Sequence-independent recognition of the amyloid structural motif by GFP protein family.

Sherry C S Xu, Josephine G LoRicco, Anthony C Bishop, Nathan A James, Welby H Huynh, Scott A McCallum, Nadia R Roan, George I Makhatadze

Proceedings of the National Academy of Sciences of the United States of America 2020 Sep 08

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Cnidarian fluorescent protein (FP) derivatives such as GFP, mCherry, and mEOS2 have been widely used to monitor gene expression and protein localization through biological imaging because they are considered functionally inert. We demonstrate that FPs specifically bind amyloid fibrils formed from many natural peptides and proteins. FPs do not bind other nonamyloid fibrillar structures such as microtubules or actin filaments and do not bind to amorphous aggregates. FPs can also bind small aggregates formed during the lag phase and early elongation phase of fibril formation and can inhibit amyloid fibril formation in a dose-dependent manner. These findings suggest caution should be taken in interpreting FP-fusion protein localization data when amyloid structures may be present. Given the pathological significance of amyloid-related species in some diseases, detection and inhibition of amyloid fibril formation using FPs can provide insights on developing diagnostic tools.

Citation

Sherry C S Xu, Josephine G LoRicco, Anthony C Bishop, Nathan A James, Welby H Huynh, Scott A McCallum, Nadia R Roan, George I Makhatadze. Sequence-independent recognition of the amyloid structural motif by GFP protein family. Proceedings of the National Academy of Sciences of the United States of America. 2020 Sep 08;117(36):22122-22127