title: Bioinformatics and mass spectrometry for microorganism identification: proteome-wide post-translational modifications and database search algorithms for characterization of intact H. pylori.
abstract: MALDI-TOF mass spectrometry has been coupled with Internet-based proteome database search algorithms in an approach for direct microorganism identification. This approach is applied here to characterize intact H. pylori (strain 26695) Gram-negative bacteria, the most ubiquitous human pathogen. A procedure for including a specific and common posttranslational modification, N-terminal Met cleavage, in the search algorithm is described. Accounting for posttranslational modifications in putative protein biomarkers improves the identification reliability by at least an order of magnitude. The influence of other factors, such as number of detected biomarker peaks, proteome size, spectral calibration, and mass accuracy, on the microorganism identification success rate is illustrated as well.
authors.affiliation: Department of Chemistry, University of Maryland, College Park 20742, USA. demirev@wam.umd.edu
authors.forename: P A
authors.initials: PA
authors.lastname: Demirev
authors.forename: J S
authors.initials: JS
authors.lastname: Lin
authors.forename: F J
authors.initials: FJ
authors.lastname: Pineda
authors.forename: C
authors.initials: C
authors.lastname: Fenselaut
mesh_terms: D000465:Algorithms; D001426:Bacterial Proteins / Q000032:analysis / Q000378:metabolism*; D019295:Computational Biology / Q000379:methods*; D016208:Databases, Factual; D016480:Helicobacter pylori / Q000737:chemistry / Q000145:classification / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000378:metabolism*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*
chemical_list: D001426:Bacterial Proteins; D020543:Proteome