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PUBLIC RELEASE DATE:
15-Aug-2008

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Contact: Nick Zagorski
nzagorski@asbmb.org
301-634-7366
American Society for Biochemistry and Molecular Biology
@asbmb

Potatoes may hold key to Alzheimer's treatment

Article appears in August 15 JBC

IMAGE: Necrotic ringspots on a potato tuber (cultivar Nicola) due to Potato virus Y infection.

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A virus that commonly infects potatoes bears a striking resemblance to one of the key proteins implicated in Alzheimer's disease (AD), and researchers have used that to develop antibodies that may slow or prevent the onset of AD.

Studies in mice have demonstrated that vaccinations with the amyloid beta protein (believed to be a major AD contributor) to produce A antibodies can slow disease progression and improve cognitive function, possibly by promoting the destruction of amyloid plaques. Some early human trials have likewise been promising, but had to be halted due to the risk of autoimmune encephalitis.

One way to make Alzheimer's vaccinations safer would be to use a closely-related, but not human, protein as the vaccine, much like cowpox virus is used for smallpox immunizations.

In the August 15 Journal of Biological Chemistry, Robert Friedland and colleagues used this concept on an amyloid-like protein found in potato virus (PVY). They injected PVY into mice followed by monthly boosters for four months. The researchers found that the mice produced strong levels of antibodies that could attach to amyloid beta protein both in both solution and in tissue samples of Alzheimer's patients. And although the levels were lower, mice also developed A antibodies if given injections of PVY-infected potato leaf as opposed to purified PVY.

Friedland and colleagues note that potato virus is a fairly common infection that poses no risk to humans (many people have probably eaten PVY infected potatoes). While tests of PVY antibodies will ultimately determine how useful they can be, they may be a promising lead to treating this debilitating disease.

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From the JBC article: "Antibodies to Potato Virus Y Bind the Amyloid Beta Peptide" by Robert P. Friedland, Jonathan M. Tedesco, Andrea Wilson, Craig Atwood, Mark Smith, George Perry and Michael Zagorski.

Article Link: http://www.jbc.org/cgi/content/full/283/33/22550

Corresponding Author: Robert P. Friedland, Department of Neurology, Case Western Reserve University School of Medicine, Clevelland, OH; Tel: 216-368-1913, Email: Robert.friedland@case.edu

The American Society for Biochemistry and Molecular Biology is a nonprofit scientific and educational organization with over 11,900 members in the United States and internationally. Most members teach and conduct research at colleges and universities. Others conduct research in various government laboratories, nonprofit research institutions and industry. The Society's student members attend undergraduate or graduate institutions.

Founded in 1906, the Society is based in Bethesda, Maryland, on the campus of the Federation of American Societies for Experimental Biology. The Society's purpose is to advance the science of biochemistry and molecular biology through publication of the Journal of Biological Chemistry, the Journal of Lipid Research, and Molecular and Cellular Proteomics, organization of scientific meetings, advocacy for funding of basic research and education, support of science education at all levels, and promoting the diversity of individuals entering the scientific work force.

For more information about ASBMB, see the Society's Web site at www.asbmb.org.



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