Characterization of a Critical Interaction between the Coronavirus Nucleocapsid Protein and Nonstructural Protein 3 of the Viral Replicase-Transcriptase Complex

Hurst, Kelley R.; Koetzner, Cheri A.; Masters, Paul S.

doi:10.1128/jvi.01275-13

Cited by 138 publications

(223 citation statements)

References 72 publications

(130 reference statements)

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“…The NMR structure of the residues 1e112 of SARS-CoV nsp3 exhibits a globular ubiquitin-like fold with two additional helices which make the overall structure of the Ub1 domain somewhat more elongated than other ubiquitin-like proteins (Serrano et al, 2007b). In contrast, the following HVR was shown to be structurally disordered for SARS-CoV (Serrano et al, 2007b) and is dispensable for replication in MHV (Hurst et al, 2013).…”

Section: Nsp3 (Ub1 To Pl1 Pro )mentioning

confidence: 99%

“…While the function of Ub1 has only been investigated in MHV, this domain has been found to play an essential role in initiating viral RNA synthesis, where it interacts with the viral nucleoprotein (N; (Hurst et al, 2013;Hurst-Hess et al, 2015)). This was demonstrated in experiments that attempted to delete nsp3 domains, or substitute with the corresponding domains from other coronaviruses.…”

Section: Nsp3 (Ub1 To Pl1 Pro )mentioning

confidence: 99%

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Bioinformatics and functional analyses of coronavirus nonstructural proteins involved in the formation of replicative organelles

Neuman

2016

Antiviral Research

107

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Replication of eukaryotic positive-stranded RNA viruses is usually linked to the presence of membrane-associated replicative organelles. The purpose of this review is to discuss the function of proteins responsible for formation of the coronavirus replicative organelle. This will be done by identifying domains that are conserved across the order Nidovirales, and by summarizing what is known about function and structure at the level of protein domains.

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Section: Nsp3 (Ub1 To Pl1 Pro )mentioning

confidence: 99%

Section: Nsp3 (Ub1 To Pl1 Pro )mentioning

confidence: 99%

Bioinformatics and functional analyses of coronavirus nonstructural proteins involved in the formation of replicative organelles

Neuman

2016

Antiviral Research

107

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“…The N-nsp3 interaction has been specifically mapped to the ubiquitin-like domain (Ubl1) of nsp3, an essential domain to the virus [127]. Moreover, it was also shown that this N-nsp3 interaction is required for N protein to promote optimal infectivity of gRNA [52].…”

Section: Functions Of the Nucleocapsidmentioning

confidence: 99%

The Coronavirus Nucleocapsid Is a Multifunctional Protein

McBride

Zyl

Fielding

2014

Viruses

823

907

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The coronavirus nucleocapsid (N) is a structural protein that forms complexes with genomic RNA, interacts with the viral membrane protein during virion assembly and plays a critical role in enhancing the efficiency of virus transcription and assembly. Recent studies have confirmed that N is a multifunctional protein. The aim of this review is to highlight the properties and functions of the N protein, with specific reference to (i) the topology; (ii) the intracellular localization and (iii) the functions of the protein.

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“…The known functional roles of Ubl1 in CoVs are related to singlestranded (ssRNA) binding and interacting with the nucleocapsid (N) protein (Fig. 1B;Serrano et al, 2007;Hurst et al, 2010Hurst et al, , 2013. The Ubl1 of SARS-CoV binds ssRNA containing AUA patterns.…”

Section: Ubiquitin-like Domain 1 and The Glu-rich Acidic Regionmentioning

confidence: 99%

“…In MHV, the Ubl1 domain efficiently binds the cognate nucleocapsid (N) protein; thus it seems to be important for virus replication as well as initiation of viral infection. There is a critical relationship between Nsp3 interaction with the N protein and infectivity, as this interaction serves to tether the viral genome to the newly translated RTC at an early stage of coronavirus infection (Hurst et al, 2010(Hurst et al, , 2013. Deletion of the Ubl1 core (residues 19-111) of MHV abrogates viral replication (Hurst et al, 2013).…”

Section: Ubiquitin-like Domain 1 and The Glu-rich Acidic Regionmentioning

confidence: 99%

Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein

2018

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The multi-domain non-structural protein 3 (Nsp3) is the largest protein encoded by the coronavirus (CoV) genome, with an average molecular mass of about 200 kD. Nsp3 is an essential component of the replication/transcription complex. It comprises various domains, the organization of which differs between CoV genera, due to duplication or absence of some domains. However, eight domains of Nsp3 exist in all known CoVs: the ubiquitin-like domain 1 (Ubl1), the Glu-rich acidic domain (also called "hypervariable region"), a macrodomain (also named "X domain"), the ubiquitin-like domain 2 (Ubl2), the papain-like protease 2 (PL2), the Nsp3 ectodomain (3Ecto, also called "zinc-finger domain"), as well as the domains Y1 and CoV-Y of unknown functions. In addition, the two transmembrane regions, TM1 and TM2, exist in all CoVs. The three-dimensional structures of domains in the N-terminal two thirds of Nsp3 have been investigated by X-ray crystallography and/or nuclear magnetic resonance (NMR) spectroscopy since the outbreaks of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) in 2003 as well as Middle-East Respiratory Syndrome coronavirus (MERS-CoV) in 2012. In this review, the structures and functions of these domains of Nsp3 are discussed in depth.

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Characterization of a Critical Interaction between the Coronavirus Nucleocapsid Protein and Nonstructural Protein 3 of the Viral Replicase-Transcriptase Complex

Cited by 138 publications

References 72 publications

Bioinformatics and functional analyses of coronavirus nonstructural proteins involved in the formation of replicative organelles

Bioinformatics and functional analyses of coronavirus nonstructural proteins involved in the formation of replicative organelles

The Coronavirus Nucleocapsid Is a Multifunctional Protein

Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein

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