Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities.
Identifieur interne : 001A61 ( PubMed/Curation ); précédent : 001A60; suivant : 001A62Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities.
Auteurs : Anna M. Mielech [États-Unis] ; Yafang Chen [États-Unis] ; Andrew D. Mesecar [États-Unis] ; Susan C. Baker [États-Unis]Source :
- Virus research [ 1872-7492 ] ; 2014.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Nidovirales.
- métabolisme : Enzymes multifonctionnelles, Peptide hydrolases, Ubiquitin-specific proteases.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Multifunctional Enzymes, Peptide Hydrolases, Ubiquitin-Specific Proteases.
- enzymology : Nidovirales.
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.
DOI: 10.1016/j.virusres.2014.01.025
PubMed: 24512893
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<front><div type="abstract" xml:lang="en">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. </div>
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<ReferenceList><Reference><Citation>Lancet Infect Dis. 2013 Oct;13(10):859-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23933067</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Viruses. 2010 Oct;2(10):2154-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21994614</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 2014 Feb;450-451:64-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24503068</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>EMBO J. 2005 Nov 2;24(21):3747-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16211010</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2009 Sep;83(18):9449-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19587037</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1986 Oct;60(1):12-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3018279</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):E838-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23401522</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Gen Virol. 2014 Mar;95(Pt 3):614-626</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24362959</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 1999 May 21;274(21):14918-25</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10329692</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2005 Dec;79(24):15199-208</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306591</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 2007 Nov 2;282(44):32208-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17761676</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2010 Oct;84(19):10102-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20668084</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Biochim Biophys Acta. 2010 May;1802(5):485-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20153823</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2005 Nov;79(22):13974-83</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16254333</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1999 Apr;73(4):2658-66</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10074111</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>PLoS One. 2011 Feb 18;6(2):e17192</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21364999</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2000 Sep;74(17):7911-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10933699</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2005 Apr;79(7):4550-1</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15767458</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Lancet Infect Dis. 2014 Feb;14(2):140-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24355866</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 1998 Sep 15;95(19):11089-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9736694</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Emerg Infect Dis. 2014 Apr;20(4):552-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24655412</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Protein Sci. 2008 Jun;17(6):1035-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18424514</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2003 Jul;77(13):7376-82</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12805436</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Gen Virol. 2013 Jul;94(Pt 7):1554-1567</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23596270</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2004 Dec;78(24):13600-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15564471</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Annu Rev Biochem. 2012;81:203-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22524316</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell Host Microbe. 2007 Dec 13;2(6):404-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18078692</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2006 Apr 11;103(15):5717-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16581910</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Mol Cell Biol. 2004 Feb;24(4):1779-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14749392</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Rev Mol Cell Biol. 2009 Aug;10(8):550-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19626045</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1989 Sep;63(9):3693-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2547993</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Emerg Infect Dis. 2013 Nov;19(11):1819-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">24206838</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2010 May;84(9):4619-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20181693</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Virology. 1992 Jul;189(1):274-84</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1318604</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Arch Biochem Biophys. 2007 Oct 1;466(1):8-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17692280</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1371-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17227866</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2012 Apr;86(7):3839-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22258253</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 1993 Oct;67(10):6056-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8396668</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>mBio. 2012 Nov 20;3(6):</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23170002</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2013 Aug;87(15):8638-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23720729</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Nat Rev Microbiol. 2009 Jun;7(6):439-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19430490</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2005 Dec;79(24):15189-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306590</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2007 Jun;81(11):6007-18</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17392370</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Cell Res. 2008 Nov;18(11):1105-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18957937</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2012 Jan;86(2):773-85</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22072774</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2010 Oct;84(19):10063-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20668092</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17717-22</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16301520</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2009 Jul;83(13):6689-705</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19369340</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2013 Nov;87(21):11955-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23986593</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Virol. 2010 Aug;84(15):7832-46</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20504922</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
<ReferenceList><Reference><Citation>J Biol Chem. 1995 Jul 14;270(28):16671-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7622476</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
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