Type

Journal Article

Authors

R Paul Ross
Colin Hill
Paul D. Cotter
Paula M. O'Connor
Lorraine A Draper
Catalin Iancu
Evelyn M. Molloy
Des Field

Subjects

Microbiology

Topics
lantibiotic antimicrobial activity staphylococcus aureus residues antimicrobial peptides antimicrobial peptide lacticin 3147 mutagenesis

Saturation mutagenesis of selected residues of the α-peptide of the lantibiotic lacticin 3147 yields a derivative with enhanced antimicrobial activity. (2012)

Abstract 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.
Collections Ireland -> University College Cork -> PubMed

Full list of authors on original publication

R Paul Ross, Colin Hill, Paul D. Cotter, Paula M. O'Connor, Lorraine A Draper, Catalin Iancu, Evelyn M. Molloy, Des Field

Experts in our system

1
R Paul Ross
Teagasc
Total Publications: 441
 
2
Colin Hill
University College Cork
Total Publications: 351
 
3
Paul D. Cotter
Teagasc
Total Publications: 253
 
4
Paula M. O'Connor
Teagasc
Total Publications: 85
 
5
Lorraine A Draper
University College Cork
Total Publications: 24
 
6
Des Field
Teagasc
Total Publications: 30