10.1371/journal.pgen.1005190.t003 Louis S. Ates Louis S. Ates Roy Ummels Roy Ummels Susanna Commandeur Susanna Commandeur Robert van der Weerd Robert van der Weerd Marion Sparrius Marion Sparrius Eveline Weerdenburg Eveline Weerdenburg Marina Alber Marina Alber Rainer Kalscheuer Rainer Kalscheuer Sander R. Piersma Sander R. Piersma Abdallah M. Abdallah Abdallah M. Abdallah Moataz Abd El Ghany Moataz Abd El Ghany Alyaa M. Abdel-Haleem Alyaa M. Abdel-Haleem Arnab Pain Arnab Pain Connie R. Jiménez Connie R. Jiménez Wilbert Bitter Wilbert Bitter Edith N.G. Houben Edith N.G. Houben ESX-5-dependent surface proteins of <i>M</i>. <i>marinum</i>. Public Library of Science 2015 membrane ATPase EccC 5 pe substrate T 7S systems Outer Membrane Permeability carbon sources cell envelope fractions type VII secretion Subsequent proteomic analysis cell envelope proteins heterologous porin MspA ppe esx Pathogenic Mycobacteria Mycobacteria 2015-05-04 03:25:37 Dataset https://plos.figshare.com/articles/dataset/_ESX_5_dependent_surface_proteins_of_M_marinum_/1402941 <p>* Average normalized spectral counts from two biological replicates</p><p>Cell surface enriched and cell envelope proteins of <i>M</i>. <i>marinum</i>::<i>mspA and Δesx-5</i>::<i>mspA</i> strains were analyzed by LC-MS/MS. Proteins were classified as secreted proteins when the relative normalized abundance was four times higher in the cell-surface enriched fractions as compared to the cell envelope. Shown here are only proteins with at least a five-fold decrease in spectral counts in the Δ<i>esx-5</i>::<i>mspA</i> strain. Rows in bold indicate proteins with restored secretion in the presence of <i>esx-5</i><sub><i>tub</i></sub>.</p><p>ESX-5-dependent surface proteins of <i>M</i>. <i>marinum</i>.</p>