Proteomics

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Searching for Pseudomonas aeruginosa MagD partners


ABSTRACT: Opportunistic pathogen Pseudomonas aeruginosa synthesizes a structural homologue of the human alpha2-Macroglobulin protein, a large spectrum protease inhibitor and important player of innate immunity. Delta-MagD and MagD-WT Pseudomonas aeruginosa strains were lysed and lysates submitted to co-immunoprecipitation using anti-MagD antibody (2 biological replicates). Immunoprecipitated proteins were in-gel digested and resulting peptides analysed by nanoLC-MS/MS. Identifications were realised using Mascot and filtered using IRMa software (1% FDR). Results were exported to a relational database (MSIdb) and processed using hEIDI software to identify proteins enriched in MagD-WT samples compared to delta-MagD samples.

INSTRUMENT(S): LTQ Orbitrap Velos, instrument model

ORGANISM(S): Pseudomonas Aeruginosa Pao1

SUBMITTER: Yohann Couté  

PROVIDER: PXD000189 | Pride | 2013-08-09

REPOSITORIES: Pride

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Publications


<h4>Unlabelled</h4>Human pathogens frequently use protein mimicry to manipulate host cells in order to promote their survival. Here we show that the opportunistic pathogen Pseudomonas aeruginosa synthesizes a structural homolog of the human α2-macroglobulin, a large-spectrum protease inhibitor and important player of innate immunity. Small-angle X-ray scattering analysis demonstrated that the fold of P. aeruginosa MagD (PA4489) is similar to that of the human macroglobulin and undergoes a confor  ...[more]

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