Duilio Cascio

Abstract The self-assembly of the Nucleocapsid protein (NCAP) of SARS-CoV-2 is crucial for its function. Computational analysis of the amino acid sequence of NCAP reveals low-complexity domains (LCDs) akin to LCDs in other proteins known to self-assemble as phase separation droplets and amyloid fibrils. Previous reports have described NCAP’s propensity to phase-separate. Here we show that the central LCD of NCAP is capable of both, phase separation and amyloid formation.

Abstract hnRNPA2 is a human ribonucleoprotein (RNP) involved in RNA metabolism. It forms fibrils both under cellular stress and in mutated form in neurodegenerative conditions. Previous work established that the C-terminal low-complexity domain (LCD) of hnRNPA2 fibrillizes under stress, and missense mutations in this domain are found in the disease multisystem proteinopathy (MSP).

Romany Abskharon1,2‡, Paul M. Seidler1,2‡, Michael R. Sawaya1,2, Duilio Cascio1,2, Tianxiao P. Yang1,2, Stephan Philipp3, Christopher Kazu Williams4, Kathy L. Newell5, Bernardino Ghetti5, Michael A. DeTure6, Dennis W. Dickson6, Harry V. Vinters4,7, Philip L. Felgner8, Rie Nakajima9, Charles G. Glabe3 and David S.