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  In-depth quantitative proteomics analysis of the Pseudomonas aeruginosa secretome

Lampaki, D., Diepold, A., & Glatter, T. (2024). In-depth quantitative proteomics analysis of the Pseudomonas aeruginosa secretome. In G. Bertoni (Ed.), Pseudomonas aeruginosa. Methods in Molecular Biology (pp. 197-211). doi:10.1007/978-1-0716-3473-8_14.

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 Creators:
Lampaki, Dimitrios1, Author           
Diepold, Andreas1, Author                 
Glatter, Timo2, Author                 
Affiliations:
1Research Group Bacterial Secretion Systems, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266306              
2Core Facility Mass Spectrometry and Proteomics, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266266              

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 Abstract: Secreted proteins play vital roles in bacterial communication, metabolism, and virulence. However, analysis of the bacterial secretome can be challenging, especially if bacteria require rich media for growth or secretion. In this protocol, we describe an efficient and sensitive method to analyze the secretome by shotgun proteomics, using a combination of trichloroacetic acid (TCA) precipitation and single-pot solid-phase-enhanced sample preparation (SP3) for the preparation of the samples. The method was used to identify and quantify proteins secreted by wildtype Pseudomonas aeruginosa PAO1, highlighting its applicability for proteins secreted in limited amounts and in rich media.

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Language(s): eng - English
 Dates: 20232024
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Pseudomonas aeruginosa. Methods in Molecular Biology
Source Genre: Book
 Creator(s):
Bertoni, G.1, Editor
Ferrara, S., Author
Affiliations:
1 Humana, New York, NY. , ou_persistent22            
Publ. Info: -
Pages: - Volume / Issue: 2721 Sequence Number: - Start / End Page: 197 - 211 Identifier: -