans serotype h carbohydrate antigen. Microbiol Immunol. 1984;28(4):407–413. doi: 10.1111/j.1348-0421.1984.tb00692.x. [DOI] [PubMed] [Google Scholar]
  14. Robeson J. P., Barletta R. G., Curtiss R., 3rd Expression of a Streptococcus mutans glucosyltransferase gene in Escherichia coli. J Bacteriol. 1983 Jan;153(1):211–221. doi: 10.1128/jb.153.1.211-221.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Robyt J. F., Martin P. J. Mechanism of synthesis of D-glucans by D-glucosyltransferases from Streptococcus mutans 6715. Carbohydr Res. 1983 Mar 1;113(2):301–315. doi: 10.1016/0008-6215(83)88245-7. [DOI] [PubMed] [Google Scholar]
  16. Russell R. R., Coleman D., Dougan G. Expression of a gene for glucan-binding protein from Streptococcus mutans in Escherichia coli. J Gen Microbiol. 1985 Feb;131(2):295–299. doi: 10.1099/00221287-131-2-295. [DOI] [PubMed] [Google Scholar]
  17. Russell R. R. Glycosyltransferases of Streptococcus mutans strain Ingbritt. Microbios. 1978;23(93-94):136–146. [PubMed] [Google Scholar]
  18. Russell R. R. Use of triton X-100 to overcome the inhibition of fructosyltransferase by SDS. Anal Biochem. 1979 Aug;97(1):173–175. doi: 10.1016/0003-2697(79)90342-7. [DOI] [PubMed] [Google Scholar]
  19. Shimamura A., Tsumori H., Mukasa H. Purification and properties of Streptococcus mutans extracellular glucosyltransferase. Biochim Biophys Acta. 1982 Mar 18;702(1):72–80. doi: 10.1016/0167-4838(82)90028-0. [DOI] [PubMed] [Google Scholar]
  20. Tsumori H., Shimamura A., Mukasa H. Comparative study of Streptococcus mutans extracellular glycosyltransferases by isoelectric focusing. J Gen Microbiol. 1983 Oct;129(10):3261–3269. doi: 10.1099/00221287-129-10-3261. [DOI] [PubMed] [Google Scholar]

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