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Biological Chemistry

Prion Aggregate Size Affects Transmissibility

The size of prion aggregates affects their ability to induce further aggregation and cause protein-misfolding diseases

by Stuart A. Borman
November 1, 2010 | A version of this story appeared in Volume 88, Issue 44

In work that could aid understanding of protein-misfolding diseases, researchers have found that the size of prion aggregates affects their ability to induce further aggregation and cause illness (Science 2010, 330, 680). The prion hypothesis proposes that aggregates of misfolded infectious prion protein cause conditions such as mad cow disease in cattle and Creutzfeldt-Jakob disease in people by acting as seeds for the transformation of normally folded prion protein into more of the misfolded infectious form, which then tends to spread from cell to cell. Experiments and modeling on how prion aggregates proliferate in yeast now show that aggregate size has a critical influence on prion transmissibility. Suzanne S. Sindi, Tricia R. Serio, and coworkers at Brown University observed that small aggregates spread readily, whereas large ones are much less prone to do so. The findings suggest that prion-disease treatments that reduce the size of prion aggregates in people might promote the spread of prions inadvertently by boosting levels of highly transmissible small aggregates. Size-dependent transmissibility may also apply to other protein-misfolding disorders, such as Parkinson’s, Alzheimer’s, and Huntington’s, the researchers say.


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