About: Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities

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About: Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities 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	Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities
Creator	Chen, Yafang Mesecar, Andrew Baker, Susan Mielech, Anna
Source	Elsevier; Medline; PMC
abstract	Coronaviruses and arteriviruses, members of the order Nidovirales, are positive strand RNA viruses that encode large replicase polyproteins that are processed by viral proteases to generate the nonstructural proteins which mediate viral RNA synthesis. The viral papain-like proteases (PLPs) are critical for processing the amino-terminal end of the replicase and are attractive targets for antiviral therapies. With the analysis of the papain-like protease of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV), came the realization of the multifunctional nature of these enzymes. Structural and enzymatic studies revealed that SARS-CoV PLpro can act as both a protease to cleave peptide bonds and also as a deubiquitinating (DUB) enzyme to cleave the isopeptide bonds found in polyubiquitin chains. Furthermore, viral DUBs can also remove the protective effect of conjugated ubiquitin-like molecules such as interferon stimulated gene 15 (ISG15). Extension of these studies to other coronaviruses and arteriviruses led to the realization that viral protease/DUB activity is conserved in many family members. Overexpression studies revealed that viral protease/DUB activity can modulate or block activation of the innate immune response pathway. Importantly, mutations that alter DUB activity but not viral protease activity have been identified and arteriviruses expressing DUB mutants stimulated higher levels of acute inflammatory cytokines after infection. Further understanding of the multifunctional nature of the Nidovirus PLP/DUBs may facilitate vaccine development. Here, we review studies describing the PLPs’ enzymatic activity and their role in virus pathogenesis.
has issue date	2014-12-01(xsd:dateTime)
bibo:doi	10.1016/j.virusres.2014.01.025
bibo:pmid	24512893
has license	green-oa
sha1sum (hex)	45de9e3fa82e45cc8c88661dbffd27a70a2b41a6
schema:url	https://doi.org/10.1016/j.virusres.2014.01.025
resource representing a document's title	Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities
has PubMed Central identifier	PMC4125544
has PubMed identifier	24512893
schema:publication	Virus Research
resource representing a document's body	covid:45de9e3fa82e45cc8c88661dbffd27a70a2b41a6#body_text
is schema:about of	named entity 'coronaviruses' named entity 'targets' named entity 'Here' named entity 'higher' named entity 'mutations' named entity 'molecules' named entity 'enzymatic activity' named entity 'expressing' named entity 'block' named entity 'activation' named entity 'viral' named entity 'stimulated' named entity 'activities' named entity 'BONDS' named entity 'VIRAL RNA' named entity 'ANALYSIS' named entity 'RNA SYNTHESIS' named entity 'PROTEASE' named entity 'LIKE' named entity 'MOLECULES' named entity 'MEMBERS' named entity 'THEIR' named entity 'LEVELS' named entity 'REALIZATION' named entity 'BUT' named entity 'THESE' named entity 'MODULATE' named entity 'POSITIVE STRAND' named entity 'POLYPROTEINS' named entity 'UNDERSTANDING' named entity 'STIMULATED' named entity 'VACCINE DEVELOPMENT' named entity 'PROCESSING' named entity 'HIGHER' named entity 'FOUND' named entity 'PROCESSED' covid:arg/45de9e3fa82e45cc8c88661dbffd27a70a2b41a6 named entity 'DEUBIQUITINATING' named entity 'CONSERVED' named entity 'PROTECTIVE EFFECT' named entity 'REMOVE' named entity 'SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS' named entity 'LED' named entity 'FAMILY MEMBERS' named entity 'PROTEASES' named entity 'ACTIVITIES' named entity 'PAPAIN' named entity 'MULTIFUNCTIONAL ENZYMES' named entity 'MUTANTS' named entity 'INNATE IMMUNE RESPONSE PATHWAY' named entity 'ENZYMATIC' named entity 'RNA VIRUSES' named entity 'REPLICASE' named entity 'HAVE' named entity 'ATTRACTIVE' named entity 'INFECTION' named entity 'PATHOGENESIS' named entity 'CYTOKINES' named entity 'LIKE' named entity 'ANTIVIRAL' named entity 'DESCRIBING' named entity 'POLYUBIQUITIN' named entity 'THERAPIES' named entity 'INFLAMMATORY' named entity 'ENZYMES' named entity 'LARGE' named entity 'PAPAIN' named entity 'ENCODE' named entity 'CRITICAL' named entity 'NONSTRUCTURAL PROTEINS' named entity 'PLP' named entity 'ENZYME' named entity 'TO CLEAVE' named entity 'REVEALED' named entity 'TERMINAL' named entity 'STRUCTURAL' named entity 'ACT' named entity 'CAME'

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