Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease.
Identifieur interne : 000F89 ( PubMed/Corpus ); précédent : 000F88; suivant : 000F90Structural Basis for the Ubiquitin-Linkage Specificity and deISGylating activity of SARS-CoV papain-like protease.
Auteurs : Kiira Ratia ; Andrew Kilianski ; Yahira M. Baez-Santos ; Susan C. Baker ; Andrew MesecarSource :
- PLoS pathogens [ 1553-7374 ] ; 2014.
English descriptors
- KwdEn :
- Amino Acid Sequence, Catalytic Domain, Coronavirus Infections (metabolism), Coronavirus Infections (virology), Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (genetics), Cysteine Endopeptidases (metabolism), Cytokines (metabolism), HEK293 Cells, Humans, Models, Molecular, Protein Conformation, Protein Processing, Post-Translational, SARS Virus (enzymology), SARS Virus (genetics), SARS Virus (metabolism), Substrate Specificity, Ubiquitin (metabolism), Ubiquitination (genetics), Ubiquitins (metabolism), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Viral Proteins.
- chemical , genetics : Cysteine Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- genetics : SARS Virus, Ubiquitination.
- metabolism : Coronavirus Infections, Cysteine Endopeptidases, Cytokines, SARS Virus, Ubiquitin, Ubiquitins, Viral Proteins.
- virology : Coronavirus Infections.
- Amino Acid Sequence, Catalytic Domain, Crystallography, X-Ray, HEK293 Cells, Humans, Models, Molecular, Protein Conformation, Protein Processing, Post-Translational, Substrate Specificity.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a papain-like protease (PLpro) with both deubiquitinating (DUB) and deISGylating activities that are proposed to counteract the post-translational modification of signaling molecules that activate the innate immune response. Here we examine the structural basis for PLpro's ubiquitin chain and interferon stimulated gene 15 (ISG15) specificity. We present the X-ray crystal structure of PLpro in complex with ubiquitin-aldehyde and model the interaction of PLpro with other ubiquitin-chain and ISG15 substrates. We show that PLpro greatly prefers K48- to K63-linked ubiquitin chains, and ISG15-based substrates to those that are mono-ubiquitinated. We propose that PLpro's higher affinity for K48-linked ubiquitin chains and ISG15 stems from a bivalent mechanism of binding, where two ubiquitin-like domains prefer to bind in the palm domain of PLpro with the most distal ubiquitin domain interacting with a "ridge" region of the thumb domain. Mutagenesis of residues within this ridge region revealed that these mutants retain viral protease activity and the ability to catalyze hydrolysis of mono-ubiquitin. However, a select number of these mutants have a significantly reduced ability to hydrolyze the substrate ISG15-AMC, or be inhibited by K48-linked diubuiquitin. For these latter residues, we found that PLpro antagonism of the nuclear factor kappa-light-chain-enhancer of activated B-cells (NFκB) signaling pathway is abrogated. This identification of key and unique sites in PLpro required for recognition and processing of diubiquitin and ISG15 versus mono-ubiquitin and protease activity provides new insight into ubiquitin-chain and ISG15 recognition and highlights a role for PLpro DUB and deISGylase activity in antagonism of the innate immune response.
DOI: 10.1371/journal.ppat.1004113
PubMed: 24854014
Links to Exploration step
pubmed:24854014Le document en format XML
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<term>Crystallography, X-Ray</term>
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<front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a papain-like protease (PLpro) with both deubiquitinating (DUB) and deISGylating activities that are proposed to counteract the post-translational modification of signaling molecules that activate the innate immune response. Here we examine the structural basis for PLpro's ubiquitin chain and interferon stimulated gene 15 (ISG15) specificity. We present the X-ray crystal structure of PLpro in complex with ubiquitin-aldehyde and model the interaction of PLpro with other ubiquitin-chain and ISG15 substrates. We show that PLpro greatly prefers K48- to K63-linked ubiquitin chains, and ISG15-based substrates to those that are mono-ubiquitinated. We propose that PLpro's higher affinity for K48-linked ubiquitin chains and ISG15 stems from a bivalent mechanism of binding, where two ubiquitin-like domains prefer to bind in the palm domain of PLpro with the most distal ubiquitin domain interacting with a "ridge" region of the thumb domain. Mutagenesis of residues within this ridge region revealed that these mutants retain viral protease activity and the ability to catalyze hydrolysis of mono-ubiquitin. However, a select number of these mutants have a significantly reduced ability to hydrolyze the substrate ISG15-AMC, or be inhibited by K48-linked diubuiquitin. For these latter residues, we found that PLpro antagonism of the nuclear factor kappa-light-chain-enhancer of activated B-cells (NFκB) signaling pathway is abrogated. This identification of key and unique sites in PLpro required for recognition and processing of diubiquitin and ISG15 versus mono-ubiquitin and protease activity provides new insight into ubiquitin-chain and ISG15 recognition and highlights a role for PLpro DUB and deISGylase activity in antagonism of the innate immune response. </div>
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<Abstract><AbstractText>Severe acute respiratory syndrome coronavirus (SARS-CoV) encodes a papain-like protease (PLpro) with both deubiquitinating (DUB) and deISGylating activities that are proposed to counteract the post-translational modification of signaling molecules that activate the innate immune response. Here we examine the structural basis for PLpro's ubiquitin chain and interferon stimulated gene 15 (ISG15) specificity. We present the X-ray crystal structure of PLpro in complex with ubiquitin-aldehyde and model the interaction of PLpro with other ubiquitin-chain and ISG15 substrates. We show that PLpro greatly prefers K48- to K63-linked ubiquitin chains, and ISG15-based substrates to those that are mono-ubiquitinated. We propose that PLpro's higher affinity for K48-linked ubiquitin chains and ISG15 stems from a bivalent mechanism of binding, where two ubiquitin-like domains prefer to bind in the palm domain of PLpro with the most distal ubiquitin domain interacting with a "ridge" region of the thumb domain. Mutagenesis of residues within this ridge region revealed that these mutants retain viral protease activity and the ability to catalyze hydrolysis of mono-ubiquitin. However, a select number of these mutants have a significantly reduced ability to hydrolyze the substrate ISG15-AMC, or be inhibited by K48-linked diubuiquitin. For these latter residues, we found that PLpro antagonism of the nuclear factor kappa-light-chain-enhancer of activated B-cells (NFκB) signaling pathway is abrogated. This identification of key and unique sites in PLpro required for recognition and processing of diubiquitin and ISG15 versus mono-ubiquitin and protease activity provides new insight into ubiquitin-chain and ISG15 recognition and highlights a role for PLpro DUB and deISGylase activity in antagonism of the innate immune response. </AbstractText>
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<ReferenceList><Reference><Citation>Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):247-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10089417</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2001 Sep 17;20(18):5187-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11566882</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2002 Jun;76(12):6323-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12021365</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2002 Dec 27;111(7):1041-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12507430</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Gen Virol. 2003 Sep;84(Pt 9):2305-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12917450</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2004 Dec;78(24):13600-12</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15564471</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15572765</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Apr;79(7):4550-1</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15767458</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Protein Expr Purif. 2005 May;41(1):207-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15915565</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2005 Jul 22;280(29):27356-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15917233</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Mol Cell Biol. 2005 Aug;6(8):599-609</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16064136</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Mol Cell Biol. 2005 Aug;6(8):610-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16064137</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2005 Aug 19;19(4):547-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16109378</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2005 Nov 2;24(21):3747-56</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16211010</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15189-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306590</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15199-208</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306591</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2005 Dec;79(24):15582-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16306630</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Immunol. 2005 Dec;5(12):941-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16322747</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2005;399:37-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16338347</ArticleId>
</ArticleIdList>
</Reference>
<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>
<Reference><Citation>Structure. 2006 Aug;14(8):1293-302</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16905103</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Dec 8;281(49):38061-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17035239</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2007 Mar 16;367(1):204-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17240395</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2007 Mar 21;26(6):1532-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17318178</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Biochem Biophys. 2007 Oct 1;466(1):8-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17692280</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Nov 2;282(44):32208-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17761676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2007 Dec 7;318(5856):1628-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17991829</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell Host Microbe. 2007 Dec 13;2(6):404-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18078692</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2008 Feb 29;29(4):451-64</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18313383</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Immunol. 2008 Jul;8(7):501-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18535581</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2008 Sep 18;455(7211):358-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18758443</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cell. 2009 Mar 20;136(6):1098-109</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19303852</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2009 Jul;83(13):6689-705</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19369340</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO Rep. 2009 May;10(5):466-73</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19373254</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Microbiol. 2009 Jun;7(6):439-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19430490</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Appl Crystallogr. 2007 Aug 1;40(Pt 4):658-674</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19461840</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Mol Cell Biol. 2009 Aug;10(8):550-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19626045</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2009 Oct 9;392(5):1117-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19664638</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2010 Mar 3;29(5):943-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20075863</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2010 Mar 12;285(11):7852-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20093371</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2010 May;84(9):4619-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20181693</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2010 May;30(10):2424-36</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20308324</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell. 2010 Jun 11;38(5):722-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">20542004</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2011 Apr;85(7):3621-30</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21228232</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2011 Feb 8;108(6):2222-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21245344</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2011 Feb 8;108(6):2228-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21266548</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO Rep. 2011 Apr;12(4):350-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21399617</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2011 Dec;85(23):12201-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">21937658</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Rev Immunol. 2011 Dec 09;12(1):35-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22158412</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Immunol Rev. 2012 Mar;246(1):107-24</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22435550</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2012;81:291-322</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22482907</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2012;81:203-29</Citation>
<ArticleIdList><ArticleId IdType="pubmed">22524316</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>N Engl J Med. 2012 Nov 8;367(19):1814-20</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23075143</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2012 Dec 13;492(7428):266-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23201676</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2013 Feb 1;339(6119):590-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23287719</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 2013 Apr;87(7):3815-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">23345508</ArticleId>
</ArticleIdList>
</Reference>
<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>
<Reference><Citation>J Biol Chem. 1987 Aug 15;262(23):11315-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2440890</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 1997;276:307-26</Citation>
<ArticleIdList><ArticleId IdType="pubmed">27754618</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1994 Feb 18;236(2):601-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8107144</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1996 Mar;16(3):1058-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8622650</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1996 Oct 1;35(39):12893-900</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8841133</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1998 Feb 17;37(7):1868-79</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9485312</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1998 Mar 3;37(9):2925-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9485444</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 1998;67:425-79</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9759494</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
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