Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.
Identifieur interne : 000A47 ( PubMed/Checkpoint ); précédent : 000A46; suivant : 000A48Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication.
Auteurs : Yusuke Sakai [Japon] ; Kengo Kawachi [Japon] ; Yutaka Terada [Japon] ; Hiroko Omori [Japon] ; Yoshiharu Matsuura [Japon] ; Wataru Kamitani [Japon]Source :
- Virology [ 1096-0341 ] ; 2017.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Viral Nonstructural Proteins.
- genetics : SARS Virus.
- physiology : SARS Virus.
- Amino Acid Substitution, DNA Mutational Analysis, Protein Interaction Mapping, Virus Replication.
Abstract
Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.
DOI: 10.1016/j.virol.2017.07.019
PubMed: 28738245
Affiliations:
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<front><div type="abstract" xml:lang="en">Infection with coronavirus rearranges the host cell membrane to assemble a replication/transcription complex in which replication of the viral genome and transcription of viral mRNA occur. Although coexistence of nsp3 and nsp4 is known to cause membrane rearrangement, the mechanisms underlying the interaction of these two proteins remain unclear. We demonstrated that binding of nsp4 with nsp3 is essential for membrane rearrangement and identified amino acid residues in nsp4 responsible for the interaction with nsp3. In addition, we revealed that the nsp3-nsp4 interaction is not sufficient to induce membrane rearrangement, suggesting the participation of other factors such as host proteins. Finally, we showed that loss of the nsp3-nsp4 interaction eliminated viral replication by using an infectious cDNA clone and replicon system of SARS-CoV. These findings provide clues to the mechanism of the replication/transcription complex assembly of SARS-CoV and could reveal an antiviral target for the treatment of betacoronavirus infection.</div>
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<affiliations><list><country><li>Japon</li>
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<name sortKey="Matsuura, Yoshiharu" sort="Matsuura, Yoshiharu" uniqKey="Matsuura Y" first="Yoshiharu" last="Matsuura">Yoshiharu Matsuura</name>
<name sortKey="Omori, Hiroko" sort="Omori, Hiroko" uniqKey="Omori H" first="Hiroko" last="Omori">Hiroko Omori</name>
<name sortKey="Terada, Yutaka" sort="Terada, Yutaka" uniqKey="Terada Y" first="Yutaka" last="Terada">Yutaka Terada</name>
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