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Analysis of a crucial interaction between the coronavirus nucleocapsid protein and the major membrane-bound subunit of the viral replicase-transcriptase complex.
Koetzner, Cheri A; Hurst-Hess, Kelley R; Kuo, Lili; Masters, Paul S.
  • Koetzner CA; Laboratory of Viral Replication and Vector Biology, Wadsworth Center, New York State Department of Health, Slingerlands, NY, 12159, USA.
  • Hurst-Hess KR; Laboratory of Viral Replication and Vector Biology, Wadsworth Center, New York State Department of Health, Slingerlands, NY, 12159, USA.
  • Kuo L; Laboratory of Viral Replication and Vector Biology, Wadsworth Center, New York State Department of Health, Slingerlands, NY, 12159, USA.
  • Masters PS; Laboratory of Viral Replication and Vector Biology, Wadsworth Center, New York State Department of Health, Slingerlands, NY, 12159, USA; Department of Biomedical Sciences, School of Public Health, State University of New York, Albany, NY, 12208, USA. Electronic address: Paul.Masters@health.ny.gov.
Virology ; 567: 1-14, 2022 02.
Article in English | MEDLINE | ID: covidwho-1628759
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.
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Full text: Available Collection: International databases Database: MEDLINE Main subject: Coronavirus Nucleocapsid Proteins / Viral Replicase Complex Proteins / Intracellular Membranes Limits: Animals Language: English Journal: Virology Year: 2022 Document Type: Article Affiliation country: J.virol.2021.12.004

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Full text: Available Collection: International databases Database: MEDLINE Main subject: Coronavirus Nucleocapsid Proteins / Viral Replicase Complex Proteins / Intracellular Membranes Limits: Animals Language: English Journal: Virology Year: 2022 Document Type: Article Affiliation country: J.virol.2021.12.004