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Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease.

Identifieur interne : 001350 ( PubMed/Curation ); précédent : 001349; suivant : 001351

Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease.

Auteurs : Bo-Lin Ho [Taïwan] ; Shu-Chun Cheng [Taïwan] ; Lin Shi [Taïwan] ; Ting-Yun Wang [Taïwan] ; Kuan-I Ho [Taïwan] ; Chi-Yuan Chou [Taïwan]

Source :

PloS one [ 1932-6203 ] ; 2015.

RBID : pubmed:26658006

Descripteurs français

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.

DOI: 10.1371/journal.pone.0144865
PubMed: 26658006

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<front><div type="abstract" xml:lang="en">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.</div>
</front>
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<Month>08</Month>
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<ArticleTitle>Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease.</ArticleTitle>
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<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">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.</AbstractText>
<AbstractText Label="METHODS AND RESULTS" NlmCategory="RESULTS">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.</AbstractText>
<AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">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.</AbstractText>
</Abstract>
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<AffiliationInfo><Affiliation>Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan.</Affiliation>
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<ForeName>Ting-Yun</ForeName>
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<ForeName>Kuan-I</ForeName>
<Initials>KI</Initials>
<AffiliationInfo><Affiliation>Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan.</Affiliation>
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<Author ValidYN="Y"><LastName>Chou</LastName>
<ForeName>Chi-Yuan</ForeName>
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Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease.

Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease.

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