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Plant lectin‐like antibacterial proteins from phytopathogens Pseudomonas syringae and Xanthomonas citri
Author(s) -
Ghequire Maarten G. K.,
Li Wen,
Proost Paul,
Loris Remy,
De Mot René
Publication year - 2012
Publication title -
environmental microbiology reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.229
H-Index - 69
ISSN - 1758-2229
DOI - 10.1111/j.1758-2229.2012.00331.x
Subject(s) - pseudomonas syringae , biology , xanthomonas citri , bacteriocin , xanthomonas , microbiology and biotechnology , pseudomonas fluorescens , pseudomonas putida , rhizosphere , lectin , pseudomonadaceae , pseudomonas , pseudomonadales , bacteria , antimicrobial , pathogen , genetics , biochemistry
Summary 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, LlpA Pss642 and LlpA Xcm761 , 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 LlpA Xcm761 . 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.