Engineered recombinant human paraoxonase 1 (rHuPON1) purified from Escherichia coli protects against organophosphate poisoning.

Proceedings of the National Academy of Sciences of the United States of America
R C StevensC E Furlong

Abstract

The high-density lipoprotein-associated enzyme paraoxonase 1 (PON1) hydrolyzes lactones, aromatic esters, and neurotoxic organophosphorus (OP) compounds, including insecticide metabolites and nerve agents. Experiments with mice lacking PON1 (PON1(-/-) mice) have established that plasma PON1 protects against chlorpyrifos/chlorpyrifos-oxon and diazinon/diazoxon (DZO) exposure but does not protect against parathion/paraoxon or nerve agents. The catalytic efficiency of PON1 determines whether or not it will protect against a given OP exposure. Expression of active recombinant human PON1 (rHuPON1) in Escherichia coli provides a system in which PON1 can be engineered to achieve a catalytic efficiency sufficient to protect against or treat specific OP exposures. Here, we describe the generation of highly purified engineered rHuPON1(K192) that protects against DZO exposure when injected into PON1(-/-) mice. The injected rHuPON1 is nontoxic, persists in serum for at least 2 days after injection, and provides protection against DZO exposures of at least three times the median lethal dose value.

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Citations

Jul 3, 2013·Chemico-biological Interactions·Florian NachonPatrick Masson
Aug 30, 2008·Proceedings of the National Academy of Sciences of the United States of America·Janice E Chambers
Aug 27, 2011·Antioxidants & Redox Signaling·Zhi-Gang SheDe-Pei Liu
Jun 16, 2011·Toxicological Sciences : an Official Journal of the Society of Toxicology·Toby B ColeClement E Furlong
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Nov 12, 2014·TheScientificWorldJournal·Priyanka BajajAbhay H Pande
Dec 25, 2012·Toxicology·Judit MarsillachClement E Furlong
Mar 20, 2012·Neurotoxicology and Teratology·Toby B ColeClement E Furlong
Feb 4, 2012·Toxicology Letters·Manojkumar ValiyaveettilMadhusoodana P Nambiar
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