Targeted Mass Spectrometry Analysis of Clostridium perfringens Toxins

Targeted proteomics recently proved to be a technique for the detection and absolute quantification of proteins not easily accessible to classical bottom-up approaches. Due to this, it has been considered as a high fidelity tool to detect potential warfare agents in wide spread kinds of biological a...

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Bibliographic Details
Published in:Toxins 2019-03, Vol.11 (3), p.177
Main Authors: Duracova, Miloslava, Klimentova, Jana, Myslivcova Fucikova, Alena, Zidkova, Lenka, Sheshko, Valeria, Rehulkova, Helena, Dresler, Jiri, Krocova, Zuzana
Format: Article
Language:English
Subjects:
Bacteria
Bacterial Proteins - analysis
Bacterial Proteins - genetics
Bacterial Toxins - analysis
Bacterial Toxins - genetics
Biological & chemical weapons
Biological weapons
Chromatography
Chromatography, Liquid
Clostridium perfringens
Clostridium perfringens - genetics
Clostridium perfringens - growth & development
Clostridium perfringens - metabolism
Dogs
E coli
epsilon toxin
Escherichia coli - genetics
Food contamination & poisoning
Gangrene
Immunoassay
Laboratories
Mass spectrometry
Mass spectroscopy
Peptides
Peptides - analysis
Peptides - genetics
PRM
protein toxin
Proteins
Proteomics
Quadrupoles
Recombinant Proteins - analysis
Scientific imaging
Spectroscopy
Tandem Mass Spectrometry
Target acquisition
Toxins
Warfare
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Summary:Targeted proteomics recently proved to be a technique for the detection and absolute quantification of proteins not easily accessible to classical bottom-up approaches. Due to this, it has been considered as a high fidelity tool to detect potential warfare agents in wide spread kinds of biological and environmental matrices. toxins are considered to be potential biological weapons, especially the epsilon toxin which belongs to a group of the most powerful bacterial toxins. Here, the development of a target mass spectrometry method for the detection of protein toxins (alpha, beta, beta2, epsilon, iota) is described. A high-resolution mass spectrometer with a quadrupole-Orbitrap system operating in target acquisition mode (parallel reaction monitoring) was utilized. Because of the lack of commercial protein toxin standards recombinant toxins were prepared within . The analysis was performed using proteotypic peptides as the target compounds together with their isotopically labeled synthetic analogues as internal standards. Calibration curves were calculated for each peptide in concentrations ranging from 0.635 to 1101 fmol/μL. Limits of detection and quantification were determined for each peptide in blank matrices.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins11030177