Field, D;Molloy, EM;Iancu, C;Draper, LA;O' Connor, PM;Cotter, PD;Hill, C;Ross, RP

2013

September

Microbial Biotechnology

Saturation mutagenesis of selected residues of the -peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity

Validated

WOS: 18 ()

SITE-DIRECTED MUTAGENESIS PRECURSOR LIPID-II 2-PEPTIDE LANTIBIOTICS STAPHYLOCOCCUS-AUREUS NISIN BIOSYNTHESIS SYSTEM IDENTIFICATION HALODURACIN BACTERIOCIN

6

564

575

The lantibiotic lacticin 3147 consists of two ribosomally synthesized and post-translationally modified antimicrobial peptides, Ltn alpha and Ltn beta, which act synergistically against a wide range of Gram-positive microorganisms. We performed saturation mutagenesis of specific residues of Ltna to determine their functional importance. The results establish that Ltna is more tolerant to change than previously suggested by alanine scanning mutagenesis. One substitution, LtnaH23S, 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.

HOBOKEN

1751-7907

10.1111/1751-7915.12041