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. 1978 Jul;135(1):153–160. doi: 10.1128/jb.135.1.153-160.1978

Cellular lysis of Streptococcus faecalis induced with triton X-100.

J B Cornett, G D Shockman
PMCID: PMC224794  PMID: 97265

Abstract

Lysis of exponential-phase cultures of Streptococcus faecalis ATCC 9790 was induced by exposure to both anionic (sodium dodecyl sulfate) and nonionic (Triton X-100) surfactants. Lysis in response to sodium dodecyl sulfate was effective only over a limited range of concentrations, whereas Triton X-100-induced lysis occurred over a broad range of surfactant concentrations. The data presented indicate that the bacteriolytic response of growing cells to Triton X-100: (i) was related to the ratio of surfactant to cells and not the surfactant concentration per se; (ii) required the expression of the cellular autolytic enzyme system; and (iii) was most likely due to an effect of the surfactant on components of the autolytic system that are associated with the cytoplasmic membrane. The possibility that Triton X-100 may induce cellular lysis by releasing a lipid inhibitor of the cellular autolytic enzyme is discussed.

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Selected References

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

  1. Birdsell D. C., Cota-Robles E. H. Lysis of spheroplasts of Escherichia coli by a non-ionic detergent. Biochem Biophys Res Commun. 1968 May 10;31(3):438–446. doi: 10.1016/0006-291x(68)90496-8. [DOI] [PubMed] [Google Scholar]
  2. Brierley G. P., Jurkowitz M., Merola A. J., Scott K. M. Ion transport by heart mitochondria. XXV. Activation of energy-linked K + uptake by non-ionic detergents. Arch Biochem Biophys. 1972 Oct;152(2):744–754. doi: 10.1016/0003-9861(72)90270-6. [DOI] [PubMed] [Google Scholar]
  3. Cavard D., Vallée M., Barbu E. Mise an évidence par le lauryl-sulfate de quelques modifications précoces de la membrane de E. COLI PROVOQUEES PAR LES PHAGES T4, les faômes de phages T4 et la colicine K. Biochimie. 1974;56(2):221–230. doi: 10.1016/s0300-9084(74)80381-0. [DOI] [PubMed] [Google Scholar]
  4. Cleveland R. F., Daneo-Moore L., Wicken A. J., Shockman G. D. Effect of lipoteichoic acid and lipids on lysis of intact cells of Streptococcus faecalis. J Bacteriol. 1976 Sep;127(3):1582–1584. doi: 10.1128/jb.127.3.1582-1584.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Cleveland R. F., Holtje J. V., Wicken A. J., Tomasz A., Daneo-Moore L., Shockman G. D. Inhibition of bacterial wall lysins by lipoteichoic acids and related compounds. Biochem Biophys Res Commun. 1975 Dec 1;67(3):1128–1135. doi: 10.1016/0006-291x(75)90791-3. [DOI] [PubMed] [Google Scholar]
  6. Cleveland R. F., Wicken A. J., Daneo-Moore L., Shockman G. D. Inhibition of wall autolysis in Streptococcus faecalis by lipoteichoic acid and lipids. J Bacteriol. 1976 Apr;126(1):192–197. doi: 10.1128/jb.126.1.192-197.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cornett J. B., Redman B. E., Shockman G. D. Autolytic defective mutant of Streptococcus faecalis. J Bacteriol. 1978 Feb;133(2):631–640. doi: 10.1128/jb.133.2.631-640.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Coyette J., Shockman G. D. Some properties of the autolytic N-acetylmuramidase of Lactobacillus acidophilus. J Bacteriol. 1973 Apr;114(1):34–41. doi: 10.1128/jb.114.1.34-41.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. DAWSON I. M., LOMINSKI I., STERN H. An electron-microscope study of the action of cetyl-trimethyl-ammonium bromide on Staphylococcus aureus. J Pathol Bacteriol. 1953 Oct;66(2):513–526. doi: 10.1002/path.1700660223. [DOI] [PubMed] [Google Scholar]
  10. Davis B. D. The Isolation of Biochemically Deficient Mutants of Bacteria by Means of Penicillin. Proc Natl Acad Sci U S A. 1949 Jan;35(1):1–10. doi: 10.1073/pnas.35.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. De Petris S. Ultrastructure of the cell wall of Escherichia coli and chemical nature of its constituent layers. J Ultrastruct Res. 1967 Jul;19(1):45–83. doi: 10.1016/s0022-5320(67)80059-5. [DOI] [PubMed] [Google Scholar]
  12. Egan R. W. Hydrophile-lipophile balance and critical micelle concentration as key factors influencing surfactant disruption of mitochondrial membranes. J Biol Chem. 1976 Jul 25;251(14):4442–4447. [PubMed] [Google Scholar]
  13. Fein J. E., Rogers H. J. Autolytic enzyme-deficient mutants of Bacillus subtilis 168. J Bacteriol. 1976 Sep;127(3):1427–1442. doi: 10.1128/jb.127.3.1427-1442.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Godson G. N., Sinsheimer R. L. Lysis of Escherichia coli with a neutral detergent. Biochim Biophys Acta. 1967 Dec 19;149(2):476–488. doi: 10.1016/0005-2787(67)90175-x. [DOI] [PubMed] [Google Scholar]
  15. Hartmann R., Bock-Hennig S. B., Schwarz U. Murein hydrolases in the envelope of Escherichia coli. Properties in situ and solubilization from the envelope. Eur J Biochem. 1974 Jan 3;41(1):203–208. doi: 10.1111/j.1432-1033.1974.tb03261.x. [DOI] [PubMed] [Google Scholar]
  16. Helenius A., Simons K. Solubilization of membranes by detergents. Biochim Biophys Acta. 1975 Mar 25;415(1):29–79. doi: 10.1016/0304-4157(75)90016-7. [DOI] [PubMed] [Google Scholar]
  17. Howard L. V., Gooder H. Specificity of the autolysin of Streptococcus (Diplococcus) pneumoniae. J Bacteriol. 1974 Feb;117(2):796–804. doi: 10.1128/jb.117.2.796-804.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Joseph R., Shockman G. D. Autolytic formation of protoplasts (autoplasts) of Streptococcus faecalis 9790: release of cell wall, autolysin, and formation of stable autoplasts. J Bacteriol. 1974 May;118(2):735–746. doi: 10.1128/jb.118.2.735-746.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Joseph R., Shockman G. D. Autolytic formation of protoplasts (autoplasts) of Streptococcus faecalis; location of active and latent autolysin. J Bacteriol. 1976 Sep;127(3):1482–1493. doi: 10.1128/jb.127.3.1482-1493.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Lacks S. Mutants of Diplococcus pneumoniae that lack deoxyribonucleases and other activities possibly pertinent to genetic transformation. J Bacteriol. 1970 Feb;101(2):373–383. doi: 10.1128/jb.101.2.373-383.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. PETHICA B. A., SCHULMAN J. H. The physical chemistry of haemolysis by surface-active agents. Biochem J. 1953 Jan;53(2):177–185. doi: 10.1042/bj0530177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Pooley H. M., Shockman G. D. Relationship between the latent form and the active form of the autolytic enzyme of Streptococcus faecalis. J Bacteriol. 1969 Nov;100(2):617–624. doi: 10.1128/jb.100.2.617-624.1969. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Pooley H. M., Shockman G. D. Relationship between the location of autolysin, cell wall synthesis, and the development of resistance to cellular autolysis in Streptococcus faecalis after inhibition of protein synthesis. J Bacteriol. 1970 Aug;103(2):457–466. doi: 10.1128/jb.103.2.457-466.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Roth G. S., Shockman G. D., Daneo-Moore L. Balanced macromolecular biosynthesis in "protoplasts" of Streptococcus faecalis. J Bacteriol. 1971 Mar;105(3):710–717. doi: 10.1128/jb.105.3.710-717.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Sayare M., Daneo-Moore L., Shockman G. D. Influence of macromolecular biosynthesis on cellular autolysis in Streptococcus faecalis. J Bacteriol. 1972 Oct;112(1):337–344. doi: 10.1128/jb.112.1.337-344.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Schlieper P., De Robertis E. Triton X-100 as a channel-forming substance in artificial lipid bilayer membranes. Arch Biochem Biophys. 1977 Nov;184(1):204–208. doi: 10.1016/0003-9861(77)90343-5. [DOI] [PubMed] [Google Scholar]
  27. Schnaitman C. A. Effect of ethylenediaminetetraacetic acid, Triton X-100, and lysozyme on the morphology and chemical composition of isolate cell walls of Escherichia coli. J Bacteriol. 1971 Oct;108(1):553–563. doi: 10.1128/jb.108.1.553-563.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Schnaitman C. A. Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol. 1971 Oct;108(1):545–552. doi: 10.1128/jb.108.1.545-552.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Shockman G. D., Thompson J. S., Conover M. J. The autolytic enzyme system of Streptococcus faecalis. II. Partial characterization of the autolysin and its substrate. Biochemistry. 1967 Apr;6(4):1054–1065. doi: 10.1021/bi00856a014. [DOI] [PubMed] [Google Scholar]
  30. Singer H. J., Wise E. M., Jr, Park J. T. Properties and purification of N-acetylmuramyl-L-alanine amidase from Staphylococcus aureus H. J Bacteriol. 1972 Nov;112(2):932–939. doi: 10.1128/jb.112.2.932-939.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Swenson P. A., Schenley R. L. Evidence relating cessation of respiration, cell envelope changes, and death in ultraviolet-irradiated Escherichia coli B-r cells. J Bacteriol. 1974 Feb;117(2):551–559. doi: 10.1128/jb.117.2.551-559.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Tomasz A., Waks S. Enzyme replacement in a bacterium: phenotypic correction by the experimental introduction of the wild type enzyme into a live enzyme defective mutant pneumococcus. Biochem Biophys Res Commun. 1975 Aug 18;65(4):1311–1319. doi: 10.1016/s0006-291x(75)80373-1. [DOI] [PubMed] [Google Scholar]
  33. Tomasz A., Waks S. Mechanism of action of penicillin: triggering of the pneumococcal autolytic enzyme by inhibitors of cell wall synthesis. Proc Natl Acad Sci U S A. 1975 Oct;72(10):4162–4166. doi: 10.1073/pnas.72.10.4162. [DOI] [PMC free article] [PubMed] [Google Scholar]
  34. Umbreit J. N., Strominger J. L. Relation of detergent HLB number to solubilization and stabilization of D-alanine carboxypeptidase from Bacillus subtilis membranes. Proc Natl Acad Sci U S A. 1973 Oct;70(10):2997–3001. doi: 10.1073/pnas.70.10.2997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Van Zutphen H., Merola A. J., Brierley G. P., Cornwell D. G. The interaction of nonionic detergents with lipid bilayer membranes. Arch Biochem Biophys. 1972 Oct;152(2):755–766. doi: 10.1016/0003-9861(72)90271-8. [DOI] [PubMed] [Google Scholar]
  36. WEIDEL W., PELZER H. BAGSHAPED MACROMOLECULES--A NEW OUTLOOK ON BACTERIAL CELL WALLS. Adv Enzymol Relat Areas Mol Biol. 1964;26:193–232. doi: 10.1002/9780470122716.ch5. [DOI] [PubMed] [Google Scholar]
  37. Woldringh C. L., van Iterson W. Effects of treatment with sodium dodecyl sulfate on the ultrastructure of Escherichia coli. J Bacteriol. 1972 Sep;111(3):801–813. doi: 10.1128/jb.111.3.801-813.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]

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