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• W2014322428 abstract "Anthrax infections progress at a rapid pace, making rapid detection methods of utmost importance. MALDI-MS proteomics methods focused on Bacillus anthracis detection have targeted chromosomally encoded proteins, which are highly conserved between closely related species, hindering species identification. Presented here is an AP-MALDI-MS method targeting plasmid-borne proteins from Bacillus spores for species-level identification. A bioinformatics analysis revealed that 60.3% and 75.4% of tryptic peptides from plasmid-borne proteins of B. anthracis and B. thuringiensis were species-specific, respectively. Reported here is a method in which plasmid-borne delta-endotoxins were extracted directly from B. thuringiensis spores in 100 mM KOH. The pH was then adjusted to 8 and a 5-min trypsin digestion was performed on the extracted proteins. The resulting tryptic peptides were analyzed by AP-MALDI-MS/MS, which produced a definitive identification the B. thuringiensis species-specific Cry1Ab protein with a MASCOT score of 278 and expect value of 7.5 x 10(-23). This method has demonstrated the detection and identification of B. thuringiensis spores at the species level following a 5-min trypsin digestion. The challenges in applying a similar approach to the detection of plasmid-borne protein toxins from B. anthracis are also discussed." @default.
• W2014322428 created "2016-06-24" @default.
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• W2014322428 creator A5066886135 @default.
• W2014322428 date "2010-06-01" @default.
• W2014322428 modified "2023-10-10" @default.
• W2014322428 title "Targeted proteomics approach to species-level identification of <i>Bacillus thuringiensis</i> spores by AP-MALDI-MS" @default.
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• W2014322428 doi "https://doi.org/10.1016/j.jasms.2010.01.032" @default.
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