On The Origin And Size Of Infectious Prions

Byron Caughey and colleagues also reveal that groups of fewer than six such molecules have essentially no infectivity. Attempts to alleviate symptoms by destabilizing these large protein aggregates might make things worse by producing smaller but more infectious particles. These findings might have implications for the treatment of other afflictions such as Alzheimer's and Parkinson's disease, also characterized by deposition of amyloid fibrils.

In the same issue, the origins of infectious prion 'seeds' in yeast are explored in a paper by Tricia Serio and Prasanna Satpute-Krishnan (pp. 262-265). They demonstrate that the conversion of the yeast protein Sup35 to its prion form does not need to happen during the synthesis of Sup35 -mature and fully functional molecules can readily join a prion seed. This remodelling of mature protein is accompanied by the loss of its activity and therefore causes immediate effects in the cell.

CONTACT:

Byron Caughey (NIAID/NIH Rocky Mountain Laboratories, Hamilton, MT, USA)
E-mail: bcaughey@nih.gov

Tricia R. Serio (Brown University, Providence, RI, USA)
E-mail: Tricia_Serio@Brown.edu

(C) Nature press release.

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