Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease
Identifieur interne : 001844 ( Main/Exploration ); précédent : 001843; suivant : 001845Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease
Auteurs : Bo-Lin Ho ; Shu-Chun Cheng ; Lin Shi ; Ting-Yun Wang ; Kuan-I Ho ; Chi-Yuan ChouSource :
- PLoS ONE [ 1932-6203 ] ; 2015.
Descripteurs français
- KwdFr :
- Analyse de séquence de protéine, Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (enzymologie), Cristallographie aux rayons X, Modèles moléculaires, Multimérisation de protéines, Papaïne (), Papaïne (métabolisme), Peptide hydrolases (), Peptide hydrolases (métabolisme), Protéines virales (), Protéines virales (analyse).
- MESH :
- analyse : Protéines virales.
- enzymologie : Coronavirus du syndrome respiratoire du Moyen-Orient.
- métabolisme : Papaïne, Peptide hydrolases.
- Analyse de séquence de protéine, Coronavirus du syndrome respiratoire du Moyen-Orient, Cristallographie aux rayons X, Modèles moléculaires, Multimérisation de protéines, Papaïne, Peptide hydrolases, Protéines virales.
English descriptors
- KwdEn :
- Crystallography, X-Ray, Middle East Respiratory Syndrome Coronavirus (chemistry), Middle East Respiratory Syndrome Coronavirus (enzymology), Models, Molecular, Papain (chemistry), Papain (metabolism), Peptide Hydrolases (chemistry), Peptide Hydrolases (metabolism), Protein Multimerization, Sequence Analysis, Protein, Viral Proteins (analysis), Viral Proteins (chemistry).
- MESH :
- chemical , analysis : Viral Proteins.
- chemical , chemistry : Papain, Peptide Hydrolases, Viral Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus.
- enzymology : Middle East Respiratory Syndrome Coronavirus.
- chemical , metabolism : Papain, Peptide Hydrolases.
- Crystallography, X-Ray, Models, Molecular, Protein Multimerization, Sequence Analysis, Protein.
Abstract
A highly pathogenic human coronavirus (CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), has emerged in Jeddah and other places in Saudi Arabia, and has quickly spread to European and Asian countries since September 2012. Up to the 1st October 2015 it has infected at least 1593 people with a global fatality rate of about 35%. Studies to understand the virus are necessary and urgent. In the present study, MERS-CoV main protease (Mpro) is expressed; the dimerization of the protein and its relationship to catalysis are investigated.
The crystal structure of MERS-CoV Mpro indicates that it shares a similar scaffold to that of other coronaviral Mpro and consists of chymotrypsin-like domains I and II and a helical domain III of five helices. Analytical ultracentrifugation analysis demonstrated that MERS-CoV Mpro undergoes a monomer to dimer conversion in the presence of a peptide substrate. Glu169 is a key residue and plays a dual role in both dimerization and catalysis. The mutagenesis of other residues found on the dimerization interface indicate that dimerization of MERS-CoV Mpro is required for its catalytic activity. One mutation, M298R, resulted in a stable dimer with a higher level of proteolytic activity than the wild-type enzyme.
MERS-CoV Mpro shows substrate-induced dimerization and potent proteolytic activity. A critical assessment of the residues important to these processes provides insights into the correlation between dimerization and catalysis within the coronaviral Mpro family.
Url:
DOI: 10.1371/journal.pone.0144865
PubMed: 26658006
PubMed Central: 4682845
Affiliations:
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K" first="Kuan-I" last="Ho">Kuan-I Ho</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">26658006</idno><idno type="pmc">4682845</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4682845</idno><idno type="RBID">PMC:4682845</idno><idno type="doi">10.1371/journal.pone.0144865</idno><date when="2015">2015</date><idno type="wicri:Area/Pmc/Corpus">001016</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001016</idno><idno type="wicri:Area/Pmc/Curation">001016</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001016</idno><idno type="wicri:Area/Pmc/Checkpoint">000E80</idno><idno type="wicri:explorRef" 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Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease</title><author><name sortKey="Ho, Bo Lin" sort="Ho, Bo Lin" uniqKey="Ho B" first="Bo-Lin" last="Ho">Bo-Lin Ho</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Cheng, Shu Chun" sort="Cheng, Shu Chun" uniqKey="Cheng S" first="Shu-Chun" last="Cheng">Shu-Chun Cheng</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Shi, Lin" sort="Shi, Lin" uniqKey="Shi L" first="Lin" last="Shi">Lin Shi</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Wang, Ting Yun" sort="Wang, Ting Yun" uniqKey="Wang T" first="Ting-Yun" last="Wang">Ting-Yun Wang</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Ho, Kuan I" sort="Ho, Kuan I" uniqKey="Ho K" first="Kuan-I" last="Ho">Kuan-I Ho</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author><author><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name><affiliation><nlm:aff id="aff001"></nlm:aff></affiliation></author></analytic><series><title level="j">PLoS ONE</title><idno type="eISSN">1932-6203</idno><imprint><date when="2015">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Crystallography, X-Ray</term><term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term><term>Middle East Respiratory Syndrome Coronavirus (enzymology)</term><term>Models, Molecular</term><term>Papain (chemistry)</term><term>Papain (metabolism)</term><term>Peptide Hydrolases (chemistry)</term><term>Peptide Hydrolases (metabolism)</term><term>Protein Multimerization</term><term>Sequence Analysis, Protein</term><term>Viral Proteins (analysis)</term><term>Viral Proteins (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Analyse de séquence de protéine</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient ()</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient (enzymologie)</term><term>Cristallographie aux rayons X</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Papaïne ()</term><term>Papaïne (métabolisme)</term><term>Peptide hydrolases ()</term><term>Peptide hydrolases (métabolisme)</term><term>Protéines virales ()</term><term>Protéines virales (analyse)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Papain</term><term>Peptide Hydrolases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Protéines virales</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Papain</term><term>Peptide Hydrolases</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Papaïne</term><term>Peptide hydrolases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Crystallography, X-Ray</term><term>Models, Molecular</term><term>Protein Multimerization</term><term>Sequence Analysis, Protein</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Analyse de séquence de protéine</term><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term><term>Cristallographie aux rayons X</term><term>Modèles moléculaires</term><term>Multimérisation de protéines</term><term>Papaïne</term><term>Peptide hydrolases</term><term>Protéines virales</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec id="sec001"><title>Background</title><p>A highly pathogenic human coronavirus (CoV), Middle East respiratory syndrome coronavirus (MERS-CoV), has emerged in Jeddah and other places in Saudi Arabia, and has quickly spread to European and Asian countries since September 2012. Up to the 1<sup>st</sup> October 2015 it has infected at least 1593 people with a global fatality rate of about 35%. Studies to understand the virus are necessary and urgent. In the present study, MERS-CoV main protease (M<sup>pro</sup>) is expressed; the dimerization of the protein and its relationship to catalysis are investigated.</p></sec><sec id="sec002"><title>Methods and Results</title><p>The crystal structure of MERS-CoV M<sup>pro</sup> indicates that it shares a similar scaffold to that of other coronaviral M<sup>pro</sup> and consists of chymotrypsin-like domains I and II and a helical domain III of five helices. Analytical ultracentrifugation analysis demonstrated that MERS-CoV M<sup>pro</sup> undergoes a monomer to dimer conversion in the presence of a peptide substrate. Glu169 is a key residue and plays a dual role in both dimerization and catalysis. The mutagenesis of other residues found on the dimerization interface indicate that dimerization of MERS-CoV M<sup>pro</sup> is required for its catalytic activity. One mutation, M298R, resulted in a stable dimer with a higher level of proteolytic activity than the wild-type enzyme.</p></sec><sec id="sec003"><title>Conclusions</title><p>MERS-CoV M<sup>pro</sup> shows substrate-induced dimerization and potent proteolytic activity. A critical assessment of the residues important to these processes provides insights into the correlation between dimerization and catalysis within the coronaviral M<sup>pro</sup> family.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Zaki, Am" uniqKey="Zaki A">AM Zaki</name></author><author><name sortKey="Van Boheemen, S" uniqKey="Van Boheemen S">S van Boheemen</name></author><author><name sortKey="Bestebroer, Tm" uniqKey="Bestebroer T">TM Bestebroer</name></author><author><name sortKey="Osterhaus, Ad" uniqKey="Osterhaus A">AD Osterhaus</name></author><author><name sortKey="Fouchier, Ra" uniqKey="Fouchier R">RA Fouchier</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Chan, Jf" uniqKey="Chan J">JF Chan</name></author><author><name sortKey="Li, Ks" uniqKey="Li K">KS Li</name></author><author><name sortKey="To, Kk" uniqKey="To K">KK To</name></author><author><name sortKey="Cheng, Vc" 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sortKey="Hsieh, Hp" uniqKey="Hsieh H">HP Hsieh</name></author><author><name sortKey="Turk, B" uniqKey="Turk B">B Turk</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Zhang, S" uniqKey="Zhang S">S Zhang</name></author><author><name sortKey="Zhong, N" uniqKey="Zhong N">N Zhong</name></author><author><name sortKey="Xue, F" uniqKey="Xue F">F Xue</name></author><author><name sortKey="Kang, X" uniqKey="Kang X">X Kang</name></author><author><name sortKey="Ren, X" uniqKey="Ren X">X Ren</name></author><author><name sortKey="Chen, J" uniqKey="Chen J">J Chen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Gouet, P" uniqKey="Gouet P">P Gouet</name></author><author><name sortKey="Courcelle, E" uniqKey="Courcelle E">E Courcelle</name></author><author><name sortKey="Stuart, Di" uniqKey="Stuart D">DI Stuart</name></author><author><name sortKey="Metoz, F" uniqKey="Metoz F">F Metoz</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list></list><tree><noCountry><name sortKey="Cheng, Shu Chun" sort="Cheng, Shu Chun" uniqKey="Cheng S" first="Shu-Chun" last="Cheng">Shu-Chun Cheng</name><name sortKey="Chou, Chi Yuan" sort="Chou, Chi Yuan" uniqKey="Chou C" first="Chi-Yuan" last="Chou">Chi-Yuan Chou</name><name sortKey="Ho, Bo Lin" sort="Ho, Bo Lin" uniqKey="Ho B" first="Bo-Lin" last="Ho">Bo-Lin Ho</name><name sortKey="Ho, Kuan I" sort="Ho, Kuan I" uniqKey="Ho K" first="Kuan-I" last="Ho">Kuan-I Ho</name><name sortKey="Shi, Lin" sort="Shi, Lin" uniqKey="Shi L" first="Lin" last="Shi">Lin Shi</name><name sortKey="Wang, Ting Yun" sort="Wang, Ting Yun" uniqKey="Wang T" first="Ting-Yun" last="Wang">Ting-Yun Wang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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