The Properties of Virginiamycin-resistant Mutants of Free

Abstract

Summary: Single components of virginiamycin M and S inhibit the growth of sensitive strains of The mixture of M and S halts completely the multiplication of double-sensitive organisms and of S-sensitive M-resistant mutants, but only partly inhibits growth of M-sensitive S-resistant cells, and is without effect on double-resistant mutants. Single virginiamycin components have essentially a bacteriostatic activity, whereas the association of M and S is lethal for double-sensitive bacteria as well as for S-sensitive M-resistant mutants. This lethal effect is a two-step process, which occurs without appreciable lysis. No bactericidal effect can be observed when S-resistant cells are incubated with a mixture of M and S. The patterns of inhibition of protein synthesis in different mutants are similar to those of growth inhibition and viability loss: the latter effects are therefore consequences of the former. Virginiamycin S can have different effects on protein synthesis: it enhances the action of M in S-sensitive cells but prevents the inhibitory action of M in S-resistant mutants. It can be concluded that both virginiamycin components interfere with growth, protein formation and cell viability. However, only the gene for S-sensitivity is essential (i) for the lethal action of the association of virginiamycin M and S, (ii) for the inactivation of cells submitted to an alternate treatment with the two virginiamycin components and (iii) for rendering permanent the inhibition of protein synthesis.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-76-1-115
1973-05-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/micro/76/1/mic-76-1-115.html?itemId=/content/journal/micro/10.1099/00221287-76-1-115&mimeType=html&fmt=ahah

References

  1. Cocito C. 1969a; Metabolism of macromolecules in bacteria treated with virginiamycin. Journal of General Microbiology 57:179–194
    [Google Scholar]
  2. Cocito C. 1969b; The action of virginiamycin on nucleic acid and protein synthesis in B. subtilis infected with bacteriophage 2C. Journal of General Microbiology 57:195–206
    [Google Scholar]
  3. Cocito C. 1971; Formation and decay of polyribosomes and ribosomes during the inhibition of protein synthesis and recovery. Biochimie 53:987–1000
    [Google Scholar]
  4. Cocito C. 1973; Formation of ribosomal particles in virginiamycin sensitive and resistant mutants of B. subtilis . Biochimie (in the press)
    [Google Scholar]
  5. Cocito C., Bronchart R., Van Pel B. 1972; Phenotypic and genotypic changes produced in eucaryotic cells by protein inhibitors. Biochemical and Biophysical Research Communications 46:1688–1694
    [Google Scholar]
  6. Cocito C., Kaji A. 1971; Virginiamycin M – a specific inhibitor of the acceptor site of ribosomes. Biochimie 53:763–770
    [Google Scholar]
  7. Ennis H. L. 1965a; Inhibition of protein synthesis by polypeptide antibiotics. I. Inhibition in intact bacteria. Journal of Bacteriology 90:1102–1108
    [Google Scholar]
  8. Ennis H. L. 1965b; Inhibition of protein synthesis by polypeptide antibiotics. II. In vitro protein synthesis. Journal of Bacteriology 90:1109–1119
    [Google Scholar]
  9. Ennis H. L. 1971; Interaction of vernamycin A with E. coli ribosomes. Biochemistry 10:1265–1270
    [Google Scholar]
  10. Fan D. P., Higa A., Levinthal C. 1964; Messenger RNA decay and protection. Journal of Molecular Biology 8:210
    [Google Scholar]
  11. Laskin A. I., Chan W. M. 1964; Inhibition by vernamycin A of amino acid incorporation in E. coli cell-free systems. Antimicrobial Agents and Chemotherapy 1963:485–488
    [Google Scholar]
  12. Okamoto K., Mudd J. A., Mangan J., Hang W. M., Subbaiah T. V., Marmur J. 1968; Properties of the defective phage of B. subtilis . Journal of Molecular Biology 34:413–420
    [Google Scholar]
  13. Pestka S. 1971; Inhibitors of ribosome functions. Annual Review of Biochemistry 40:696–710
    [Google Scholar]
  14. Van Pel B., Bronchart R., Kebers F., Cocito C. 1972; Structure and function of cytoplasmic organelles in transiently and permanently bleached Euglena. Experimental Cell Research (in the press)
    [Google Scholar]
  15. Van Pel B., Cocito C. 1972; Formation of chloroplast ribosomes and ribosomal RNA in Euglena incubated with protein inhibitors. Experimental Cell Research (in the press)
    [Google Scholar]
  16. Vazquez D. 1966; Studies on the mode of action of the streptogramin antibiotics. Journal of General Microbiology 42:93–106
    [Google Scholar]
  17. Vazquez D. 1967; The streptogramin family of antibiotics. In Antibiotics vol 1 p 387 Edited by Gottlieb D., Shaw P. D. New York: Springer Verlag;
    [Google Scholar]
  18. Yamaguchi H., Tanaka N. 1964; Selective toxicity of mikamycins, inhibitors of protein synthesis. Nature, London 201:499–501
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-76-1-115
Loading
/content/journal/micro/10.1099/00221287-76-1-115
Loading

Data & Media loading...

Most cited Most Cited RSS feed