Journal
MOLECULAR CELL
Volume 80, Issue 6, Pages 1078-+Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2020.11.041
Keywords
-
Categories
Funding
- NIH [R01GM081506, 2139, T32 CA 9156-43, F32GM136164, R01HG005998, U54HL117798, R01GM071966, R35 GM122532]
- HHMI faculty Scholar Award
- L'OREAL USA for Women in Science Fellowship
- HHS grant [HHSN272201000054C]
- Simons Foundation grant [395506]
- Ruth L. Kirschstein Postdoctoral Fellowship [F32 GM128330]
- National Institute of Allergy and Infectious Diseases grants [1U19AI142759]
- North Carolina Policy Collaboratory at University of North Carolina at Chapel Hill
- North Carolina Coronavirus Relief Fund
Ask authors/readers for more resources
We report that the SARS-CoV-2 nucleocapsid protein (N-protein) undergoes liquid-liquid phase separation (LLPS) with viral RNA. N-protein condenses with specific RNA genomic elements under physiological buffer conditions and condensation is enhanced at human body temperatures (33 degrees C and 37 degrees C) and reduced at room temperature (22 degrees C). RNA sequence and structure in specific genomic regions regulate N-protein condensation while other genomic regions promote condensate dissolution, potentially preventing aggregation of the large genome. At low concentrations, N-protein preferentially crosslinks to specific regions characterized by single-stranded RNA flanked by structured elements and these features specify the location, number, and strength of N-protein binding sites (valency). Liquid-like N-protein condensates form in mammalian cells in a concentration-dependent manner and can be altered by small molecules. Condensation of N-protein is RNA sequence and structure specific, sensitive to human body temperature, and manipulatable with small molecules, and therefore presents a screenable process for identifying antiviral compounds effective against SARS-CoV-2.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available