Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism
Identifieur interne : 000B76 ( Main/Exploration ); précédent : 000B75; suivant : 000B77Structural insights into the Middle East respiratory syndrome coronavirus 4a protein and its dsRNA binding mechanism
Auteurs : Maria Batool ; Masaud Shah ; Mahesh Chandra Patra ; Dhanusha Yesudhas ; Sangdun ChoiSource :
- Scientific Reports [ 2045-2322 ] ; 2017.
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.
Url:
DOI: 10.1038/s41598-017-11736-6
PubMed: 28900197
PubMed Central: 5596018
Affiliations:
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<front><div type="abstract" xml:lang="en"><p id="Par1">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.</p>
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<tree><noCountry><name sortKey="Batool, Maria" sort="Batool, Maria" uniqKey="Batool M" first="Maria" last="Batool">Maria Batool</name>
<name sortKey="Choi, Sangdun" sort="Choi, Sangdun" uniqKey="Choi S" first="Sangdun" last="Choi">Sangdun Choi</name>
<name sortKey="Patra, Mahesh Chandra" sort="Patra, Mahesh Chandra" uniqKey="Patra M" first="Mahesh Chandra" last="Patra">Mahesh Chandra Patra</name>
<name sortKey="Shah, Masaud" sort="Shah, Masaud" uniqKey="Shah M" first="Masaud" last="Shah">Masaud Shah</name>
<name sortKey="Yesudhas, Dhanusha" sort="Yesudhas, Dhanusha" uniqKey="Yesudhas D" first="Dhanusha" last="Yesudhas">Dhanusha Yesudhas</name>
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