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>