Proteomics

Dataset Information

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Mass spectrometry-based characterization of secretomes from different strains of Pseudomonas chlororaphis and Pseudomonas entomophila.


ABSTRACT: To characterize the molecular basis of cytotoxicity of different Pseudomonas species and strains, we analyzed the protein content of secretomes of three P. chlororaphis strains (CIP63, CIP75 and the reference strain PA23) and of six P. entomophila strains (L48 WT, or deleted for various virulence factors: the global activator GacA, the pore-forming toxin Mnl, the pore-forming toxin ExlA, and double mutants for these genes).

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Pseudomonas Entomophila L48 Pseudomonas Chlororaphis

SUBMITTER: Yohann Couté  

LAB HEAD: Yohann Couté

PROVIDER: PXD029397 | Pride | 2022-07-25

REPOSITORIES: Pride

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Publications


Two-partner secretion (TPS) is widespread in the bacterial world. The pore-forming TPS toxin ExlA of <i>Pseudomonas aeruginosa</i> is conserved in pathogenic and environmental <i>Pseudomonas</i>. While <i>P. chlororaphis</i> and <i>P. entomophila</i> displayed ExlA-dependent killing, <i>P. putida</i> did not cause damage to eukaryotic cells. ExlA proteins interacted with epithelial cell membranes; however, only ExlA <sup><i>Pch</i></sup> induced the cleavage of the adhesive molecule E-cadherin.  ...[more]

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