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HGNC Genes

SARS-CoV-2 proteins

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    SARS-CoV-2 nucleocapsid protein PROTEIN undergoes liquid-liquid phase separation stimulated by RNA and partitions into phases of human ribonucleoproteins

    Authors: Theodora Myrto Perdikari; Anastasia C Murthy; Veronica H Ryan; Scott Watters; Mandar T Naik; Nicolas L Fawzi

    doi:10.1101/2020.06.09.141101 Date: 2020-06-10 Source: bioRxiv

    Tightly packed complexes of nucleocapsid protein PROTEIN and genomic RNA form the core of viruses and may assemble within viral factories, dynamic compartments formed within the host cells. Here, we examine the possibility that the multivalent RNA-binding nucleocapsid protein (N PROTEIN) from the severe acute respiratory syndrome coronavirus (SARS-CoV-2) MESHD compacts RNA via protein-RNA liquid-liquid phase separation ( LLPS MESHD) and that N interactions with host RNA-binding proteins are mediated by phase separation. To this end, we created a construct expressing recombinant N fused to a N-terminal maltose binding protein tag which helps keep the oligomeric N soluble for purification. Using in vitro phase separation assays, we find that N is assembly-prone and phase separates avidly. Phase separation is modulated by addition of RNA and changes in pH and is disfavored at high concentrations of salt. Furthermore, N enters into in vitro phase separated condensates of full-length human hnRNPs ( TDP-43 HGNC, FUS HGNC, and hnRNPA2 HGNC) and their low complexity domains (LCs). However, N partitioning into the LC of FUS HGNC, but not TDP MESHD TDP HGNC-43 or hnRNPA2 HGNC, requires cleavage of the solubilizing MBP HGNC fusion. Hence, LLPS MESHD may be an essential mechanism used for SARS-CoV-2 and other RNA viral genome packing and host protein co-opting, functions necessary for viral replication and hence infectivity.

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MeSH Disease
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