Open AccessSaturation mutagenesis of selected residues of the α‐peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity
Author(s) -
Field Des,
Molloy Evelyn M.,
Iancu Catalin,
Draper Lorraine A.,
O' Connor Paula M.,
Cotter Paul D.,
Hill Colin,
Ross R. Paul
Publication year - 2013
Publication title -
microbial biotechnology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.287
H-Index - 74
ISSN - 1751-7915
DOI - 10.1111/1751-7915.12041
Subject(s) - lantibiotics , mutagenesis , antimicrobial , saturated mutagenesis , biology , peptide , alanine scanning , antimicrobial peptides , bacteriocin , biochemistry , nisin , microbiology and biotechnology , mutation , gene , mutant
Summary The lantibiotic lacticin 3147 consists of two ribosomally synthesized and post‐translationally modified antimicrobial peptides, Ltn α and Ltn β, which act synergistically against a wide range of G ram‐positive microorganisms. We performed saturation mutagenesis of specific residues of Ltn α to determine their functional importance. The results establish that Ltn α is more tolerant to change than previously suggested by alanine scanning mutagenesis. One substitution, Ltn α H 23 S , was identified which improved the specific activity of lacticin 3147 against one pathogenic strain, S taphylococcus aureus NCDO 1499. This represents the first occasion upon which the activity of a two peptide lantibiotic has been enhanced through bioengineering.