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The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli.

Abstract
The attacins are antibacterial proteins which accumulate in the hemolymph of the giant silk moth, Hyalophora cecropia, in response to a bacterial infection. Here we show that the permeability barrier function of the outer membrane is affected shortly after addition of attacin to growing cultures of Escherichia coli. Specifically, the penetration through the outer membrane of beta-lactam antibiotics, chicken egg white lysozyme and the detergent Triton X-100 was found to be facilitated. The sensitivity of E. coli to cecropin B, another antibacterial protein present in the hemolymph of H. cecropia, was also found to be increased after treatment with attacin. The results suggest that the target of the attacins in E. coli is the outer membrane. Other effects of the attacins which have been observed are likely to be indirect consequences of the alteration in the properties of the outer membrane. These effects include changes in the cell shape, irregular patterns of cell division and lysis. The minimal concentration at which the attacins affected the growth of E. coli was 1 and 0.5 microM for the neutral (pI 7) and basic (pI 9) attacins, respectively, which corresponds to less than 2% of the concentration of the attacins in the hemolymph of infected pupae.
AuthorsP Engström, A Carlsson, A Engström, Z J Tao, H Bennich
JournalThe EMBO journal (EMBO J) Vol. 3 Issue 13 Pg. 3347-51 (Dec 20 1984) ISSN: 0261-4189 [Print] England
PMID6396089 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)
Chemical References
  • Anti-Bacterial Agents
  • Insect Hormones
  • Insect Proteins
  • attacin antibacterial protein, insect
Topics
  • Animals
  • Anti-Bacterial Agents (pharmacology)
  • Cell Division (drug effects)
  • Cell Membrane (drug effects)
  • Cell Membrane Permeability (drug effects)
  • Escherichia coli (drug effects)
  • Insect Hormones (pharmacology)
  • Insect Proteins
  • Lepidoptera (metabolism)
  • Moths (metabolism)

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