tetano
Editor, Senior Moderator
Virology
. 2021 Dec 14;567:1-14.
doi: 10.1016/j.virol.2021.12.004. Online ahead of print.
Analysis of a crucial interaction between the coronavirus nucleocapsid protein and the major membrane-bound subunit of the viral replicase-transcriptase complex
Cheri A Koetzner[SUP] 1 [/SUP], Kelley R Hurst-Hess[SUP] 1 [/SUP], Lili Kuo[SUP] 1 [/SUP], Paul S Masters[SUP] 2 [/SUP]
Affiliations
Abstract
The coronavirus nucleocapsid (N) protein comprises two RNA-binding domains connected by a central spacer, which contains a serine- and arginine-rich (SR) region. The SR region engages the largest subunit of the viral replicase-transcriptase, nonstructural protein 3 (nsp3), in an interaction that is essential for efficient initiation of infection by genomic RNA. We carried out an extensive genetic analysis of the SR region of the N protein of mouse hepatitis virus in order to more precisely define its role in RNA synthesis. We further examined the N-nsp3 interaction through construction of nsp3 mutants and by creation of an interspecies N protein chimera. Our results indicate a role for the central spacer as an interaction hub of the N molecule that is partially regulated by phosphorylation. These findings are discussed in relation to the recent discovery that nsp3 forms a molecular pore in the double-membrane vesicles that sequester the coronavirus replicase-transcriptase.
Keywords: Coronavirus; Mouse hepatitis virus; Nonstructural protein 3; Nucleocapsid protein; Viral RNA synthesis; Viral genomic RNA.
. 2021 Dec 14;567:1-14.
doi: 10.1016/j.virol.2021.12.004. Online ahead of print.
Analysis of a crucial interaction between the coronavirus nucleocapsid protein and the major membrane-bound subunit of the viral replicase-transcriptase complex
Cheri A Koetzner[SUP] 1 [/SUP], Kelley R Hurst-Hess[SUP] 1 [/SUP], Lili Kuo[SUP] 1 [/SUP], Paul S Masters[SUP] 2 [/SUP]
Affiliations
- PMID: 34933176
- PMCID: PMC8669624
- DOI: 10.1016/j.virol.2021.12.004
Abstract
The coronavirus nucleocapsid (N) protein comprises two RNA-binding domains connected by a central spacer, which contains a serine- and arginine-rich (SR) region. The SR region engages the largest subunit of the viral replicase-transcriptase, nonstructural protein 3 (nsp3), in an interaction that is essential for efficient initiation of infection by genomic RNA. We carried out an extensive genetic analysis of the SR region of the N protein of mouse hepatitis virus in order to more precisely define its role in RNA synthesis. We further examined the N-nsp3 interaction through construction of nsp3 mutants and by creation of an interspecies N protein chimera. Our results indicate a role for the central spacer as an interaction hub of the N molecule that is partially regulated by phosphorylation. These findings are discussed in relation to the recent discovery that nsp3 forms a molecular pore in the double-membrane vesicles that sequester the coronavirus replicase-transcriptase.
Keywords: Coronavirus; Mouse hepatitis virus; Nonstructural protein 3; Nucleocapsid protein; Viral RNA synthesis; Viral genomic RNA.