A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein

Kamitani, Wataru; Huang, Cheng; Narayanan, Krishna; Lokugamage, Kumari G.; Makino, Shinji

doi:10.1038/nsmb.1680

Cited by 377 publications

(548 citation statements)

References 41 publications

Supporting

Mentioning

512

Contrasting

Order By: Relevance

“…A subsequent BCoV DI RNA mutagenesis study further suggested that this multipartite RNA structure may involve several stem-loop (sub)structures identified in earlier studies (Gustin et al, 2009;Raman and Brian, 2005) but require refolding of other RNA structures suggested earlier to be essential for DI RNA replication (Brown et al, 2007). The study by Su et al (2014) also identified an intriguing requirement in cis of an oligopeptide sequence in the Nproximal part of nsp1, suggesting that nsp1 may be an essential cis-acting protein factor in betacoronavirus replication, in addition to its multiple other functions (Brockway and Denison, 2005;Huang et al, 2011a,b;Kamitani et al, 2006Kamitani et al, , 2009Lei et al, 2013;Lokugamage et al, 2012;Narayanan et al, 2008a;Tanaka et al, 2012;Tohya et al, 2009;Wathelet et al, 2007;Züst et al, 2007). Possible interacting partners for nsp1 remain to be identified.…”

Section: Functional and Structural Features Of Coronavirus 5 Cis-actimentioning

confidence: 91%

RNA structure analysis of alphacoronavirus terminal genome regions

et al. 2014

View full text Add to dashboard Cite

Coronavirus genome replication is mediated by a multi-subunit protein complex that is comprised of more than a dozen virally encoded and several cellular proteins. Interactions of the viral replicase complex with cis-acting RNA elements located in the 5' and 3'-terminal genome regions ensure the specific replication of viral RNA. Over the past years, boundaries and structures of cis-acting RNA elements required for coronavirus genome replication have been extensively characterized in betacoronaviruses and, to a lesser extent, other coronavirus genera. Here, we review our current understanding of coronavirus cis-acting elements located in the terminal genome regions and use a combination of bioinformatic and RNA structure probing studies to identify and characterize putative cis-acting RNA elements in alphacoronaviruses. The study suggests significant RNA structure conservation among members of the genus Alphacoronavirus but also across genus boundaries. Overall, the conservation pattern identified for 5' and 3'-terminal RNA structural elements in the genomes of alpha- and betacoronaviruses is in agreement with the widely used replicase polyprotein-based classification of the Coronavirinae, suggesting co-evolution of the coronavirus replication machinery with cognate cis-acting RNA elements.

show abstract

Section: Functional and Structural Features Of Coronavirus 5 Cis-actimentioning

confidence: 91%

RNA structure analysis of alphacoronavirus terminal genome regions

et al. 2014

View full text Add to dashboard Cite

show abstract

“…In addition to the nsps mentioned above, other CoV nsps are involved in RNA binding (nsp9 and nsp10; [48,49]) or in evasion of the antiviral response of the host (nsp1 and nsp3; [50,51,52,53,54,55,56,57]). The function of nsp2 is not yet known, although this protein was shown not to be essential for virus replication [58,59].…”

Section: Coronavirus Nonstructural Proteinsmentioning

confidence: 99%

Biogenesis and Dynamics of the Coronavirus Replicative Structures

Hagemeijer

Rottier

Haan

2012

Viruses

View full text Add to dashboard Cite

Coronaviruses are positive-strand RNA viruses that are important infectious agents of both animals and humans. A common feature among positive-strand RNA viruses is their assembly of replication-transcription complexes in association with cytoplasmic membranes. Upon infection, coronaviruses extensively rearrange cellular membranes into organelle-like replicative structures that consist of double-membrane vesicles and convoluted membranes to which the nonstructural proteins involved in RNA synthesis localize. Double-stranded RNA, presumably functioning as replicative intermediate during viral RNA synthesis, has been detected at the double-membrane vesicle interior. Recent studies have provided new insights into the assembly and functioning of the coronavirus replicative structures. This review will summarize the current knowledge on the biogenesis of the replicative structures, the membrane anchoring of the replication-transcription complexes, and the location of viral RNA synthesis, with particular focus on the dynamics of the coronavirus replicative structures and individual replication-associated proteins.

show abstract

“…This 'host shutoff' phenotype can be triggered through a range of mechanisms that operate at nearly every stage of the gene expression cascade. Viruses whose host shutoff strategies involve the induction of widespread mRNA decay include the alpha and gammaherpesviruses, vaccinia virus (VACV), influenza A virus (IAV), and SARS coronavirus (SCoV) [1][2][3][4][5] In each of the above cases, mRNA degradation is induced via one or more internal endonucleolytic cleavages in the target mRNA or, in the case of VACV, direct removal of the mRNA 5' cap [5][6][7][8][9]. This is invariably followed by exonucleolytic degradation of the cleaved fragment(s) by components of the mammalian RNA decay machinery such as Xrn1 [1,10,11].…”

Section: Introductionmentioning

confidence: 99%

Nuclease escape elements protect messenger RNA against cleavage by multiple viral endonucleases

Muller

Glaunsinger

2017

Preprint

View full text Add to dashboard Cite

During lytic Kaposi's sarcoma-associated herpesvirus (KSHV) infection, the viral endonuclease SOX promotes widespread degradation of cytoplasmic messenger RNA (mRNA). However, select mRNAs, including the transcript encoding interleukin-6 (IL-6), escape SOX-induced cleavage. IL-6 escape is mediated through a 3' UTR RNA regulatory element that overrides the SOX targeting mechanism. Here, we reveal that this protective RNA element functions to broadly restrict cleavage by a range of homologous and non-homologous viral endonucleases. However, it does not impede cleavage by cellular endonucleases. The IL-6 protective sequence may be representative of a larger class of nuclease escape elements, as we identified a similar protective element in the GADD45B mRNA. The IL-6 and GADD45B-derived elements display similarities in their sequence, putative structure, and several associated RNA binding proteins. However, the overall composition of their ribonucleoprotein complexes appears distinct, leading to differences in the breadth of nucleases restricted. These findings highlight how RNA elements can selectively control transcript abundance in the background of widespread virus-induced mRNA degradation.

show abstract

A two-pronged strategy to suppress host protein synthesis by SARS coronavirus Nsp1 protein

Cited by 377 publications

References 41 publications

RNA structure analysis of alphacoronavirus terminal genome regions

RNA structure analysis of alphacoronavirus terminal genome regions

Biogenesis and Dynamics of the Coronavirus Replicative Structures

Nuclease escape elements protect messenger RNA against cleavage by multiple viral endonucleases

Contact Info

Product

Resources

About