These authors contributed equally to this work.
Saturation mutagenesis of selected residues of the α-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity
Article first published online: 25 FEB 2013
© 2013 The Authors. Microbial Biotechnology Published by John Wiley & Sons Ltd and Society for Applied Microbiology.
This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
Volume 6, Issue 5, pages 564–575, September 2013
How to Cite
Field, D., Molloy, E. M., Iancu, C., Draper, L. A., O' Connor, P. M., Cotter, P. D., Hill, C. and Ross, R. P. (2013), Saturation mutagenesis of selected residues of the α-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity. Microbial Biotechnology, 6: 564–575. doi: 10.1111/1751-7915.12041
Funding Information Work in the authors' laboratory is supported by the Irish Government under the National Development Plan; by the Irish Research Council for Science Engineering and Technology (IRCSET); by Enterprise Ireland; and by Science Foundation Ireland (SFI), through the Alimentary Pharmabiotic Centre (APC) at University College Cork, Ireland, which is supported by the SFI-funded Centre for Science, Engineering and Technology (SFI-CSET) and provided P.D.C., C.H and R.P.R. with SFI Principal Investigator funding.
- Issue published online: 14 AUG 2013
- Article first published online: 25 FEB 2013
- Manuscript Accepted: 27 DEC 2012
- Manuscript Revised: 30 NOV 2012
- Manuscript Received: 3 MAY 2012
- SFI-funded Centre for Science, Engineering and Technology (SFI-CSET)
- Irish Government
- Irish Research Council for Science Engineering and Technology (IRCSET)
- Enterprise Ireland
- Science Foundation Ireland (SFI)
The lantibiotic lacticin 3147 consists of two ribosomally synthesized and post-translationally modified antimicrobial peptides, Ltnα and Ltnβ, which act synergistically against a wide range of Gram-positive microorganisms. We performed saturation mutagenesis of specific residues of Ltnα to determine their functional importance. The results establish that Ltnα is more tolerant to change than previously suggested by alanine scanning mutagenesis. One substitution, LtnαH23S, was identified which improved the specific activity of lacticin 3147 against one pathogenic strain, Staphylococcus aureus NCDO1499. This represents the first occasion upon which the activity of a two peptide lantibiotic has been enhanced through bioengineering.