MersV1, PubMed, Checkpoint, bibRecord, 000B16

Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism.

Identifieur interne : 000B16 ( PubMed/Checkpoint ); précédent : 000B15; suivant : 000B17

Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism.

Auteurs : Maria Batool [Corée du Sud] ; Masaud Shah [Corée du Sud] ; Mahesh Chandra Patra [Corée du Sud] ; Dhanusha Yesudhas [Corée du Sud] ; Sangdun Choi [Corée du Sud]

Source :

Scientific reports [ 2045-2322 ] ; 2017.

RBID : pubmed:28900197

Descripteurs français

KwdFr :
- ARN double brin (génétique), ARN double brin (métabolisme), ARN viral (génétique), ARN viral (métabolisme), Conformation moléculaire, Coronavirus du syndrome respiratoire du Moyen-Orient (physiologie), Infections à coronavirus (virologie), Liaison aux protéines, Liaison hydrogène, Modèles moléculaires, Mutagenèse, Protéines virales (métabolisme), Relation structure-activité, Séquence d'acides aminés.
MESH :
- génétique : ARN double brin, ARN viral.
- métabolisme : ARN double brin, ARN viral, Protéines virales.
- physiologie : Coronavirus du syndrome respiratoire du Moyen-Orient.
- virologie : Infections à coronavirus.
- Conformation moléculaire, Liaison aux protéines, Liaison hydrogène, Modèles moléculaires, Mutagenèse, Relation structure-activité, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence, Coronavirus Infections (virology), Hydrogen Bonding, Middle East Respiratory Syndrome Coronavirus (physiology), Models, Molecular, Molecular Conformation, Mutagenesis, Protein Binding, RNA, Double-Stranded (genetics), RNA, Double-Stranded (metabolism), RNA, Viral (genetics), RNA, Viral (metabolism), Structure-Activity Relationship, Viral Proteins (metabolism).
MESH :
- chemical , genetics : RNA, Double-Stranded, RNA, Viral.
- chemical , metabolism : RNA, Double-Stranded, RNA, Viral, Viral Proteins.
- physiology : Middle East Respiratory Syndrome Coronavirus.
- virology : Coronavirus Infections.
- Amino Acid Sequence, Hydrogen Bonding, Models, Molecular, Molecular Conformation, Mutagenesis, Protein Binding, Structure-Activity Relationship.

Abstract

Middle East respiratory syndrome coronavirus (MERS-CoV) has evolved to navigate through the sophisticated network of a host's immune system. The immune evasion mechanism including type 1 interferon and protein kinase R-mediated antiviral stress responses has been recently attributed to the involvement of MERS-CoV protein 4a (p4a) that masks the viral dsRNA. However, the structural mechanism of how p4a recognizes and establishes contacts with dsRNA is not well explained. In this study, we report a dynamic mechanism deployed by p4a to engage the viral dsRNA and make it unavailable to the host immune system. Multiple variants of p4a-dsRNA were created and investigated through extensive molecular dynamics procedures to highlight crucial interfacial residues that may be used as potential pharmacophores for future drug development. The structural analysis revealed that p4a exhibits a typical αβββα fold structure, as found in other dsRNA-binding proteins. The α1 helix and the β1-β2 loop play a crucial role in recognizing and establishing contacts with the minor grooves of dsRNA. Further, mutational and binding free energy analyses suggested that in addition to K63 and K67, two other residues, K27 and W45, might also be crucial for p4a-dsRNA stability.

DOI: 10.1038/s41598-017-11736-6
PubMed: 28900197

Affiliations:

Corée du Sud

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000B57
to stream PubMed, to step Curation: 000B57

Links to Exploration step

pubmed:28900197

Le document en format XML

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<front><div type="abstract" xml:lang="en">Middle East respiratory syndrome coronavirus (MERS-CoV) has evolved to navigate through the sophisticated network of a host's immune system. The immune evasion mechanism including type 1 interferon and protein kinase R-mediated antiviral stress responses has been recently attributed to the involvement of MERS-CoV protein 4a (p4a) that masks the viral dsRNA. However, the structural mechanism of how p4a recognizes and establishes contacts with dsRNA is not well explained. In this study, we report a dynamic mechanism deployed by p4a to engage the viral dsRNA and make it unavailable to the host immune system. Multiple variants of p4a-dsRNA were created and investigated through extensive molecular dynamics procedures to highlight crucial interfacial residues that may be used as potential pharmacophores for future drug development. The structural analysis revealed that p4a exhibits a typical αβββα fold structure, as found in other dsRNA-binding proteins. The α1 helix and the β1-β2 loop play a crucial role in recognizing and establishing contacts with the minor grooves of dsRNA. Further, mutational and binding free energy analyses suggested that in addition to K63 and K67, two other residues, K27 and W45, might also be crucial for p4a-dsRNA stability.</div>
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Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism.

Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism.

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