Abstract
The bacteriolytic effect of beta-lactam antibiotics on Bacillus subtilis and on Streptococcus pneumoniae was found to be a function of the pH; lysis was suppressed if the pH of the pneumococcal culture was below 6.0 during penicillin treatment. In the case of B. subtilis, growth at pH 6.6 prevented penicillin-induced lysis. In pneumococci, the addition of trypsin to the growth medium also protected against lysis. The pH-dependent protection phenomenon resembled in several respects the antibiotic “tolerance” of pneumococci with a defective autolytic system. (i) At the pH nonpermissive for lysis, the bacteria retained their normal sensitivity to beta-lactam and to other cell wall inhibitors; however, instead of lysis, the drug-treated bacteria simply stopped growing. Loss of viability of the cells was also greatly reduced. (ii) Protection against lysis was independent of the dose and chemical nature of the cell wall inhibitors. (iii) The protection effect was reversible; lysis and loss of viability could be triggered by a postincubation of the drug-treated bacteria at the pH permissive for lysis.
Full text
PDF









Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Anagnostopoulos C., Spizizen J. REQUIREMENTS FOR TRANSFORMATION IN BACILLUS SUBTILIS. J Bacteriol. 1961 May;81(5):741–746. doi: 10.1128/jb.81.5.741-746.1961. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Brown W. C., Young F. E. Dynamic interactions between cell wall polymers, extracellular proteases and autolytic enzymes. Biochem Biophys Res Commun. 1970 Feb 20;38(4):564–568. doi: 10.1016/0006-291x(70)90618-2. [DOI] [PubMed] [Google Scholar]
- Herbold D. R., Glaser L. Bacillus subtilis N-acetylmuramic acid L-alanine amidase. J Biol Chem. 1975 Mar 10;250(5):1676–1682. [PubMed] [Google Scholar]
- Houtsmuller U. M., van Deenen L. L. On the amino acid esters of phosphatidyl glycerol from bacteria. Biochim Biophys Acta. 1965 Dec 2;106(3):564–576. doi: 10.1016/0005-2760(65)90072-x. [DOI] [PubMed] [Google Scholar]
- Höltje J. V., Tomasz A. Purification of the pneumococcal N-acetylmuramyl-L-alanine amidase to biochemical homogeneity. J Biol Chem. 1976 Jul 25;251(14):4199–4207. [PubMed] [Google Scholar]
- LACKS S., HOTCHKISS R. D. A study of the genetic material determining an enzyme in Pneumococcus. Biochim Biophys Acta. 1960 Apr 22;39:508–518. doi: 10.1016/0006-3002(60)90205-5. [DOI] [PubMed] [Google Scholar]
- LEDERBERG J., ST CLAIR J. Protoplasts and L-type growth of Escherichia coli. J Bacteriol. 1958 Feb;75(2):143–160. doi: 10.1128/jb.75.2.143-160.1958. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Leive L. The barrier function of the gram-negative envelope. Ann N Y Acad Sci. 1974 May 10;235(0):109–129. doi: 10.1111/j.1749-6632.1974.tb43261.x. [DOI] [PubMed] [Google Scholar]
- PRESTIDGE L. S., PARDEE A. B. Induction of bacterial lysis by penicillin. J Bacteriol. 1957 Jul;74(1):48–59. doi: 10.1128/jb.74.1.48-59.1957. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Rogers H. J., Forsberg C. W. Role of autolysins in the killing of bacteria by some bactericidal antibiotics. J Bacteriol. 1971 Dec;108(3):1235–1243. doi: 10.1128/jb.108.3.1235-1243.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SCHWARZ U., WEIDEL W. ZUM WIRKUNGSMECHANISMUS VON PENICILLIN. I. ISOLIERUNG UND CHARAKTERISIERUNG 2,6-DIAMINOPIMELINSAEURE ENTHALTENDER NIEDERMOLEKULARER PEPTIDE AUS PENICILLINSPHAEROPLASTEN VON ESCHERICHIA COLI B. Z Naturforsch B. 1965 Feb;20:147–153. [PubMed] [Google Scholar]
- Tomasz A., Albino A., Zanati E. Multiple antibiotic resistance in a bacterium with suppressed autolytic system. Nature. 1970 Jul 11;227(5254):138–140. doi: 10.1038/227138a0. [DOI] [PubMed] [Google Scholar]
- Tomasz A. Biological consequences of the replacement of choline by ethanolamine in the cell wall of Pneumococcus: chanin formation, loss of transformability, and loss of autolysis. Proc Natl Acad Sci U S A. 1968 Jan;59(1):86–93. doi: 10.1073/pnas.59.1.86. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tomasz A. Cellular metabolism in genetic transformation of pneumococci: requirement for protein synthesis during induction of competence. J Bacteriol. 1970 Mar;101(3):860–871. doi: 10.1128/jb.101.3.860-871.1970. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Tomasz A. The role of autolysins in cell death. Ann N Y Acad Sci. 1974 May 10;235(0):439–447. doi: 10.1111/j.1749-6632.1974.tb43282.x. [DOI] [PubMed] [Google Scholar]
- 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]
- 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]
- 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]
- Young F. E. Autolytic enzyme associated with cell walls of Bacillus subtilis. J Biol Chem. 1966 Aug 10;241(15):3462–3467. [PubMed] [Google Scholar]
- den Kamp JA O. P., van Iterson W., van Deenen L. L. Studies of the phospholipids and morphology of protoplasts of Bacillus megaterium. Biochim Biophys Acta. 1967;135(5):862–884. doi: 10.1016/0005-2736(67)90056-9. [DOI] [PubMed] [Google Scholar]