About: Arterivirus nsp12 versus the coronavirus nsp16 2′-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins

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About: Arterivirus nsp12 versus the coronavirus nsp16 2′-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Arterivirus nsp12 versus the coronavirus nsp16 2′-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins
Creator	Gulyaeva, Anastasia Samborskiy, Dmitry Zevenhoven-Dobbe, Jessika Gorbalenya, Alexander Snijder, Eric Gorbalenya, A Lehmann, Kathleen Nl, Posthuma, Clara Correspondence, Alexander Gorbalenya@lumc, Hooghiemstra, Lisa Nl, Clara Posthuma,
Source	Medline; PMC
abstract	The 3′-terminal domain of the most conserved ORF1b in three of the four families of the order Nidovirales (except for the family Arteriviridae) encodes a (putative) 2′-O-methyltransferase (2′-O-MTase), known as non structural protein (nsp) 16 in the family Coronaviridae and implicated in methylation of the 5′ cap structure of nidoviral mRNAs. As with coronavirus transcripts, arterivirus mRNAs are assumed to possess a 5′ cap although no candidate MTases have been identified thus far. To address this knowledge gap, we analysed the uncharacterized nsp12 of arteriviruses, which occupies the ORF1b position equivalent to that of the nidovirus 2′-O-MTase (coronavirus nsp16). In our in-depth bioinformatics analysis of nsp12, the protein was confirmed to be family specific whilst having diverged much further than other nidovirus ORF1b-encoded proteins, including those of the family Coronaviridae. Only one invariant and several partially conserved, predominantly aromatic residues were identified in nsp12, which may adopt a structure with alternating α-helices and β-strands, an organization also found in known MTases. However, no statistically significant similarity was found between nsp12 and the twofold larger coronavirus nsp16, nor could we detect MTase activity in biochemical assays using recombinant equine arteritis virus (EAV) nsp12. Our further analysis established that this subunit is essential for replication of this prototypic arterivirus. Using reverse genetics, we assessed the impact of 25 substitutions at 14 positions, yielding virus phenotypes ranging from WT-like to non-viable. Notably, replacement of the invariant phenylalanine 109 with tyrosine was lethal. We concluded that nsp12 plays an essential role during EAV replication, possibly by acting as a co-factor for another enzyme.
has issue date	2015-09-01(xsd:dateTime)
bibo:doi	10.1099/vir.0.000209
bibo:pmid	26041874
has license	bronze-oa
sha1sum (hex)	faeb9fe9e13d4bb64069905a64c28e2e36adf6a9
schema:url	https://doi.org/10.1099/vir.0.000209
resource representing a document's title	Arterivirus nsp12 versus the coronavirus nsp16 2′-O-methyltransferase: comparison of the C-terminal cleavage products of two nidovirus pp1ab polyproteins
has PubMed Central identifier	PMC7081073
has PubMed identifier	26041874
schema:publication	Journal of General Virology
resource representing a document's body	covid:faeb9fe9e13d4bb64069905a64c28e2e36adf6a9#body_text
is schema:about of	named entity 'CLEAVAGE' named entity 'position' named entity 'phenotypes' named entity 'virus' named entity 'FAMILY' named entity 'ENCODED' named entity 'VIRUS' named entity 'HELICES' named entity 'IDENTIFIED' named entity 'SPECIFIC' named entity 'DOMAIN' named entity 'FACTOR' named entity 'PLAYS' named entity 'EQUINE ARTERITIS VIRUS' named entity 'REVERSE GENETICS' named entity 'IMPACT' named entity 'BIOCHEMICAL' named entity 'RECOMBINANT' named entity 'DETECT' named entity 'CAP' named entity 'ARTERIVIRUSES' named entity 'ADDRESS' named entity 'LARGER' named entity 'PRODUCTS' named entity 'CORONAVIRUS' named entity 'C-TERMINAL' named entity 'O-METHYLTRANSFERASE' named entity 'FAMILY CORONAVIRIDAE' named entity 'MUCH' named entity 'INCLUDING' named entity 'LETHAL' named entity 'STRUCTURAL PROTEIN' named entity 'SIMILARITY' named entity 'LIKE' named entity 'PHENYLALANINE' named entity 'USING' named entity 'POLYPROTEINS' named entity 'ARTERIVIRUS' named entity 'O-METHYLTRANSFERASE' named entity 'COMPARISON' named entity 'NON' named entity 'MRNAS' named entity 'ESTABLISHED' named entity 'ENZYME' named entity 'FOUND' named entity 'SUBUNIT' named entity 'PROTEINS' named entity 'PROTEIN ' named entity 'PARTIALLY' named entity 'ROLE' named entity 'CANDIDATE' named entity 'ASSUMED' named entity 'ORDER NIDOVIRALES' named entity 'STRUCTURE' named entity 'POSSIBLY' named entity 'KNOWLEDGE' named entity 'METHYLATION' named entity 'ASSESSED' named entity 'BIOINFORMATICS ANALYSIS' named entity 'AROMATIC' named entity 'REPLACEMENT' named entity 'PHENOTYPES' named entity 'REPLICATION' named entity 'ACTIVITY' named entity 'CAP STRUCTURE' named entity 'HAVE' named entity 'FAR' named entity 'FAMILIES'

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