Ricin detection: tracking active toxin

William P Bozza; William H Tolleson; Leslie A Rivera Rosado; Baolin Zhang

doi:10.1016/j.biotechadv.2014.11.012

Ricin detection: tracking active toxin

Biotechnol Adv. 2015 Jan-Feb;33(1):117-123. doi: 10.1016/j.biotechadv.2014.11.012. Epub 2014 Dec 4.

Authors

William P Bozza¹, William H Tolleson², Leslie A Rivera Rosado³, Baolin Zhang⁴

Affiliations

¹ Division of Therapeutic Proteins, Office of Biotechnology Products, Center for Drug Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA.
² Division of Biochemical Toxicology, National Center for Toxicological Research, Food and Drug Administration, Jefferson, AR 72079, USA.
³ Division of Therapeutic Proteins, Office of Biotechnology Products, Center for Drug Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA; United States Public Health Service Commissioned Corps, Rockville, MD, USA.
⁴ Division of Therapeutic Proteins, Office of Biotechnology Products, Center for Drug Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892, USA. Electronic address: Baolin.zhang@fda.hhs.gov.

PMID: 25481398
DOI: 10.1016/j.biotechadv.2014.11.012

Abstract

Ricin is a plant toxin with high bioterrorism potential due to its natural abundance and potency in inducing cell death. Early detection of the active toxin is essential for developing appropriate countermeasures. Here we review concepts for designing ricin detection methods, including mechanism of action of the toxin, advantages and disadvantages of current detection assays, and perspectives on the future development of rapid and reliable methods for detecting ricin in environmental samples.

Keywords: Bioterrorism; Detection methods; Plant toxins; Ricin.

Published by Elsevier Inc.

Publication types

Research Support, U.S. Gov't, P.H.S.
Review

MeSH terms

Biological Assay / methods*
Bioterrorism
Enzyme-Linked Immunosorbent Assay
Protein Conformation
Ricin / isolation & purification*

Substances

Ricin