The ADP-ribose-1″-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses

Kuri, Thomas; Eriksson, Klara Kristin; Putics, Ákos; Züst, Roland; Snijder, Eric J.; Davidson, Andrew D.; Siddell, Stuart G.; Thiel, Volker; Ziebuhr, John; Weber, Friedemann

doi:10.1099/vir.0.031856-0

Cited by 99 publications

(130 citation statements)

References 42 publications

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“…4E and Table 2) (46–48). The activity of this domain is not essential for replication in vitro but may help counteract the innate immune response in vivo (49, 50). At approximately the same position of snake virus pp1a is a predicted protein kinase (PFam PKinase domain) that is not present in any other nidovirus as determined by HMMER analysis (HMMER3 E value, 1.5 × 10 −6 ) (Fig.…”

Section: Resultsmentioning

confidence: 99%

Ball Python Nidovirus: a Candidate Etiologic Agent for Severe Respiratory Disease in Python regius

Stenglein

Jacobson

Wozniak

et al. 2014

mBio

128

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A severe, sometimes fatal respiratory disease has been observed in captive ball pythons (Python regius) since the late 1990s. In order to better understand this disease and its etiology, we collected case and control samples and performed pathological and diagnostic analyses. Electron micrographs revealed filamentous virus-like particles in lung epithelial cells of sick animals. Diagnostic testing for known pathogens did not identify an etiologic agent, so unbiased metagenomic sequencing was performed. Abundant nidovirus-like sequences were identified in cases and were used to assemble the genome of a previously unknown virus in the order Nidovirales. The nidoviruses, which were not previously known to infect nonavian reptiles, are a diverse order that includes important human and veterinary pathogens. The presence of the viral RNA was confirmed in all diseased animals (n = 8) but was not detected in healthy pythons or other snakes (n = 57). Viral RNA levels were generally highest in the lung and other respiratory tract tissues. The 33.5-kb viral genome is the largest RNA genome yet described and shares canonical characteristics with other nidovirus genomes, although several features distinguish this from related viruses. This virus, which we named ball python nidovirus (BPNV), will likely establish a new genus in Torovirinae subfamily. The identification of a novel nidovirus in reptiles contributes to our understanding of the biology and evolution of related viruses, and its association with lung disease in pythons is a promising step toward elucidating an etiology for this long-standing veterinary disease.

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Section: Resultsmentioning

confidence: 99%

Ball Python Nidovirus: a Candidate Etiologic Agent for Severe Respiratory Disease in Python regius

Stenglein

Jacobson

Wozniak

et al. 2014

mBio

128

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“…Our group has shown that the X domain (Mac1) is dispensable for RNA replication in the context of a SARS-CoV replicon (Kusov et al, 2015). Recently, evidence accumulated showing that the X domain plays a role in counteracting the host innate immune response (Eriksson et al, 2008;Kuri et al, 2011;Fehr et al, , 2016.…”

Section: Macrodomain I (Mac1 X Domain)mentioning

confidence: 99%

“…These results suggest that the main function of the X domain may differ in different CoVs. On the other hand, the expression level of type-I IFN (α or β) is increased in cells infected with SARS-CoV or MHV carrying the Asn-to-Ala mutation in the X domain (Eriksson et al, 2008;Kuri et al, 2011;Fehr et al, 2016). This indicates that suppression of innate immunity by the X domain may be a feature conserved across the coronaviruses.…”

Section: Macrodomain I (Mac1 X Domain)mentioning

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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“…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

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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.

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The ADP-ribose-1″-monophosphatase domains of severe acute respiratory syndrome coronavirus and human coronavirus 229E mediate resistance to antiviral interferon responses

Cited by 99 publications

References 42 publications

Ball Python Nidovirus: a Candidate Etiologic Agent for Severe Respiratory Disease in Python regius

Ball Python Nidovirus: a Candidate Etiologic Agent for Severe Respiratory Disease in Python regius

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

Biogenesis and Dynamics of the Coronavirus Replicative Structures

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