title: Ribosomal proteins as biomarkers for bacterial identification by mass spectrometry in the clinical microbiology laboratory.
abstract: Whole-cell matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-TOF MS) is a rapid method for identification of microorganisms that is increasingly used in microbiology laboratories. This identification is based on the comparison of the tested isolate mass spectrum with reference databases. Using Neisseria meningitidis as a model organism, we showed that in one of the available databases, the Andromas database, 10 of the 13 species-specific biomarkers correspond to ribosomal proteins. Remarkably, one biomarker, ribosomal protein L32, was subject to inter-strain variability. The analysis of the ribosomal protein patterns of 100 isolates for which whole genome sequences were available, confirmed the presence of inter-strain variability in the molecular weight of 29 ribosomal proteins, thus establishing a correlation between the sequence type (ST) and/or clonal complex (CC) of each strain and its ribosomal protein pattern. Since the molecular weight of three of the variable ribosomal proteins (L30, L31 and L32) was included in the spectral window observed by MALDI-TOF MS in clinical microbiology, i.e., 3640-12000 m/z, we were able by analyzing the molecular weight of these three ribosomal proteins to classify each strain in one of six subgroups, each of these subgroups corresponding to specific STs and/or CCs. Their detection by MALDI-TOF allows therefore a quick typing of N. meningitidis isolates.
authors.affiliation: Hôpital Necker Enfants Malades, Paris, France.
authors.forename: Stéphanie
authors.initials: S
authors.lastname: Suarez
authors.forename: Agnès
authors.initials: A
authors.lastname: Ferroni
authors.forename: Aurélie
authors.initials: A
authors.lastname: Lotz
authors.forename: Keith A
authors.initials: KA
authors.lastname: Jolley
authors.forename: Philippe
authors.initials: P
authors.lastname: Guérin
authors.forename: Julie
authors.initials: J
authors.lastname: Leto
authors.forename: Brunhilde
authors.initials: B
authors.lastname: Dauphin
authors.forename: Anne
authors.initials: A
authors.lastname: Jamet
authors.forename: Martin C J
authors.initials: MC
authors.lastname: Maiden
authors.forename: Xavier
authors.initials: X
authors.lastname: Nassif
authors.forename: Jean
authors.initials: J
authors.lastname: Armengaud
mesh_terms: D001426:Bacterial Proteins / Q000032:analysis* / Q000737:chemistry / Q000145:classification; D015373:Bacterial Typing Techniques / Q000379:methods*; D015415:Biomarkers / Q000032:analysis* / Q000737:chemistry; D016000:Cluster Analysis; D030562:Databases, Protein; D006801:Humans; D008585:Meningitis, Meningococcal / Q000382:microbiology; D008954:Models, Biological; D009345:Neisseria meningitidis / Q000737:chemistry / Q000302:isolation & purification; D010802:Phylogeny; D012269:Ribosomal Proteins / Q000032:analysis* / Q000737:chemistry / Q000145:classification; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods
chemical_list: D001426:Bacterial Proteins; D015415:Biomarkers; D012269:Ribosomal Proteins
keywords: Biomarkers; Mass spectrometry; Neisseria meningitidis; Ribosomal proteins
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