Proteomic characterization of the whole secretome of Legionella pneumophila and functional analysis of outer membrane vesicles.

ABSTRACT: Secretion of effector molecules is one of the major mechanisms by which the intracellular human pathogen Legionella pneumophila interacts with host cells during infection. Specific secretion machineries which are responsible for the subfraction of secreted proteins (soluble supernatant proteins [SSPs]) and the production of bacterial outer membrane vesicles (OMVs) both contribute to the protein composition of the extracellular milieu of this lung pathogen. Here we present comprehensive proteome reference maps for both SSPs and OMVs. Protein identification and assignment analyses revealed a total of 181 supernatant proteins, 107 of which were specific to the SSP fraction and 33 of which were specific to OMVs. A functional classification showed that a large proportion of the identified OMV p

SUBMITTER: Galka F 

PROVIDER: S-EPMC2346698 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature