Plant lectin-like antibacterial proteins from phytopathogens Pseudomonas syringae and Xanthomonas citri
Maarten G K Ghequire1, Wen Li, Paul Proost
1Centre of Microbial and Plant Genetics, KU Leuven, Kasteelpark Arenberg 20, 3001 Heverlee, Belgium Laboratory of Molecular Immunology, Rega Institute for Medical Research, KU Leuven, 3000 Leuven, Belgium Molecular Recognition Unit, Department of Structural Biology, Vlaams Instituut voor Biotechnologie, 1050 Brussel, Belgium Structural Biology Brussels, Department of Biotechnology (DBIT), Vrije Universiteit Brussel, 1050 Brussel, Belgium.
Abstract:
The genomes of Pseudomonas syringae pv. syringae 642 and Xanthomonas citri pv. malvacearum LMG 761 each carry a putative homologue of the plant lectin-like bacteriocin (llpA) genes previously identified in the rhizosphere isolate Pseudomonas putida BW11M1 and the biocontrol strain Pseudomonas fluorescens Pf-5. The respective purified recombinant proteins, LlpAPss642 and LlpAXcm761 , display genus-specific antibacterial activity across species boundaries. The inhibitory spectrum of the P. syringae bacteriocin overlaps partially with those of the P. putida and P. fluorescens LlpAs. Notably, Xanthomonas axonopodis pv. citri str. 306 secretes a protein identical to LlpAXcm761 . The functional characterization of LlpA proteins from two different phytopathogenic γ-proteobacterial species expands the lectin-like bacteriocin family beyond the Pseudomonas genus and suggests its involvement in competition among closely related plant-associated bacteria with different lifestyles.
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