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Toxins 2016, 8(3), 64; doi:10.3390/toxins8030064

Isolation of Anti-Ricin Protective Antibodies Exhibiting High Affinity from Immunized Non-Human Primates

1
Department of Biochemistry and Molecular Genetics, Israel Institute for Biological Research, Ness-Ziona 76100, Israel
2
Department of Biotechnology, Israel Institute for Biological Research, Ness-Ziona 76100, Israel
*
Author to whom correspondence should be addressed.
Academic Editor: Daniel Gillet
Received: 6 January 2016 / Revised: 25 February 2016 / Accepted: 26 February 2016 / Published: 3 March 2016
(This article belongs to the Section Plant Toxins)
View Full-Text   |   Download PDF [951 KB, uploaded 3 March 2016]   |  

Abstract

Ricin, derived from the castor bean plant Ricinus communis, is one of the most potent and lethal toxins known, against which there is no available antidote. To date, the use of neutralizing antibodies is the most promising post-exposure treatment for ricin intoxication. The aim of this study was to isolate high affinity anti-ricin antibodies that possess potent toxin-neutralization capabilities. Two non-human primates were immunized with either a ricin-holotoxin- or subunit-based vaccine, to ensure the elicitation of diverse high affinity antibodies. By using a comprehensive set of primers, immune scFv phage-displayed libraries were constructed and panned. A panel of 10 antibodies (five directed against the A subunit of ricin and five against the B subunit) was isolated and reformatted into a full-length chimeric IgG. All of these antibodies were found to neutralize ricin in vitro, and several conferred full protection to ricin-intoxicated mice when given six hours after exposure. Six antibodies were found to possess exceptionally high affinity toward the toxin, with KD values below pM (koff < 1 × 10−7 s−1) that were well correlated with their ability to neutralize ricin. These antibodies, alone or in combination, could be used for the development of a highly-effective therapeutic preparation for post-exposure treatment of ricin intoxication. View Full-Text
Keywords: ricin; antibody; neutralization; affinity; immunization; non-human primates ricin; antibody; neutralization; affinity; immunization; non-human primates
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Noy-Porat, T.; Rosenfeld, R.; Ariel, N.; Epstein, E.; Alcalay, R.; Zvi, A.; Kronman, C.; Ordentlich, A.; Mazor, O. Isolation of Anti-Ricin Protective Antibodies Exhibiting High Affinity from Immunized Non-Human Primates. Toxins 2016, 8, 64.

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