ArticlePloS one2012
Analysis of Pseudomonas aeruginosa cell envelope proteome by capture of surface-exposed proteins on activated magnetic nanoparticles.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- A Shaving Proteomic Approach to Unveil Surface Proteins Modulation of Multi-Drug ResistantFrontiers in medicine · 2022Article
- The Quorum-Sensing Inhibitor Furanone C-30 Rapidly Loses Its Tobramycin-Potentiating Activity against Pseudomonas aeruginosa Biofilms during Experimental Evolution.Antimicrobial agents and chemotherapy · 2021Article
- Surfaceome and Exoproteome Dynamics in Dual-SpeciesFrontiers in microbiology · 2021Article
- Structural characterization of PaFkbA: A periplasmic chaperone fromComputational and structural biotechnology journal · 2021Article
- The Landscape ofCells · 2020Article
- Deep phenotypic characterization of immunization-induced antibacterial IgG repertoires in mice using a single-antibody bioassay.Communications biology · 2020Article
- Identification of a Ribosomal Protein RpsB as a Surface-Exposed Protein and Adhesin ofBioMed research international · 2019Article
- Article
- Outer-membrane protein LptD (PA0595) plays a role in the regulation of alginate synthesis in Pseudomonas aeruginosa.Journal of medical microbiology · 2018Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We report on specific magneto-capturing followed by Multidimensional Protein Identification Technology (MudPIT) for the analysis of surface-exposed proteins of intact cells of the bacterial opportunistic pathogen Pseudomonas aeruginosa. The magneto-separation of cell envelope fragments from the soluble cytoplasmic fraction allowed the MudPIT identification of the captured and neighboring proteins. Remarkably, we identified 63 proteins captured directly by nanoparticles and 67 proteins embedded in the cell envelope fragments. For a high number of proteins, our analysis strongly indicates either surface exposure or localization in an envelope district. The localization of most identified proteins was only predicted or totally unknown. This novel approach greatly improves the sensitivity and specificity of the previous methods, such as surface shaving with proteases that was also tested on P. aeruginosa. The magneto-capture procedure is simple, safe, and rapid, and appears to be well-suited for envelope studies in highly pathogenic bacteria.
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