Bacteriophage-produced enzyme destroys anthraz bacteria. (Studies in Humans Needed).
An anthrax-specific bacteriophage produces a protein--a lysin--that kills anthrax bacteria by destroying their cell walls from the outside, the researchers said.
A letter by Raymond Schuch, Ph.D., Daniel Nelson, Ph.D., and Vincent A. Fischetti, Ph.D., to Nature details the findings, which identified the enzyme PlyG as the jump-starter that causes bacteriophages specific to Bacillus anthracis to rupture and destroy the bacteria (Nature 418:884-89, 2002).
Better yet, the anthrax bacteria seem unable to develop resistance to this external attack, they noted.
The investigators explained that "lysins are highly evolved enzymes, modified and improved for high activity and specificity over millennia. ... Lysins are already one of the most ubiquitous and successful antimicrobial agents on Earth."
The PlyG lysin has treatment value, too, the investigators said. Approximately 70% (13 of 19) of mice infected with Bacillus cereus (a close relative of anthrax used for lab work) survived when given PlyG 15 minutes after infection.
Although FDA approval is probably 1-2 years away, the investigators are working toward the use of the enzyme to treat anthrax in humans. More animal studies are in progress, to be followed by tests for toxicity in humans.
The idea is to use the enzyme as an intravenous intervention as soon as possible after exposure to anthrax, in conjunction with an antitoxin and antibiotics, Dr. Schuch said in an interview.
The specificity of the bacteriophage means essentially no adverse side effects or damage to other cellular structures, he added.
In an accompanying editorial, Dr. M.J. Rosovitz and Dr. Stephen H. Leppla of the National Institute of Allergy and Infectious Diseases, Bethesda, Md., wrote that the PlyG enzyme may help detect anthrax as well as destroy it.
The adenosine triphosphate released by the degrading anthrax contributes to light visible on a light meter, they noted (Nature 418:825-26, 2002).
The research is sponsored in part by the Defense Advanced Research Projects Agency, the central research and development arm of the United States Department of Defense.
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|Publication:||OB GYN News|
|Date:||Oct 15, 2002|
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