Authors: A Khemiri A Galland D Vaudry P Chan Tchi Song H Vaudry T Jouenne P Cosette
Publish Date: 2008/02/19
Volume: 390, Issue: 7, Pages: 1861-1871
Abstract
Bacterial surfaceassociated proteins play crucial roles in host–pathogen interactions and pathogenesis The identification of these proteins represents an important goal of bacterial proteomics for vaccine development but also for environmental concerns such as microbial biosensing Here we developed such an approach for Legionella pneumophila a bacterium that causes severe pneumonia We propose a complementary strategy consisting of 1 a fluorescent labelling of surfaceexposed proteins in parallel with 2 a fractionation of the outermembrane protein extract These two distinct protein populations were subsequently separated using twodimensional gel electrophoresis and characterised by mass spectrometry Within these populations we found proteins which were expected for the compartments studied but also a great number of proteins never experimentally described and also a nonnegligible fraction of proteins never described in these fractions These data provided new routes of inspection for transport and host recognition for Legionella pneumophila In addition these results on the membranome and surfaceome show that Legionella in the stationary phase of growth possesses the major determinants to infect host cellsThis work was supported by a grant from the INTERREG IIIA programme of the European Community AMACOM We are particularly grateful to the Centre de Ressources Informatiques de HauteNormandie CRIHAN for giving us access to their computing facility and for hosting the Mascot server
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