Antibacterial activity of a lectin‐like Burkholderia cenocepacia protein. Issue 4 (5th June 2013)

• Record Type: Journal Article
• Authors: Ghequire, Maarten G. K.; De, Evelien; Wattiau, Pierre; Van, Iris; Loris, Remy; Coenye, Tom; De, René
• Is Part Of: MicrobiologyOpen. Volume 2:Issue 4(2013:Aug.)
• Page Start: 566
• Page End: 575
• Publication Date: 2013-06-05
• Subjects: Microbiology -- Periodicals; 579
• DOI: 10.1002/mbo3.95
• Languages: English
• ISSNs: 2045-8827

Abstract

<abstract abstract-type="main" id="mbo395-abs-0001"> <title>Abstract</title> <p>Bacteriocins of the LlpA family have previously been characterized in the γ‐proteobacteria <italic>Pseudomonas</italic> and <italic>Xanthomonas</italic>. 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 <italic>Burkholderia cepacia</italic> complex (Bcc) and the <italic>Burkholderia pseudomallei</italic> group. A selected recombinant LlpA‐like protein from the human isolate <italic>Burkholderia cenocepacia</italic> 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 Bcc, with mostly <italic>Burkholderia ambifaria</italic> strains being susceptible. In addition to killing planktonic cells, this bacteriocin also acted as an antibiofilm agent.</p> </abstract>