Functional magnetic nanoparticle–based affinity probe for MALDI mass spectrometric detection of ricin B

Kandasamy, Karthikeyan; Selvaprakash, Karuppuchamy; Chen, Yu-Chie

doi:10.1007/s00604-021-04991-y

Cited by 6 publications

(2 citation statements)

References 43 publications

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“…We then turned to glycoproteins instead of simple carbohydrates to better mimic the in vivo binding of the toxins because the B-chain is known to bind to glycoproteins with terminal galactose on the cell surfaces, and other laboratories have shown success with using glycoproteins to bind to ricin. , Ovalbumin, fetuin, asialofetuin, and α1-acid glycoprotein (Table ) were biotinylated and tested as ligands coupled to streptavidin beads for their ability to pull down abrin. We measured the extraction of the toxins by observing the level of depurination of the RNA14A substrate.…”

Section: Resultsmentioning

confidence: 99%

“…Because ricin and abrin have similar mechanisms of action and cause similar symptoms, an assay that could detect and differentiate between both would be beneficial for public safety. Furthermore, an assay that measures both A-chain enzymatic activity and the ability of the B-chain to bind galactose on cell membrane − glycoproteins would give a more comprehensive idea of the biological threat. Both of these attributes would allow public health laboratories to efficiently test for both toxins to gain a more complete understanding of the threat.…”

Section: Introductionmentioning

confidence: 99%

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Mass Spectrometric Detection and Differentiation of Enzymatically Active Abrin and Ricin Combined with a Novel Affinity Enrichment Technique

Drinkard,

Barr,

Kalb

2024

Chem. Res. Toxicol.

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Abrin and ricin are toxic proteins produced by plants. Both proteins are composed of two subunits, an A-chain and a Bchain. The A-chain is responsible for the enzymatic activity, which causes toxicity. The B-chain binds to glycoproteins on the cell surface to direct the A-chain to its target. Both toxins depurinate 28S rRNA, making it impossible to differentiate these toxins based on only their enzymatic activity. We developed an analytical workflow for both ricin and abrin using a single method and sample. We have developed a novel affinity enrichment technique based on the ability of the B-chain to bind a glycoprotein, asialofetuin. After the toxin is extracted with asialofetuin-coated magnetic beads, an RNA substrate is added. Then, depurination is detected by a benchtop matrixassisted laser desorption/ionization time-of-flight (MALDI TOF) mass spectrometer to determine the presence or absence of an active toxin. Next, the beads are subjected to tryptic digest. Toxin fingerprinting is done on a benchtop MALDI-TOF MS. We validated the assay through sensitivity and specificity studies and determined the limit of detection for each toxin as nanogram level for enzymatic activity and μg level for toxin fingerprinting. We examined potential cross-reactivity from proteins that are near neighbors of the toxins and examined potential false results in the presence of white powders.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Mass Spectrometric Detection and Differentiation of Enzymatically Active Abrin and Ricin Combined with a Novel Affinity Enrichment Technique

Drinkard,

Barr,

Kalb

2024

Chem. Res. Toxicol.

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2021–2022

Harvey

2024

Mass Spectrometry Reviews

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The use of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry for the analysis of carbohydrates and glycoconjugates is a well‐established technique and this review is the 12th update of the original article published in 1999 and brings coverage of the literature to the end of 2022. As with previous review, this review also includes a few papers that describe methods appropriate to analysis by MALDI, such as sample preparation, even though the ionization method is not MALDI. The review follows the same format as previous reviews. It is divided into three sections: (1) general aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, fragmentation, quantification and the use of computer software for structural identification. (2) Applications to various structural types such as oligo‐ and polysaccharides, glycoproteins, glycolipids, glycosides and biopharmaceuticals, and (3) other general areas such as medicine, industrial processes, natural products and glycan synthesis where MALDI is extensively used. Much of the material relating to applications is presented in tabular form. MALDI is still an ideal technique for carbohydrate analysis, particularly in its ability to produce single ions from each analyte and advancements in the technique and range of applications show little sign of diminishing.

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Magnetic relaxation switch and fluorescence dual-mode biosensor for rapid and sensitive detection of ricin B toxin in edible oil and tap water

Wang

Li²,

Ren³

et al. 2022

Analytica Chimica Acta

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Functional magnetic nanoparticle–based affinity probe for MALDI mass spectrometric detection of ricin B

Cited by 6 publications

References 43 publications

Mass Spectrometric Detection and Differentiation of Enzymatically Active Abrin and Ricin Combined with a Novel Affinity Enrichment Technique

Mass Spectrometric Detection and Differentiation of Enzymatically Active Abrin and Ricin Combined with a Novel Affinity Enrichment Technique

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2021–2022

Magnetic relaxation switch and fluorescence dual-mode biosensor for rapid and sensitive detection of ricin B toxin in edible oil and tap water

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