Title: Antibacterial activity of a lectin-like Burkholderia cenocepacia protein
Authors: Ghequire, Maarten ×
De Canck, Evelien
Wattiau, Pierre
Van Winge, Iris
Loris, Remy
Coenye, Tom
De Mot, René #
Issue Date: 2013
Publisher: John Wiley & Sons Ltd.
Series Title: MicrobiologyOpen vol:2 issue:4 pages:566-575
Abstract: Bacteriocins of the LlpA family have previously been characterized in the γ-proteobacteria Pseudomonas and Xanthomonas. These proteins are composed of two MMBL (monocot mannose-binding lectin) domains, a module predominantly and abundantly found in lectins from monocot plants. Genes encoding four different types of LlpA-like proteins were identified in genomes from strains belonging to the Burkholderia cepacia complex (Bcc) and the Burkholderia pseudomallei group. A selected recombinant LlpA-like protein from the human isolate Burkholderia cenocepacia AU1054 displayed narrow-spectrum genus-specific antibacterial activity, thus representing the first functionally characterized bacteriocin within this β-proteobacterial genus. Strain-specific killing was confined to other members of the Burkholderia cepacia complex, with mostly Burkholderia ambifaria strains being susceptible. In addition to killing planktonic cells, this bacteriocin also acted as an anti-biofilm agent.
ISSN: 2045-8827
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Centre of Microbial and Plant Genetics
Teaching Support Unit, Faculty of Bioscience Engineering
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
Ghequire Burkholderia LlpA MicrobiolOpen2013.pdfOA article Published 1527KbAdobe PDFView/Open


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science