Unknown

Dataset Information

0

Assembly of SARS-CoV-2 ribonucleosomes by truncated N variant of the nucleocapsid protein.


ABSTRACT: The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) compacts the RNA genome into viral ribonucleoprotein (vRNP) complexes within virions. Assembly of vRNPs is inhibited by phosphorylation of the N protein serine/arginine (SR) region. Several SARS-CoV-2 variants of concern carry N protein mutations that reduce phosphorylation and enhance the efficiency of viral packaging. Variants of the dominant B.1.1 viral lineage also encode a truncated N protein, termed N or Δ(1-209), that mediates genome packaging despite lacking the N-terminal RNA-binding domain and SR region. Here, we use mass photometry and negative stain electron microscopy to show that purified Δ(1-209) and viral RNA assemble into vRNPs that are remarkably similar in size and shape to those formed with full-length N protein. We show that assembly of Δ(1-209) vRNPs requires the leucine-rich helix of the central disordered region and that this helix promotes N protein oligomerization. We also find that fusion of a phosphomimetic SR region to Δ(1-209) inhibits RNA binding and vRNP assembly. Our results provide new insights into the mechanisms by which RNA binding promotes N protein self-association and vRNP assembly, and how this process is modulated by phosphorylation.

SUBMITTER: Adly AN 

PROVIDER: S-EPMC10665939 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature

altmetric image

Publications

Assembly of SARS-CoV-2 ribonucleosomes by truncated N<sup>∗</sup> variant of the nucleocapsid protein.

Adly Armin N AN   Bi Maxine M   Carlson Christopher R CR   Syed Abdullah M AM   Ciling Alison A   Doudna Jennifer A JA   Cheng Yifan Y   Morgan David O DO  

The Journal of biological chemistry 20231019 12


The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) compacts the RNA genome into viral ribonucleoprotein (vRNP) complexes within virions. Assembly of vRNPs is inhibited by phosphorylation of the N protein serine/arginine (SR) region. Several SARS-CoV-2 variants of concern carry N protein mutations that reduce phosphorylation and enhance the efficiency of viral packaging. Variants of the dominant B.1.1 viral lineage also encode a truncated N protein, terme  ...[more]

Similar Datasets

| S-EPMC11194069 | biostudies-literature
| S-EPMC10200704 | biostudies-literature
| S-EPMC9235412 | biostudies-literature
| S-EPMC10690241 | biostudies-literature
| S-EPMC8845419 | biostudies-literature
| S-EPMC7263487 | biostudies-literature
| S-EPMC7405475 | biostudies-literature
| S-EPMC9328007 | biostudies-literature
| EMPIAR-10891 | biostudies-other
2024-09-16 | E-MTAB-14342 | biostudies-arrayexpress