ArticleThe FEBS journal2026
SARS-CoV-2 nucleocapsid protein variants have differential RNA chaperone activity.
Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors.
Funding
Abstract
The single-stranded RNA genome of the SARS-CoV-2 virus is characterized by a complex secondary structure formed by patches of intramolecular RNA double-strands. Here, we show that the nucleocapsid (N) protein is not only the specific viral RNA packaging protein, but also acts as an RNA chaperone, facilitating RNA folding. RNA chaperones are classified by their non-specific RNA binding and the presence of intrinsically disordered regions (IDRs). N possesses three IDRs, separated by the structured RNA-binding domain (RBD) and the C-terminal domain (CTD). Our study identifies the amino acids 46-364 (RBD-IDR2-CTD) as crucial for chaperone activity, with flanking IDRs either enhancing or repressing this function, revealing the essential role of IDRs for the chaperone mechanism. Furthermore, a comparison between the Wuhan and Omicron BA.5 variant N shows reduced chaperone activity of the Omicron N protein. However, mimicking the cellular phosphorylation state of Omicron N restored its chaperone activity to the levels of the Wuhan variant. Our results identify N-phosphorylation as a regulatory mechanism of chaperone activity, emphasizing an intricate regulatory role of post-translational modifications in the dynamics of viral RNA secondary structure establishment. The regulation of RNA chaperoning could serve as a potential therapeutic target for future treatment of RNA viruses.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.