Mass spectrometry in biodefense
Identifieur interne : 001006 ( Istex/Checkpoint ); précédent : 001005; suivant : 001007Mass spectrometry in biodefense
Auteurs : Plamen A. Demirev [États-Unis] ; Catherine Fenselau [États-Unis]Source :
- Journal of Mass Spectrometry [ 1076-5174 ] ; 2008-11.
English descriptors
- Teeft :
- Aerosol mass spectrometry, Algorithm, American chemical society, American society, Analytica chimica acta, Analytical, Analytical biochemistry, Analytical chemistry, Anthracis, Anthracis spores, Assay, Baar, Bacillus, Bacillus anthracis, Bacillus species, Bacillus spores, Barr, Biodefense, Biodefense applications, Bioinformatics, Biological weapons, Biomarker, Biomarkers, Biotoxins, Bont, Botulinum, Botulinum neurotoxin, Botulinum toxins type, Capillary electrophoresis, Cereus, Coat protein, Coli, Copyright, Database, Demirev, Desorption, Detection, Digestion, Direct analysis, Electrospray, Electrospray mass spectrometry, Environmental microbiology, Escherichia coli, Fenselau, Francisella tularensis, Genetic evaluation, Genome, Hulst, Individual microorganisms, Intact microorganisms, Intact protein, Intact proteins, Intact spores, International journal, Ionization, John wiley sons, Johns hopkins, Laser, Laser mass spectrometry, Maldi, Maldi spectra, Mass accuracy, Mass spectra, Mass spectrom, Mass spectrometer, Mass spectrometry, Mass spectrometry reviews, Matrix, Microbial, Microbial mixtures, Microbiological, Microbiological methods, Microbiology, Microorganism, National academy, Pathogen, Peptide, Physics laboratory, Precursor, Protein, Protein biomarkers, Protein toxins, Proteolytic peptides, Proteome, Proteome database, Proteomic, Proteomic analysis, Proteomics, Proteomics approaches, Rapid characterization, Rapid communications, Real time, Relative intensity, Ricin, Sample preparation, Sasp, Sasps, Spectrom, Spectrometer, Spectrometry, Spore, Staphylococcal enterotoxin, Tandem, Tandem mass spectrometry, Tandem spectra, Time frame, Toxin, Tryptic, Tryptic peptides, Tularensis, Yersinia pestis.
Abstract
Potential agents for biological attacks include both microorganisms and toxins. In mass spectrometry (MS), rapid identification of potential bioagents is achieved by detecting the masses of unique biomarkers, correlated to each agent. Currently, proteins are the most reliable biomarkers for detection and characterization of both microorganisms and toxins, and MS‐based proteomics is particularly well suited for biodefense applications. Confident identification of an organism can be achieved by top‐down proteomics following identification of individual protein biomarkers from their tandem mass spectra. In bottom‐up proteomics, rapid digestion of intact protein biomarkers is again followed by MS/MS to provide unambiguous bioagent identification and characterization. Bioinformatics obviates the need for culturing and rigorous control of experimental variables to create and use MS fingerprint libraries for various classes of bioweapons. For specific applications, MS methods, instruments and algorithms have also been developed for identification based on biomarkers other than proteins and peptides. Copyright © 2008 John Wiley & Sons, Ltd.
Url:
DOI: 10.1002/jms.1474
Affiliations:
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scheme="Teeft" xml:lang="en"><term>Aerosol mass spectrometry</term><term>Algorithm</term><term>American chemical society</term><term>American society</term><term>Analytica chimica acta</term><term>Analytical</term><term>Analytical biochemistry</term><term>Analytical chemistry</term><term>Anthracis</term><term>Anthracis spores</term><term>Assay</term><term>Baar</term><term>Bacillus</term><term>Bacillus anthracis</term><term>Bacillus species</term><term>Bacillus spores</term><term>Barr</term><term>Biodefense</term><term>Biodefense applications</term><term>Bioinformatics</term><term>Biological weapons</term><term>Biomarker</term><term>Biomarkers</term><term>Biotoxins</term><term>Bont</term><term>Botulinum</term><term>Botulinum neurotoxin</term><term>Botulinum toxins type</term><term>Capillary electrophoresis</term><term>Cereus</term><term>Coat protein</term><term>Coli</term><term>Copyright</term><term>Database</term><term>Demirev</term><term>Desorption</term><term>Detection</term><term>Digestion</term><term>Direct analysis</term><term>Electrospray</term><term>Electrospray mass spectrometry</term><term>Environmental microbiology</term><term>Escherichia coli</term><term>Fenselau</term><term>Francisella tularensis</term><term>Genetic evaluation</term><term>Genome</term><term>Hulst</term><term>Individual microorganisms</term><term>Intact microorganisms</term><term>Intact protein</term><term>Intact proteins</term><term>Intact spores</term><term>International journal</term><term>Ionization</term><term>John wiley sons</term><term>Johns hopkins</term><term>Laser</term><term>Laser mass spectrometry</term><term>Maldi</term><term>Maldi spectra</term><term>Mass accuracy</term><term>Mass spectra</term><term>Mass spectrom</term><term>Mass spectrometer</term><term>Mass spectrometry</term><term>Mass spectrometry reviews</term><term>Matrix</term><term>Microbial</term><term>Microbial mixtures</term><term>Microbiological</term><term>Microbiological methods</term><term>Microbiology</term><term>Microorganism</term><term>National academy</term><term>Pathogen</term><term>Peptide</term><term>Physics laboratory</term><term>Precursor</term><term>Protein</term><term>Protein biomarkers</term><term>Protein toxins</term><term>Proteolytic peptides</term><term>Proteome</term><term>Proteome database</term><term>Proteomic</term><term>Proteomic analysis</term><term>Proteomics</term><term>Proteomics approaches</term><term>Rapid characterization</term><term>Rapid communications</term><term>Real time</term><term>Relative intensity</term><term>Ricin</term><term>Sample preparation</term><term>Sasp</term><term>Sasps</term><term>Spectrom</term><term>Spectrometer</term><term>Spectrometry</term><term>Spore</term><term>Staphylococcal enterotoxin</term><term>Tandem</term><term>Tandem mass spectrometry</term><term>Tandem spectra</term><term>Time frame</term><term>Toxin</term><term>Tryptic</term><term>Tryptic peptides</term><term>Tularensis</term><term>Yersinia pestis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Potential agents for biological attacks include both microorganisms and toxins. In mass spectrometry (MS), rapid identification of potential bioagents is achieved by detecting the masses of unique biomarkers, correlated to each agent. Currently, proteins are the most reliable biomarkers for detection and characterization of both microorganisms and toxins, and MS‐based proteomics is particularly well suited for biodefense applications. Confident identification of an organism can be achieved by top‐down proteomics following identification of individual protein biomarkers from their tandem mass spectra. In bottom‐up proteomics, rapid digestion of intact protein biomarkers is again followed by MS/MS to provide unambiguous bioagent identification and characterization. Bioinformatics obviates the need for culturing and rigorous control of experimental variables to create and use MS fingerprint libraries for various classes of bioweapons. For specific applications, MS methods, instruments and algorithms have also been developed for identification based on biomarkers other than proteins and peptides. Copyright © 2008 John Wiley & Sons, Ltd.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Maryland</li></region><settlement><li>College Park (Maryland)</li></settlement><orgName><li>Université du Maryland</li></orgName></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Demirev, Plamen A" sort="Demirev, Plamen A" uniqKey="Demirev P" first="Plamen A." last="Demirev">Plamen A. Demirev</name></region><name sortKey="Demirev, Plamen A" sort="Demirev, Plamen A" uniqKey="Demirev P" first="Plamen A." last="Demirev">Plamen A. Demirev</name><name sortKey="Demirev, Plamen A" sort="Demirev, Plamen A" uniqKey="Demirev P" first="Plamen A." last="Demirev">Plamen A. Demirev</name><name sortKey="Fenselau, Catherine" sort="Fenselau, Catherine" uniqKey="Fenselau C" first="Catherine" last="Fenselau">Catherine Fenselau</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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