SrasV1, Main, Exploration, bibRecord, 000C35

Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus

Identifieur interne : 000C35 ( Main/Exploration ); précédent : 000C34; suivant : 000C36

Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus

Auteurs : Lianqi Zhang [République populaire de Chine] ; Lei Li [République populaire de Chine] ; Liming Yan [République populaire de Chine] ; Zhenhua Ming [République populaire de Chine] ; Zhihui Jia [République populaire de Chine] ; Zhiyong Lou [République populaire de Chine] ; Zihe Rao [République populaire de Chine]

Source :

Journal of Virology [ 0022-538X ] ; 2018.

RBID : PMC:6206473

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Crystallography, X-Ray, Endoribonucleases (chemistry), Endoribonucleases (genetics), Humans, Middle East Respiratory Syndrome Coronavirus (genetics), Protein Multimerization, RNA Replicase (chemistry), RNA Replicase (genetics), RNA-Binding Proteins (chemistry), RNA-Binding Proteins (genetics), Sequence Alignment, Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Virus Replication.
MESH :
- chemical , chemistry : Endoribonucleases, RNA Replicase, RNA-Binding Proteins, Viral Nonstructural Proteins.
- chemical , genetics : Endoribonucleases, RNA Replicase, RNA-Binding Proteins, Viral Nonstructural Proteins.
- genetics : Middle East Respiratory Syndrome Coronavirus.
- Amino Acid Sequence, Crystallography, X-Ray, Humans, Protein Multimerization, Sequence Alignment, Virus Replication.

Abstract

The lethally pathogenic Middle East respiratory syndrome coronavirus (MERS-CoV) and the severe acute respiratory syndrome coronavirus (SARS-CoV) pose serious threats to humans. Endoribonuclease Nsp15 encoded by coronavirus plays an important role in viral infection and pathogenesis. This study determines the structure of MERS-CoV Nsp15 and demonstrates how the catalytic activity of this protein is potentially mediated, thereby providing structural and functional evidence for developing antiviral drugs. We also hypothesize that the primase-like protein Nsp8 and the Nsp7/Nsp8 complex may interact with Nsp15 and affect enzymatic activity. This contributes to the understanding of the association of Nsp15 with the viral replication and transcription machinery.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6206473

DOI: 10.1128/JVI.00893-18
PubMed: 30135128
PubMed Central: 6206473

Affiliations:

Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Crystallography, X-Ray</term>
<term>Endoribonucleases (chemistry)</term>
<term>Endoribonucleases (genetics)</term>
<term>Humans</term>
<term>Middle East Respiratory Syndrome Coronavirus (genetics)</term>
<term>Protein Multimerization</term>
<term>RNA Replicase (chemistry)</term>
<term>RNA Replicase (genetics)</term>
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<term>RNA-Binding Proteins (genetics)</term>
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<term>Viral Nonstructural Proteins (genetics)</term>
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<term>Cristallographie aux rayons X</term>
<term>Endoribonucleases ()</term>
<term>Endoribonucleases (génétique)</term>
<term>Humains</term>
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<term>Protéines de liaison à l'ARN ()</term>
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<term>RNA replicase (génétique)</term>
<term>Réplication virale</term>
<term>Séquence d'acides aminés</term>
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<term>RNA-Binding Proteins</term>
<term>Viral Nonstructural Proteins</term>
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<term>RNA-Binding Proteins</term>
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<front><div type="abstract" xml:lang="en"><p>The lethally pathogenic Middle East respiratory syndrome coronavirus (MERS-CoV) and the severe acute respiratory syndrome coronavirus (SARS-CoV) pose serious threats to humans. Endoribonuclease Nsp15 encoded by coronavirus plays an important role in viral infection and pathogenesis. This study determines the structure of MERS-CoV Nsp15 and demonstrates how the catalytic activity of this protein is potentially mediated, thereby providing structural and functional evidence for developing antiviral drugs. We also hypothesize that the primase-like protein Nsp8 and the Nsp7/Nsp8 complex may interact with Nsp15 and affect enzymatic activity. This contributes to the understanding of the association of Nsp15 with the viral replication and transcription machinery.</p>
</div>
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Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus

Structural and Biochemical Characterization of Endoribonuclease Nsp15 Encoded by Middle East Respiratory Syndrome Coronavirus

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