Antimicrobial activity of cecropins

Moore, A.J. and Beazley, W.D. and Bibby, M.C. and Devine, D.A. (1996) Antimicrobial activity of cecropins. Journal of Antimicrobial Chemotherapy, 37 (6). pp. 1077-1089.

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Abstract

The lytic peptides, cecropins, were originally isolated from the haemolymph of the giant silk moth, Hyalophora cecropia and possess antibacterial and anticancer activity in vitro. This study investigated the antimicrobial activity of these peptides against human pathogens using standardised assay techniques, and the activity of cecropin B on outer and inner bacterial membranes. From a panel of 15 organisms, Gram-negative bacteria were generally more sensitive to cecropins than Gram-positive organisms, especially the lipopolysaccharide defective mutant, Escherichia coli BUE55. Cecropins B and P, shared similar MIC values whereas Shiva-1, a cecropin B analogue, was less active. Through combination studies with hydrophobic antibiotics and electron microscopy, cecropin B was shown to disrupt the bacterial outer membrane. Protoplasts of Staphylococcus aureus and Staphylococcus epidermidis were resistant to cecropin B, suggesting that the cytoplasmic membranes of Gram-positive organisms were inherently more resistant to the peptide.

Item Type:	Article
Additional Information:	This study was supported by Proteus Molecular Design Ltd, UK. We also gratefully acknowledge Dr L. Quesnel for his kind help and advice, and Mr M. Nutbrown for his help with electron microscopy.
Author Affiliation:	Department of Biomedical Sciences, University of Bradford West Yorkshire, BD7 1DP, UK
Subjects:	Soil Science and Microbiology Plant Physiology and Biochemistry > Biochemistry
Divisions:	General
Depositing User:	Mr Balakrishna Garadasu
Date Deposited:	24 Jan 2013 09:11
Last Modified:	24 Jan 2013 09:11
Official URL:	http://dx.doi.org/10.1093/jac/37.6.1077
URI:	http://eprints.icrisat.ac.in/id/eprint/9376

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