About: Expression and Cleavage of Middle East Respiratory Syndrome Coronavirus nsp3-4 Polyprotein Induce the Formation of Double-Membrane Vesicles That Mimic Those Associated with Coronaviral RNA Replication

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About: Expression and Cleavage of Middle East Respiratory Syndrome Coronavirus nsp3-4 Polyprotein Induce the Formation of Double-Membrane Vesicles That Mimic Those Associated with Coronaviral RNA Replication Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Expression and Cleavage of Middle East Respiratory Syndrome Coronavirus nsp3-4 Polyprotein Induce the Formation of Double-Membrane Vesicles That Mimic Those Associated with Coronaviral RNA Replication
Creator	Kikkert, Marjolein Bárcena, Montserrat Oudshoorn, Diede Groen, Kevin Rijs, Kevin Snijder, Eric Koster, Abraham Limpens, Ronald
Source	Medline; PMC
abstract	Betacoronaviruses, such as Middle East respiratory syndrome coronavirus (MERS-CoV), are important pathogens causing potentially lethal infections in humans and animals. Coronavirus RNA synthesis is thought to be associated with replication organelles (ROs) consisting of modified endoplasmic reticulum (ER) membranes. These are transformed into double-membrane vesicles (DMVs) containing viral double-stranded RNA and into other membranous elements such as convoluted membranes, together forming a reticulovesicular network. Previous evidence suggested that the nonstructural proteins (nsp’s) 3, 4, and 6 of the severe acute respiratory syndrome coronavirus (SARS-CoV), which contain transmembrane domains, would all be required for DMV formation. We have now expressed MERS-CoV replicase self-cleaving polyprotein fragments encompassing nsp3-4 or nsp3-6, as well as coexpressed nsp3 and nsp4 of either MERS-CoV or SARS-CoV, to characterize the membrane structures induced. Using electron tomography, we demonstrate that for both MERS-CoV and SARS-CoV coexpression of nsp3 and nsp4 is required and sufficient to induce DMVs. Coexpression of MERS-CoV nsp3 and nsp4 either as individual proteins or as a self-cleaving nsp3-4 precursor resulted in very similar DMVs, and in both setups we observed proliferation of zippered ER that appeared to wrap into nascent DMVs. Moreover, when inactivating nsp3-4 polyprotein cleavage by mutagenesis, we established that cleavage of the nsp3/nsp4 junction is essential for MERS-CoV DMV formation. Addition of the third MERS-CoV transmembrane protein, nsp6, did not noticeably affect DMV formation. These findings provide important insight into the biogenesis of coronavirus DMVs, establish strong similarities with other nidoviruses (specifically, the arteriviruses), and highlight possible general principles in viral DMV formation.
has issue date	2017-11-21(xsd:dateTime)
bibo:doi	10.1128/mbio.01658-17
bibo:pmid	29162711
has license	cc-by
sha1sum (hex)	b6365c84be3efb9b6845cf8f664ae3e5b913c4a0
schema:url	https://doi.org/10.1128/mbio.01658-17
resource representing a document's title	Expression and Cleavage of Middle East Respiratory Syndrome Coronavirus nsp3-4 Polyprotein Induce the Formation of Double-Membrane Vesicles That Mimic Those Associated with Coronaviral RNA Replication
has PubMed Central identifier	PMC5698553
has PubMed identifier	29162711
schema:publication	mBio
resource representing a document's body	covid:b6365c84be3efb9b6845cf8f664ae3e5b913c4a0#body_text
is schema:about of	named entity 'DMVs' named entity 'fragments' named entity 'nsp3' named entity 'MERS-CoV' named entity 'coronavirus' named entity 'formation' named entity 'encompassing' named entity 'functionality' named entity 'replicase' named entity 'MERS-CoV' named entity 'formation' named entity 'basis' named entity 'individual' named entity 'nsp3' named entity 'ASSOCIATED WITH' named entity 'FORMATION' named entity 'MIMIC' covid:arg/b6365c84be3efb9b6845cf8f664ae3e5b913c4a0 named entity 'COEXPRESSION' named entity 'RNA SYNTHESIS' named entity 'POSSIBLE' named entity 'REPLICATION' named entity 'ASSOCIATED WITH' named entity 'MEMBRANE' named entity 'ORGANELLES' named entity 'PRECURSOR' named entity 'FRAGMENTS' named entity 'GENERAL' named entity 'INDIVIDUAL' named entity 'SARS-COV' named entity 'NSP3' named entity 'MEMBRANES' named entity 'HAVE' named entity 'THOUGHT' named entity 'PROTEINS' named entity 'NONSTRUCTURAL PROTEINS' named entity 'MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS' named entity 'JUNCTION' named entity 'LITTLE' named entity 'FINDINGS' named entity 'MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS' named entity 'POINT' named entity 'STUDY' named entity 'PROTEIN REQUIREMENTS' named entity 'MEMBRANOUS' named entity 'PROLIFERATION' named entity 'POLYPROTEIN' named entity 'EITHER' named entity 'VIRAL' named entity 'ELECTRON TOMOGRAPHY' named entity 'TRANSMEMBRANE' named entity 'ESSENTIAL' named entity 'ANIMALS' named entity 'EXPRESSION' named entity 'ESTABLISH' named entity 'RNA REPLICATION' named entity 'TYPE' named entity 'INSIGHT' named entity 'ARTERIVIRUSES' named entity 'CLEAVAGE' named entity 'PROTEOLYTIC' named entity 'FUNCTIONALITY' named entity 'KNOWN' named entity 'FORMATION' named entity 'PROMINENT' named entity 'MATURATION' named entity 'CORONAVIRUSES' named entity 'TRANSMEMBRANE PROTEIN' named entity 'NUMBER OF' named entity 'ROS' named entity 'CONTAIN' named entity 'ELEMENTS' named entity 'NSP4' named entity 'TAKE PLACE'

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