Crystal Structure of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune Suppression*
Identifieur interne : 000D86 ( Pmc/Curation ); précédent : 000D85; suivant : 000D87Crystal Structure of the Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune Suppression*
Auteurs : Ben A. Bailey-Elkin ; Robert C. M. Knaap ; Garrett G. Johnson ; Tim J. Dalebout ; Dennis K. Ninaber ; Puck B. Van Kasteren ; Peter J. Bredenbeek ; Eric J. Snijder ; Marjolein Kikkert ; Brian L. MarkSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2014.
Abstract
Url:
DOI: 10.1074/jbc.M114.609644
PubMed: 25320088
PubMed Central: 4263872
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PMC:4263872Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Crystal Structure of the Middle East Respiratory Syndrome Coronavirus
(MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted
Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune
Suppression<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Bailey Elkin, Ben A" sort="Bailey Elkin, Ben A" uniqKey="Bailey Elkin B" first="Ben A." last="Bailey-Elkin">Ben A. Bailey-Elkin</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Knaap, Robert C M" sort="Knaap, Robert C M" uniqKey="Knaap R" first="Robert C. M." last="Knaap">Robert C. M. Knaap</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Johnson, Garrett G" sort="Johnson, Garrett G" uniqKey="Johnson G" first="Garrett G." last="Johnson">Garrett G. Johnson</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Dalebout, Tim J" sort="Dalebout, Tim J" uniqKey="Dalebout T" first="Tim J." last="Dalebout">Tim J. Dalebout</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Ninaber, Dennis K" sort="Ninaber, Dennis K" uniqKey="Ninaber D" first="Dennis K." last="Ninaber">Dennis K. Ninaber</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Van Kasteren, Puck B" sort="Van Kasteren, Puck B" uniqKey="Van Kasteren P" first="Puck B." last="Van Kasteren">Puck B. Van Kasteren</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Bredenbeek, Peter J" sort="Bredenbeek, Peter J" uniqKey="Bredenbeek P" first="Peter J." last="Bredenbeek">Peter J. Bredenbeek</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J." last="Snijder">Eric J. Snijder</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Kikkert, Marjolein" sort="Kikkert, Marjolein" uniqKey="Kikkert M" first="Marjolein" last="Kikkert">Marjolein Kikkert</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Mark, Brian L" sort="Mark, Brian L" uniqKey="Mark B" first="Brian L." last="Mark">Brian L. Mark</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25320088</idno><idno type="pmc">4263872</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263872</idno><idno type="RBID">PMC:4263872</idno><idno type="doi">10.1074/jbc.M114.609644</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">000D86</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D86</idno><idno type="wicri:Area/Pmc/Curation">000D86</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000D86</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Crystal Structure of the Middle East Respiratory Syndrome Coronavirus
(MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted
Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune
Suppression<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Bailey Elkin, Ben A" sort="Bailey Elkin, Ben A" uniqKey="Bailey Elkin B" first="Ben A." last="Bailey-Elkin">Ben A. Bailey-Elkin</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Knaap, Robert C M" sort="Knaap, Robert C M" uniqKey="Knaap R" first="Robert C. M." last="Knaap">Robert C. M. Knaap</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Johnson, Garrett G" sort="Johnson, Garrett G" uniqKey="Johnson G" first="Garrett G." last="Johnson">Garrett G. Johnson</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Dalebout, Tim J" sort="Dalebout, Tim J" uniqKey="Dalebout T" first="Tim J." last="Dalebout">Tim J. Dalebout</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Ninaber, Dennis K" sort="Ninaber, Dennis K" uniqKey="Ninaber D" first="Dennis K." last="Ninaber">Dennis K. Ninaber</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Van Kasteren, Puck B" sort="Van Kasteren, Puck B" uniqKey="Van Kasteren P" first="Puck B." last="Van Kasteren">Puck B. Van Kasteren</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Bredenbeek, Peter J" sort="Bredenbeek, Peter J" uniqKey="Bredenbeek P" first="Peter J." last="Bredenbeek">Peter J. Bredenbeek</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J." last="Snijder">Eric J. Snijder</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Kikkert, Marjolein" sort="Kikkert, Marjolein" uniqKey="Kikkert M" first="Marjolein" last="Kikkert">Marjolein Kikkert</name><affiliation><nlm:aff id="aff2"></nlm:aff></affiliation></author><author><name sortKey="Mark, Brian L" sort="Mark, Brian L" uniqKey="Mark B" first="Brian L." last="Mark">Brian L. Mark</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> MERS-CoV papain-like protease (PL<sup>pro</sup>)
processes viral polyproteins and has deubiquitinating activity.</p><p><bold>Results:</bold> A crystal structure of MERS-CoV PL<sup>pro</sup> bound to
ubiquitin guided mutagenesis to disrupt PL<sup>pro</sup> deubiquitinating
activity without affecting polyprotein cleavage.</p><p><bold>Conclusion:</bold> The deubiquitinating activity of MERS-CoV
PL<sup>pro</sup> suppresses the induction of interferon-β
expression.</p><p><bold>Significance:</bold> Our strategy to selectively disable PL<sup>pro</sup>deubiquitinating activity enables the study of its specific functions in
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<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id><journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id><journal-id journal-id-type="publisher-id">J. Biol. Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular
Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25320088</article-id><article-id pub-id-type="pmc">4263872</article-id><article-id pub-id-type="publisher-id">M114.609644</article-id><article-id pub-id-type="doi">10.1074/jbc.M114.609644</article-id><article-categories><subj-group subj-group-type="heading"><subject>Microbiology</subject></subj-group></article-categories><title-group><article-title>Crystal Structure of the Middle East Respiratory Syndrome Coronavirus
(MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted
Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune
Suppression<xref ref-type="fn" rid="FN1">*</xref></article-title><alt-title alt-title-type="short">MERS-CoV PL<sup>pro</sup>·Ub Crystal
Structure and Immune Antagonism</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Bailey-Elkin</surname><given-names>Ben A.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN2"><sup>1</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Knaap</surname><given-names>Robert C. M.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>2</sup></xref></contrib><contrib contrib-type="author"><name><surname>Johnson</surname><given-names>Garrett G.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref></contrib><contrib contrib-type="author"><name><surname>Dalebout</surname><given-names>Tim J.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Ninaber</surname><given-names>Dennis K.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>van Kasteren</surname><given-names>Puck B.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Bredenbeek</surname><given-names>Peter J.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Snijder</surname><given-names>Eric J.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Kikkert</surname><given-names>Marjolein</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref><xref ref-type="author-notes" rid="FN4"><sup>3</sup></xref><xref ref-type="corresp" rid="cor1"><sup>4</sup></xref></contrib><contrib contrib-type="author"><name><surname>Mark</surname><given-names>Brian L.</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN4"><sup>3</sup></xref><xref ref-type="corresp" rid="cor2"><sup>5</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Department of Microbiology, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada and</aff><aff id="aff2">the<label>§</label>Molecular Virology Laboratory, Department of Medical Microbiology, Leiden University Medical Center, 2333 ZA Leiden, The Netherlands</aff></contrib-group><author-notes><corresp id="cor1"><label>4</label> To whom correspondence may be addressed. Tel.:
<phone>31-71-526-1442</phone>; Fax: <fax>31-71-526-6981</fax>; E-mail:
<email>m.kikkert@lumc.nl</email>.</corresp><corresp id="cor2"><label>5</label> Holder of a Manitoba Research Chair award. To
whom correspondence may be addressed. Tel.: <phone>204-480-1430</phone>; Fax:
<fax>204-474-7603</fax>; E-mail:
<email>brian.mark@umanitoba.ca</email>.</corresp><fn fn-type="other" id="FN2"><label>1</label><p>Recipient of a Research Manitoba Studentship.</p></fn><fn fn-type="equal" id="FN3"><label>2</label><p>Both authors contributed equally to this work.</p></fn><fn fn-type="equal" id="FN4"><label>3</label><p>Both authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>12</day><month>12</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>15</day><month>10</month><year>2014</year></pub-date><volume>289</volume><issue>50</issue><fpage>34667</fpage><lpage>34682</lpage><history><date date-type="received"><day>3</day><month>9</month><year>2014</year></date><date date-type="rev-recd"><day>30</day><month>9</month><year>2014</year></date></history><permissions><copyright-statement>© 2014 by The American Society for Biochemistry and
Molecular Biology, Inc.</copyright-statement><copyright-year>2014</copyright-year><license><license-p>This article is made available via the PMC Open Access Subset for
unrestricted re-use and analyses in any form or by any means with
acknowledgement of the original source. These permissions are granted for
the duration of the COVID-19 pandemic or until permissions are revoked in
writing. Upon expiration of these permissions, PMC is granted a perpetual
license to make this article available via PMC and Europe PMC, consistent
with existing copyright protections.</license-p></license></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc05014034667.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> MERS-CoV papain-like protease (PL<sup>pro</sup>)
processes viral polyproteins and has deubiquitinating activity.</p><p><bold>Results:</bold> A crystal structure of MERS-CoV PL<sup>pro</sup> bound to
ubiquitin guided mutagenesis to disrupt PL<sup>pro</sup> deubiquitinating
activity without affecting polyprotein cleavage.</p><p><bold>Conclusion:</bold> The deubiquitinating activity of MERS-CoV
PL<sup>pro</sup> suppresses the induction of interferon-β
expression.</p><p><bold>Significance:</bold> Our strategy to selectively disable PL<sup>pro</sup>deubiquitinating activity enables the study of its specific functions in
infection.</p></abstract><abstract><p>Middle East respiratory syndrome coronavirus (MERS-CoV) is a newly emerging human
pathogen that was first isolated in 2012. MERS-CoV replication depends in part
on a virus-encoded papain-like protease (PL<sup>pro</sup>) that cleaves the
viral replicase polyproteins at three sites releasing non-structural protein 1
(nsp1), nsp2, and nsp3. In addition to this replicative function, MERS-CoV
PL<sup>pro</sup> was recently shown to be a deubiquitinating enzyme (DUB)
and to possess deISGylating activity, as previously reported for other
coronaviral PL<sup>pro</sup> domains, including that of severe acute respiratory
syndrome coronavirus. These activities have been suggested to suppress host
antiviral responses during infection. To understand the molecular basis for
ubiquitin (Ub) recognition and deconjugation by MERS-CoV PL<sup>pro</sup>, we
determined its crystal structure in complex with Ub. Guided by this structure,
mutations were introduced into PL<sup>pro</sup> to specifically disrupt Ub
binding without affecting viral polyprotein cleavage, as determined using an in
<italic>trans</italic> nsp3↓4 cleavage assay. Having developed a
strategy to selectively disable PL<sup>pro</sup> DUB activity, we were able to
specifically examine the effects of this activity on the innate immune response.
Whereas the wild-type PL<sup>pro</sup> domain was found to suppress
IFN-β promoter activation, PL<sup>pro</sup> variants specifically
lacking DUB activity were no longer able to do so. These findings directly
implicate the DUB function of PL<sup>pro</sup>, and not its proteolytic activity
<italic>per se</italic>, in the inhibition of IFN-β promoter
activity. The ability to decouple the DUB activity of PL<sup>pro</sup> from its
role in viral polyprotein processing now provides an approach to further dissect
the role(s) of PL<sup>pro</sup> as a viral DUB during MERS-CoV infection.</p></abstract><kwd-group><kwd>Cysteine Protease</kwd><kwd>Deubiquitylation (Deubiquitination)</kwd><kwd>Innate Immunity</kwd><kwd>Structural Biology</kwd><kwd>Viral Immunology</kwd><kwd>X-ray Crystallography</kwd><kwd>Middle East Respiratory Syndrome Coronavirus</kwd><kwd>PLpro</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= Crystal Structure of the Middle East Respiratory Syndrome Coronavirus
(MERS-CoV) Papain-like Protease Bound to Ubiquitin Facilitates Targeted
Disruption of Deubiquitinating Activity to Demonstrate Its Role in Innate Immune
Suppression*
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