Mode of Action of Megacin Free

Abstract

Summary: Megacin however highly bactericidal for sensitive organisms was not adsorbed by them. Its bactericidal action was markedly dependent on temperature. The viability of organisms exposed to megacin at 0° was not affected. When megacin was added to exponentially growing there was cessation of growth followed by a gradual decrease in turbidity of the culture. The decrease in turbidity was, however, not associated with a total lysis of individual organisms; rather it. was the consequence of the escape of the dense intracellular material from the organisms. Intracellular components, i.e. substances which absorbed in the ultraviolet region escaped from the bacteria into the medium while cell wall remained essentially intact. When suspended in a medium containing lactose was exposed to megacin, -galactosidase appeared on the surface of bacteria.

Protoplast preparations made from and (both sensitive to megacin) were converted into ghost-like structures on the addition of megacin. On the other hand, protoplasts made from insensitive species resisted megacin. Observations indicate that megacin causes a radical change in the osmotic barrier of sensitive organisms by attacking the cytoplasmic membrane. Data available suggest that megacin is either an enzyme which breaks down the osmotic barrier of sensitive cells, or is a substance capable of activating the intrinsic enzymes of cells which lead to an autolysis of cytoplasm.

Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-21-1-51
1959-08-01
2024-03-29
Loading full text...

Full text loading...

/deliver/fulltext/micro/21/1/mic-21-1-51.html?itemId=/content/journal/micro/10.1099/00221287-21-1-51&mimeType=html&fmt=ahah

References

  1. Alföldi L. 1957; La production induite de megacine en milieu synthetique. Ann. Inst.Pasteur 94:474
    [Google Scholar]
  2. Amano T., Kato K., Okada K., Yamatani Y., Higashi Y. 1956; Studies on the role of plakin. VII. Effects on the protoplast of Bacillus megaterium. Med. J. Osaka Univ 7:217
    [Google Scholar]
  3. Amano T., Kato K., Shimizu R. 1952; Studies on the role of plakin. Med. J. Osaka Univ 3:293
    [Google Scholar]
  4. Buss E. A., Chandler C. A., Schoenbach E. B. 1949; In vitro studies of polymyxin. Ann. N.Y. Acad. Sci 51:944
    [Google Scholar]
  5. Brenner S. et al. 1958; Bacterial protoplast. Nature; Lond.: 1811713
    [Google Scholar]
  6. Ivánovics G., Alföldi L. 1954; A new antibacterial principle: megacin. Nature; Lond.: 174465
    [Google Scholar]
  7. Ivánovics G., Alföldi L. 1955; Observation on lysogenesis in Bacillus megaterium and on megacin, the antibacterial principle of this Bacillus species. Acta microbiol. Acad. Sci. Hung 2:275
    [Google Scholar]
  8. Ivánovics G., Alföldi L. 1957; Bacteriocinogenesis in Bacillus megaterium. J. gen. Microbiol 16:522
    [Google Scholar]
  9. Ivánovics G., Alföldi L., Ábrahám E. 1955; Das antibakterielle Spektrum des Megacins. Zbl. Bakt 1. Abt. Orig. 163:274
    [Google Scholar]
  10. Ivánovics G., Alföldi L., Lovas B. 1957; Cultivation and electron microscopy of a bacteriocinogenic strain of Bacillus megaterium. Acta microbiol. Acad. Sci. Hung 4:295
    [Google Scholar]
  11. Ivánovics G., Alföldi L., Széll Á. 1957; Serological types of Bacillus megaterium and their sensitivity to phages. Acta microbiol. Acad. Sci. Hung 4:333
    [Google Scholar]
  12. Jacob F., Fuerst C. R. 1958; The mechanism of lysis by phage studied with defective lysogenic bacteria. J. gen. Microbiol 18:518
    [Google Scholar]
  13. Landman O. E. 1957; Properties and induction of β-galactosidase in Bacillus megaterium. Biochim. Biophys. Acta, 23:558
    [Google Scholar]
  14. Lederberg J. 1956; Bacterial protoplast induced by penicillin. Proc. not. Acad. Sci., Wash 42:574
    [Google Scholar]
  15. McDonald M. R. 1955 In Methods in Enzymology 2 p. 429 Eds. Colowick P. S., Caplan N. O. New York: Acad. Press Inc.;
    [Google Scholar]
  16. Murphy J. S. 1958; A phage associated enzyme of Bacillus megaterium which destroy the bacterial cell wall. Virology 4:563
    [Google Scholar]
  17. Peterson E. A., Sober H. A. 1956; Chromatography of proteins. I. Cellulose ion-exchange adsorbents. J. Amer. chem. Soc 78:751
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-21-1-51
Loading
/content/journal/micro/10.1099/00221287-21-1-51
Loading

Data & Media loading...

Most cited Most Cited RSS feed