Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase
Identifieur interne : 001251 ( Pmc/Curation ); précédent : 001250; suivant : 001252Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase
Auteurs : Adeyemi O. Adedeji ; Hilary LazarusSource :
- mSphere [ 2379-5042 ] ; 2016.
Abstract
Coronaviruses are known to cause a wide range of diseases in humans and animals. Middle East respiratory syndrome coronavirus (MERS-CoV) is a novel coronavirus discovered in 2012 and is responsible for acute respiratory syndrome in humans in the Middle East, Europe, North Africa, and the United States of America. Helicases are motor proteins that catalyze the processive separation of double-stranded nucleic acids into two single-stranded nucleic acids by utilizing the energy derived from ATP hydrolysis. MERS-CoV helicase is one of the most important viral replication enzymes of this coronavirus. Herein, we report the first bacterial expression, enzyme purification, and biochemical characterization of MERS-CoV helicase. The knowledge obtained from this study might be used to identify an inhibitor of MERS-CoV replication, and the helicase might be used as a therapeutic target.
Url:
DOI: 10.1128/mSphere.00235-16
PubMed: 27631026
PubMed Central: 5014916
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase</title><author><name sortKey="Adedeji, Adeyemi O" sort="Adedeji, Adeyemi O" uniqKey="Adedeji A" first="Adeyemi O." last="Adedeji">Adeyemi O. Adedeji</name></author><author><name sortKey="Lazarus, Hilary" sort="Lazarus, Hilary" uniqKey="Lazarus H" first="Hilary" last="Lazarus">Hilary Lazarus</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">27631026</idno><idno type="pmc">5014916</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5014916</idno><idno type="RBID">PMC:5014916</idno><idno type="doi">10.1128/mSphere.00235-16</idno><date when="2016">2016</date><idno type="wicri:Area/Pmc/Corpus">001251</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001251</idno><idno type="wicri:Area/Pmc/Curation">001251</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001251</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase</title><author><name sortKey="Adedeji, Adeyemi O" sort="Adedeji, Adeyemi O" uniqKey="Adedeji A" first="Adeyemi O." last="Adedeji">Adeyemi O. Adedeji</name></author><author><name sortKey="Lazarus, Hilary" sort="Lazarus, Hilary" uniqKey="Lazarus H" first="Hilary" last="Lazarus">Hilary Lazarus</name></author></analytic><series><title level="j">mSphere</title><idno type="eISSN">2379-5042</idno><imprint><date when="2016">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Coronaviruses are known to cause a wide range of diseases in humans and animals. Middle East respiratory syndrome coronavirus (MERS-CoV) is a novel coronavirus discovered in 2012 and is responsible for acute respiratory syndrome in humans in the Middle East, Europe, North Africa, and the United States of America. Helicases are motor proteins that catalyze the processive separation of double-stranded nucleic acids into two single-stranded nucleic acids by utilizing the energy derived from ATP hydrolysis. MERS-CoV helicase is one of the most important viral replication enzymes of this coronavirus. Herein, we report the first bacterial expression, enzyme purification, and biochemical characterization of MERS-CoV helicase. The knowledge obtained from this study might be used to identify an inhibitor of MERS-CoV replication, and the helicase might be used as a therapeutic target.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Adedeji, Ao" uniqKey="Adedeji A">AO Adedeji</name></author><author><name sortKey="Singh, K" uniqKey="Singh K">K Singh</name></author><author><name sortKey="Kassim, A" uniqKey="Kassim A">A Kassim</name></author><author><name sortKey="Coleman, Cm" uniqKey="Coleman C">CM Coleman</name></author><author><name sortKey="Elliott, R" uniqKey="Elliott R">R Elliott</name></author><author><name sortKey="Weiss, Sr" uniqKey="Weiss S">SR Weiss</name></author><author><name sortKey="Frieman, Mb" uniqKey="Frieman M">MB Frieman</name></author><author><name sortKey="Sarafianos, Sg" uniqKey="Sarafianos S">SG Sarafianos</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Raj, Vs" uniqKey="Raj V">VS 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<front><journal-meta><journal-id journal-id-type="nlm-ta">mSphere</journal-id><journal-id journal-id-type="iso-abbrev">mSphere</journal-id><journal-id journal-id-type="hwp">msph</journal-id><journal-id journal-id-type="pmc">msph</journal-id><journal-id journal-id-type="publisher-id">mSphere</journal-id><journal-title-group><journal-title>mSphere</journal-title></journal-title-group><issn pub-type="epub">2379-5042</issn><publisher><publisher-name>American Society for Microbiology</publisher-name><publisher-loc>1752 N St., N.W., Washington, DC</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">27631026</article-id><article-id pub-id-type="pmc">5014916</article-id><article-id pub-id-type="publisher-id">mSphere00235-16</article-id><article-id pub-id-type="doi">10.1128/mSphere.00235-16</article-id><article-categories><subj-group subj-group-type="heading"><subject>Research Article</subject><subj-group><subject>Molecular Biology and Physiology</subject></subj-group></subj-group></article-categories><title-group><article-title>Biochemical Characterization of Middle East Respiratory Syndrome Coronavirus Helicase</article-title><alt-title alt-title-type="running-head">Biochemical Characterization of MERS-CoV Helicase</alt-title><alt-title alt-title-type="short-authors">Adedeji and Lazarus</alt-title></title-group><contrib-group><contrib contrib-type="author" corresp="yes"><name><surname>Adedeji</surname><given-names>Adeyemi O.</given-names></name></contrib><contrib contrib-type="author"><name><surname>Lazarus</surname><given-names>Hilary</given-names></name></contrib><aff>Department of Pathology and Population Medicine, College of Veterinary Medicine, Midwestern University, Glendale, Arizona, USA</aff></contrib-group><contrib-group><contrib contrib-type="editor"><name><surname>Frieman</surname><given-names>Matthew B.</given-names></name><role>Editor</role><aff>University of Maryland</aff></contrib></contrib-group><author-notes><corresp id="cor1">Address correspondence to Adeyemi O. Adedeji, <email>aadede@midwestern.edu</email>.</corresp><fn fn-type="other"><p><bold>Citation</bold> Adedeji AO, Lazarus H. 2016. Biochemical characterization of Middle East respiratory syndrome coronavirus helicase. mSphere 1(5):e00235-16. doi:<ext-link ext-link-type="uri" xlink:href="http://dx.doi.org/10.1128/mSphere.00235-16">10.1128/mSphere.00235-16</ext-link>.</p></fn></author-notes><pub-date pub-type="epub"><day>7</day><month>9</month><year>2016</year></pub-date><pub-date pub-type="collection"><season>Sep-Oct</season><year>2016</year></pub-date><volume>1</volume><issue>5</issue><elocation-id>e00235-16</elocation-id><history><date date-type="received"><day>12</day><month>8</month><year>2016</year></date><date date-type="accepted"><day>19</day><month>8</month><year>2016</year></date></history><permissions><copyright-statement>Copyright © 2016 Adedeji and Lazarus.</copyright-statement><copyright-year>2016</copyright-year><copyright-holder>Adedeji and Lazarus</copyright-holder><license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by/4.0/"><license-p>This is an open-access article distributed under the terms of the <ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by/4.0/">Creative Commons Attribution 4.0 International license</ext-link>.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="sph005162143001.pdf"></self-uri><abstract abstract-type="precis"><p>Coronaviruses are known to cause a wide range of diseases in humans and animals. Middle East respiratory syndrome coronavirus (MERS-CoV) is a novel coronavirus discovered in 2012 and is responsible for acute respiratory syndrome in humans in the Middle East, Europe, North Africa, and the United States of America. Helicases are motor proteins that catalyze the processive separation of double-stranded nucleic acids into two single-stranded nucleic acids by utilizing the energy derived from ATP hydrolysis. MERS-CoV helicase is one of the most important viral replication enzymes of this coronavirus. Herein, we report the first bacterial expression, enzyme purification, and biochemical characterization of MERS-CoV helicase. The knowledge obtained from this study might be used to identify an inhibitor of MERS-CoV replication, and the helicase might be used as a therapeutic target.</p></abstract><abstract><title>ABSTRACT</title><p>Middle East respiratory syndrome coronavirus (MERS-CoV) helicase is a superfamily 1 helicase containing seven conserved motifs. We have cloned, expressed, and purified a Strep-fused recombinant MERS-CoV nonstructural protein 13 (M-nsp13) helicase. Characterization of its biochemical properties showed that it unwound DNA and RNA similarly to severe acute respiratory syndrome CoV nsp13 (S-nsp13) helicase. We showed that M-nsp13 unwound in a 5′-to-3′ direction and efficiently unwound the partially duplex RNA substrates with a long loading strand relative to those of the RNA substrates with a short or no loading strand. Moreover, the <italic>K<sub>m</sub></italic> of ATP for M-nsp13 is inversely proportional to the length of the 5′ loading strand of the partially duplex RNA substrates. Finally, we also showed that the rate of unwinding (<italic>ku</italic>) of M-nsp13 is directly proportional to the length of the 5′ loading strand of the partially duplex RNA substrate. These results provide insights that enhance our understanding of the biochemical properties of M-nsp13.</p><p><bold>IMPORTANCE</bold> Coronaviruses are known to cause a wide range of diseases in humans and animals. Middle East respiratory syndrome coronavirus (MERS-CoV) is a novel coronavirus discovered in 2012 and is responsible for acute respiratory syndrome in humans in the Middle East, Europe, North Africa, and the United States of America. Helicases are motor proteins that catalyze the processive separation of double-stranded nucleic acids into two single-stranded nucleic acids by utilizing the energy derived from ATP hydrolysis. MERS-CoV helicase is one of the most important viral replication enzymes of this coronavirus. Herein, we report the first bacterial expression, enzyme purification, and biochemical characterization of MERS-CoV helicase. The knowledge obtained from this study might be used to identify an inhibitor of MERS-CoV replication, and the helicase might be used as a therapeutic target.</p></abstract><kwd-group><title>KEYWORDS:</title><kwd>ATP hydrolysis</kwd><kwd>DNA</kwd><kwd>RNA</kwd><kwd>coronavirus</kwd><kwd>enzyme kinetics</kwd><kwd>helicase</kwd></kwd-group><funding-group><award-group id="award1"><funding-source>Midwestern University New Investigator Start-Up Fund</funding-source><principal-award-recipient>Adeyemi O. Adedeji</principal-award-recipient></award-group></funding-group><counts><fig-count count="9"></fig-count><table-count count="2"></table-count><equation-count count="0"></equation-count><ref-count count="43"></ref-count><page-count count="14"></page-count><word-count count="7069"></word-count></counts><custom-meta-group><custom-meta><meta-name>cover-date</meta-name><meta-value>September/October 2016</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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