Open AccessAntibacterial activity of a lectin‐like B urkholderia cenocepacia protein
Author(s) -
Ghequire Maarten G. K.,
Canck Evelien,
Wattiau Pierre,
Winge Iris,
Loris Remy,
Coenye Tom,
Mot René
Publication year - 2013
Publication title -
microbiologyopen
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.881
H-Index - 36
ISSN - 2045-8827
DOI - 10.1002/mbo3.95
Subject(s) - bacteriocin , microbiology and biotechnology , biology , lectin , recombinant dna , bacteria , biofilm , gene , antimicrobial , genetics
Bacteriocins of the LlpA family have previously been characterized in the γ‐proteobacteria P seudomonas and X anthomonas . 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 B urkholderia cepacia complex (Bcc) and the B urkholderia pseudomallei group. A selected recombinant LlpA‐like protein from the human isolate B urkholderia 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 Bcc, with mostly B urkholderia ambifaria strains being susceptible. In addition to killing planktonic cells, this bacteriocin also acted as an antibiofilm agent.