Journal
PROTEOMICS
Volume 9, Issue 7, Pages 1901-1915Publisher
WILEY
DOI: 10.1002/pmic.200800618
Keywords
Cell envelope; 2-DE; MALDI-TOF/TOF; Periplasm; Pseudomonas aeruginosa
Funding
- Ministry of Health of Italy
- Ministry of University and Research of Italy (PRIN-2006)
- Fondazione per la Ricerca sulfa Fibrosi Cistica [10/2007]
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The Gram-negative bacterium Pseudomonas aeruginosa is a main cause of infection in hospitalized, burned, immunocompromised, and cystic fibrosis patients. Many processes essential for P. aeruginosa pathogenesis, e.g., nutrient uptake, antibiotic resistance, and virulence, take place in the cell envelope and depend on components residing in the periplasmic space. Recent high-throughput studies focused on P. aeruginosa membrane compartments. However, the composition and dynamics of its periplasm remain largely uncharacterized. Here, we report a detailed description of the periplasmic proteome of the wild-type P. aeruginosa strain PAO1 by 2-DE and MALDI-TOF/TOF analysis. Three extraction methods were compared at proteome level in order to achieve the most reliable and comprehensive periplasmic protein map. A total of 495 spots representing 395 different proteins were identified. Most of the high intensity spots corresponded to periplasmic proteins, while cytoplasmic contaminants were mainly detected among faint spots. The majority, of the identified periplasmic proteins is involved in transport, cell envelope integrity, and protein folding control. Notably, more than 30% still has an unpredicted function. This work provides the first overview of the P. aeruginosa periplasm and offers the basis for future studies on periplasmic proteome changes occurring during P. aeruginosa adaptation to different environments and/or antibiotic treatments.
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