A Monoclonal-Monoclonal Antibody Based Capture ELISA for Abrin

• Published in: Toxins Vol. 9; no. 10; p. 328
• Main Authors: Tam, Christina C, Cheng, Luisa W, He, Xiaohua, Merrill, Paul, Hodge, David, Stanker, Larry H
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 18.10.2017; MDPI
• Subjects: abrin; abrus precatorius; Chains; Contamination; Cross-reactivity; ELISA; Enzyme-linked immunosorbent assay; Immunoglobulins; Monoclonal antibodies; Proteins; Reagents; ribosome-inactivating protein; Sensors; Toxicity; Toxins; abrin; abrus precatorius; ribosome-inactivating protein; ELISA; monoclonal antibodies
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins9100328

Abrin, one of the most highly potent toxins in the world, is derived from the plant, . Because of its high toxicity, it poses potential bioterror risks. Therefore, a need exists for new reagents and technologies that would be able to rapidly detect abrin contamination as well as lead to new therapeutics. We report here a group of abrin-specific monoclonal antibodies (mAbs) that recognize abrin A-chain, intact A-B chain toxin, and agglutinin by Western blot. Additionally, these mAbs were evaluated for their ability to serve as capture antibodies for a sandwich (capture) ELISA. All possible capture-detector pairs were evaluated and the best antibody pair identified and optimized for a capture ELISA. The capture ELISA based on this capture-detector mAb pair had a limit of detection (L.O.D) of ≈1 ng/mL measured using three independent experiments. The assay did not reveal any false positives with extracts containing other potential ribosome-inactivating proteins (RIPs). Thus, this new capture ELISA uses mAbs for both capture and detection; has no cross-reactivity against other plant RIPs; and has a sensitivity comparable to other reported capture ELISAs using polyclonal antibodies as either capture or detector.