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Antibacterial activity of a lectin-like Burkholderia cenocepacia protein. MicrobiologyOpen 2, 566-575 (doi:10.1002/mbo3.95)

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Bacteriocins of the LlpA family have previously been characterized in the c-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 identi ed 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-speci c antibacterial activity, thus representing the rst functionally characterized bacteriocin within this b-proteobacterial genus. Strain-speci c killing was con ned to other members of the Bcc, with mostly Burkholderia ambifaria strains being susceptible. In addition to killing planktonic cells, this bacteriocin also acted as an antibiofilm agent.
Tijdschrift: MicrobiologyOpen
ISSN: 2045-8827
Volume: 2
Pagina's: 566-575
Jaar van publicatie:2013
Trefwoorden:lectin, protein-carbohydrate interaction, bacteriocin
  • Scopus Id: 84897112328