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Proteomics. 2017 Jan;17(1-2). doi: 10.1002/pmic.201600357. Epub 2016 Dec 23.

A proteomics assay to detect eight CBRN-relevant toxins in food.

Gilquin B1,2,3,4, Jaquinod M1,2,3, Louwagie M1,2,3, Kieffer-Jaquinod S1,2,3, Kraut A1,2,3, Ferro M1,2,3, Becher F5, Brun V1,2,3.

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Université Grenoble-Alpes, Grenoble, France.
CEA, BIG, Biologie à Grande Echelle, Grenoble, France.
INSERM, U1038, Grenoble, France.
CEA, LETI, Clinatec, Grenoble, France.
CEA, iBiTec-S, Laboratoire d'Etude du Métabolisme des Médicaments, Gif-sur-Yvette, France.


A proteomics assay was set up to analyze food substrates for eight toxins of the CBRN (chemical, biological, radiological and nuclear) threat, namely ricin, Clostridium perfringens epsilon toxin (ETX), Staphylococcus aureus enterotoxins (SEA, SEB and SED), shigatoxins from Shigella dysenteriae and entero-hemorragic Escherichia coli strains (STX1 and STX2) and Campylobacter jejuni cytolethal distending toxin (CDT). The assay developed was based on an antibody-free sample preparation followed by bottom-up LC-MS/MS analysis operated in targeted mode. Highly specific detection and absolute quantification were obtained using isotopically labeled proteins (PSAQ standards) spiked into the food matrix. The sensitivity of the assay for the eight toxins was lower than the oral LD50 which would likely be used in a criminal contamination of food supply. This assay should be useful in monitoring biological threats. In the public-health domain, it opens the way for multiplex investigation of food-borne toxins using targeted LC-MS/MS.


Bioterrorism; Food; Mass spectrometry; Quantification; Technology; Toxin

[Indexed for MEDLINE]

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