New treatment could combat deadly chemical agents
An
enzyme treatment which could neutralise the effects of lethal chemicals
responsible for the deaths of hundreds of thousands of people across the world
has been developed by experts at the University of Sheffield. Organophosphorus
agents (OP) are used as pesticides in developing countries and acute poisoning
is common because of insufficient control, poor storage, ready availability,
and inadequate education amongst farmers.
It is
estimated about 200,000 people die each year across the world from OP
poisoning, through occupational exposure, unintentional use and misuse, mostly
in developing countries like India, Pakistan, and Sri Lanka and through
deliberate terrorist activities.
OPs
include compounds like Tabun, which was developed in 1936 by German scientists
during World War II, Sarin, Soman, Cyclosarin, VX, and VR.
Using a
modified human enzyme, scientist Professor Mike Blackburn from the University
of Sheffield's Department of Molecular Biology and Biotechnology collaborated
in a consultancy role with Professor Alexander Gabibov of the Shemyakin-Ovchinnikov
Institute, Moscow, and Professor Patrick Masson of the Département de
Toxicologie, Centre de Recherches du Service de Santé des Armées, to create a
"bioscavenger" which was found to protect mice against the nerve
agent VR and showed no lasting effects.
In
studies performed at the Institute of Bioorganic Chemistry in Pushchino,
Russia, a total of eight mice were treated with the new enzyme after being
subjected to enough of the VR agent to kill several of the animals -- about 63
mg -- and all survived.
Professor
Blackburn said: "This current publication describes a novel method to
generate a bioscavenger for the Russian VR organophosphorus agent with the key
property of being long-acting in the bloodstream.
"That
has been achieved by a combination of chemical surface modification
(polysialylation) and biotechnology of production (through the use of an in
vitro CHO-based expression system employing genes encoding
butyrylcholinesterase and a proline-rich peptide under special promoter
control).
Source: University
of Sheffield
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