Dynamics of oligomer and amyloid fibril formation by yeast prion Sup35 observed by high-speed atomic force microscopy

Research Highlight

How prion proteins stack up



An imaging study of prion formation in yeast could help explain how misfolded proteins aggregate in human diseases such as Alzheimer’s.

Misfolded proteins known as prions can cause fatal infections in people and animals and are associated with various neurodegenerative diseases.

A team from Japan used advanced microscopy techniques developed at Kanazawa University to visualize the process by which individual prion proteins in yeast combine to form highly ordered fibrils — all at high resolution and in real time.

The researchers found that longer incubation times were needed for individual prions to fashion themselves into fibrils, with their orderly stacked-sheet arrangement, instead of into messier, clump-like structures called oligomers.

Fibril building occurred through gradual incorporation of individual prions, not through the addition of oligomers, which are kept away from fibrils through the repulsive forces. Blocking this fibril-elongation process could help treat a range of prion-associated diseases.

Supported content

  1. PNAS 117, 7831–7836 (2020). doi: 10.1073/pnas.1916452117
Institutions Share
Kanazawa University (KU), Japan 0.67
Tokyo Institute of Technology (Tokyo Tech), Japan 0.22
Nagoya University, Japan 0.06
Exploratory Research Center on Life and Living Systems (ExCELLS), NINS, Japan 0.06