Proteomics

Dataset Information

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Mycobacterium tuberculosis culture filtrate LC-MS/MS

ABSTRACT: Triplicate culture filtrate samples of normal (log phase) and PBS cultured (starvation) M. tuberculosis were separated by SDS-PAGE, and 10 bands were excised from each lane after staining with Coomassie R-250. In-gel trypsin digestion was performed on gel bands followed by nanoLC. Eluting peptides were then analyzed on an LTQ FT instrument, and the resulting raw files were searched with Sequest (part of Proteome Discoverer) against an M. tuberculosis H37Rv database (downloaded from the Sanger Centre). The final combined dataset comprised 12,399 unique peptides derived from 1,362 proteins, each identified by a minimum of two distinct peptides.

REANALYSED by: PAe003971PAe003970

INSTRUMENT(S): LTQ FT

ORGANISM(S): Mycobacterium Tuberculosis H37rv

SUBMITTER: Ida Rosenkrands  

LAB HEAD: Ida Rosenkrands

PROVIDER: PXD000111 | Pride | 2013-01-24

REPOSITORIES: Pride

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Dataset's files

Source:
Action DRS
090313_01.RAW Raw
090313_01.mgf Mgf
090313_01.msf Msf
090313_02.RAW Raw
090313_02.mgf Mgf
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Publications

Proteomic profiling of Mycobacterium tuberculosis identifies nutrient-starvation-responsive toxin-antitoxin systems.

Albrethsen Jakob J   Agner Jeppe J   Piersma Sander R SR   Højrup Peter P   Pham Thang V TV   Weldingh Karin K   Jimenez Connie R CR   Andersen Peter P   Rosenkrands Ida I  

Molecular & cellular proteomics : MCP 20130123 5

In order to successfully enter the latent stage, Mycobacterium tuberculosis must adapt to conditions such as nutrient limitation and hypoxia. In vitro models that mimic latent infection are valuable tools for describing the changes in metabolism that occur when the bacterium exists in a non-growing form. We used two complementary proteomic approaches, label-free LC-MS/MS analysis and two-dimensional difference gel electrophoresis, to determine the proteome profile of extracellular proteins from  ...[more]

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