Skip to main content
PMC home page
Journal of Bacteriology logoLink to Journal of Bacteriology
. 1977 Nov;132(2):541–548. doi: 10.1128/jb.132.2.541-548.1977

Glucose transport in Streptococcus agalactiae and its inhibition by lactoperoxidase-thiocyanate-hydrogen peroxide.

M N Mickelson
PMCID: PMC221894  PMID: 334746

Abstract

Transport of 2-deoxyglucose or glucose in Streptococcus agalactiae was strongly inhibited if the cells were first exposed to a combination of lactoperoxidase-thiocyanate-hydrogen peroxide (LP-complex). The inhibition was completely reversible with dithiothreitol. N-ethylmaleimide and p-chloromercuribenzoate inhibited sugar transport, and the inhibition was also reversible with dithiothreitol. Sodium fluoride also inhibited sugar transport. Glucolysis was completely inhibited, and dithiothreitol completely reversed the inhibition. Phosphoenolpyruvate-dependent phosphotransferase activity in S. agalactiae was not strongly inhibited by the LP-complex. Interference of the entry of glucose into cells of S. agalactiae by the LP-complex could well account for its growth inhibitory properties with this organism. The inhibition of glucose transport by the LP-complex and its reversibility with dithiothreitol suggest the modification of functional sulfhydryl groups in the cell membrane as a cause of transport inhibition.

Full text

PDF
541

Selected References

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

  1. Barnes E. M., Jr, Kaback H. R. Mechanisms of active transport in isolated membrane vesicles. I. The site of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in Escherichia coli membrane vesicles. J Biol Chem. 1971 Sep 10;246(17):5518–5522. [PubMed] [Google Scholar]
  2. Boos W. Bacterial transport. Annu Rev Biochem. 1974;43(0):123–146. doi: 10.1146/annurev.bi.43.070174.001011. [DOI] [PubMed] [Google Scholar]
  3. Buege J. A., Aust S. D. Lactoperoxidase-catalyzed lipid peroxidation of microsomal and artificial membranes. Biochim Biophys Acta. 1976 Aug 24;444(1):192–201. doi: 10.1016/0304-4165(76)90236-1. [DOI] [PubMed] [Google Scholar]
  4. Chung J., Wood J. L. Oxidation of thiocyanate to cyanide and sulfate by the lactoperoxidase-hydrogen peroxide system. Arch Biochem Biophys. 1970 Nov;141(1):73–78. doi: 10.1016/0003-9861(70)90108-6. [DOI] [PubMed] [Google Scholar]
  5. Fox C. F., Kennedy E. P. Specific labeling and partial purification of the M protein, a component of the beta-galactoside transport system of Escherichia coli. Proc Natl Acad Sci U S A. 1965 Sep;54(3):891–899. doi: 10.1073/pnas.54.3.891. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Hogg D. M., Jago G. R. The antibacterial action of lactoperoxidase. The nature of the bacterial inhibitor. Biochem J. 1970 May;117(4):779–790. doi: 10.1042/bj1170779. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. JAGO G. R., MORRISON M. Anti-streptococcal activity of lactoperoxidase III. Proc Soc Exp Biol Med. 1962 Dec;111:585–588. doi: 10.3181/00379727-111-27862. [DOI] [PubMed] [Google Scholar]
  8. Kaback H. R., Barnes E. M., Jr Mechanisms of active transport in isolated membrane vesicles. II. The mechanism of energy coupling between D-lactic dehydrogenase and beta-galactoside transport in membrane preparations from Escherichia coli. J Biol Chem. 1971 Sep 10;246(17):5523–5531. [PubMed] [Google Scholar]
  9. Kanapka J. A., Khandelwal R. L., Hamilton I. R. Fluoride inhibition of glucose-6-P formation in Streptococcus salivarius: relation to glycogen synthesis and degradation. Arch Biochem Biophys. 1971 Jun;144(2):596–602. doi: 10.1016/0003-9861(71)90366-3. [DOI] [PubMed] [Google Scholar]
  10. Klebanoff S. J., Clem W. H., Luebke R. G. The peroxidase-thiocyanate-hydrogen peroxide antimicrobial system. Biochim Biophys Acta. 1966 Mar 28;117(1):63–72. doi: 10.1016/0304-4165(66)90152-8. [DOI] [PubMed] [Google Scholar]
  11. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  12. Leder I. G. Interrelated effects of cold shock and osmotic pressure on the permeability of the Escherichia coli membrane to permease accumulated substrates. J Bacteriol. 1972 Jul;111(1):211–219. doi: 10.1128/jb.111.1.211-219.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. McKay L., Miller A., 3rd, Sandine W. E., Elliker P. R. Mechanisms of lactose utilization by lactic acid streptococci: enzymatic and genetic analyses. J Bacteriol. 1970 Jun;102(3):804–809. doi: 10.1128/jb.102.3.804-809.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Mickelson M. N. Effect of lactoperoxidase and thiocyanate on the growth of Streptococcus pyogenes and Streptococcus agalactiae in a chemically defined culture medium. J Gen Microbiol. 1966 Apr;43(1):31–43. doi: 10.1099/00221287-43-1-31. [DOI] [PubMed] [Google Scholar]
  15. Mickelson M. N. Glucose degradation, molar growth yields, and evidence for oxidative phosphorylation in Streptococcus agalactiae. J Bacteriol. 1972 Jan;109(1):96–105. doi: 10.1128/jb.109.1.96-105.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Oram J. D., Reiter B. The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. The effect of the inhibitory system on susceptible and resistant strains of group N streptococci. Biochem J. 1966 Aug;100(2):373–381. doi: 10.1042/bj1000373. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Oram J. D., Reiter B. The inhibition of streptococci by lactoperoxidase, thiocyanate and hydrogen peroxide. The oxidation of thiocyanate and the nature of the inhibitory compound. Biochem J. 1966 Aug;100(2):382–388. doi: 10.1042/bj1000382. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Postma P. W., Roseman S. The bacterial phosphoenolpyruvate: sugar phosphotransferase system. Biochim Biophys Acta. 1976 Dec 14;457(3-4):213–257. doi: 10.1016/0304-4157(76)90001-0. [DOI] [PubMed] [Google Scholar]
  19. ROTHSTEIN A. Cell membrane as site of action of heavy metals. Fed Proc. 1959 Dec;18:1026–1038. [PubMed] [Google Scholar]
  20. Schachtele C. F., Mayo J. A. Phosphoenolpyruvate-dependent glucose transport in oral streptococci. J Dent Res. 1973 Nov-Dec;52(6):1209–1215. doi: 10.1177/00220345730520060801. [DOI] [PubMed] [Google Scholar]
  21. Simoni R. D., Nakazawa T., Hays J. B., Roseman S. Sugar transport. IV. Isolation and characterization of the lactose phosphotransferase system in Staphylococcus aureus. J Biol Chem. 1973 Feb 10;248(3):932–940. [PubMed] [Google Scholar]
  22. Steele W. F., Morrison M. Antistreptococcal activity of lactoperoxidase. J Bacteriol. 1969 Feb;97(2):635–639. doi: 10.1128/jb.97.2.635-639.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Willett N. P., Morse G. E. Long-chain fatty acid inhibition of growth of Streptococcus agalactiae in a chemically defined medium. J Bacteriol. 1966 Jun;91(6):2245–2250. doi: 10.1128/jb.91.6.2245-2250.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]

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

RESOURCES