Open AccessSensitization of Microcin J25-Resistant Strains by a Membrane-Permeabilizing Peptide
Author(s) -
María Fernanda Pomares,
Mónica Delgado,
Natalia Soledad Corbalán,
Ricardo N. Farı́as,
P Vincent
Publication year - 2010
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00307-10
Subject(s) - microbiology and biotechnology , biology , bacterial outer membrane , salmonella enterica , citrobacter freundii , escherichia coli , klebsiella pneumoniae , peptide , acinetobacter baumannii , salmonella , bacteriocin , enterobacter cloacae , bacillus cereus , bacteria , biochemistry , pseudomonas aeruginosa , antimicrobial , genetics , gene
Microcin J25 (MccJ25) is a plasmid-encoded, 21-amino-acid, antibacterial peptide produced byEscherichia coli . MccJ25 inhibits RNA polymerase and the membrane respiratory chain. MccJ25 uptake intoE. coli -sensitive strains is mediated by the outer membrane receptor FhuA and the inner membrane proteins TonB, ExbB, ExbD, and SbmA. This peptide is active on someE. coli ,Salmonella , andShigella species strains, while other Gram-negative bacteria, such as clinical isolates ofEnterobacter cloacae ,Citrobacter freundii ,Klebsiella pneumoniae ,Pseudomonas aeruginosa ,Acinetobacter baumannii ,Moraxella catarrhalis , andSalmonella enterica serovar Typhimurium, are completely resistant. In the present work, we demonstrated that the membrane-permeabilizing peptide (KFF)3 K made some resistant strains sensitive to MccJ25, among themS. Typhimurium, where the antibiotic inhibitsin vitro cell growth and bacterial replication within macrophages. The results demonstrate that the membrane permeabilization induced by (KFF)3 K allows MccJ25 penetration in an FhuA and SbmA-independent manner and suggest that the combination of both peptides could be considered as a therapeutic agent against pathogenicSalmonella strains.