Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication
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 i...
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| Published in | Virology (New York, N.Y.) Vol. 510; pp. 165 - 174 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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Elsevier Inc
01.10.2017
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| 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.
•H120 and F121 in the lumenal loop in nsp4 are essential for binding to nsp3.•H120&F121 substitutions in nsp4 cause defect in membrane rearrangement function.•Interaction with nsp3 through H120&F121 in nsp4 is crucial for viral propagation. |
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| AbstractList | 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.
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H120 and F121 in the lumenal loop in nsp4 are essential for binding to nsp3.
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H120&F121 substitutions in nsp4 cause defect in membrane rearrangement function.
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Interaction with nsp3 through H120&F121 in nsp4 is crucial for viral propagation. 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. •H120 and F121 in the lumenal loop in nsp4 are essential for binding to nsp3.•H120&F121 substitutions in nsp4 cause defect in membrane rearrangement function.•Interaction with nsp3 through H120&F121 in nsp4 is crucial for viral propagation. 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.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. 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. |
| Author | Kamitani, Wataru Sakai, Yusuke Omori, Hiroko Terada, Yutaka Kawachi, Kengo Matsuura, Yoshiharu |
| AuthorAffiliation | d Laboratory of Veterinary Pathology, Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi, Japan e Tsukuba Primate Research Center, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan b Department of Molecular Virology, Osaka, Japan c Core Instrumentation Facility, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan a Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan |
| AuthorAffiliation_xml | – name: d Laboratory of Veterinary Pathology, Joint Faculty of Veterinary Medicine, Yamaguchi University, Yamaguchi, Japan – name: c Core Instrumentation Facility, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan – name: b Department of Molecular Virology, Osaka, Japan – name: a Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan – name: e Tsukuba Primate Research Center, National Institutes of Biomedical Innovation, Health and Nutrition, Tsukuba, Ibaraki 305-0843, Japan |
| Author_xml | – sequence: 1 givenname: Yusuke surname: Sakai fullname: Sakai, Yusuke organization: Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan – sequence: 2 givenname: Kengo surname: Kawachi fullname: Kawachi, Kengo organization: Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan – sequence: 3 givenname: Yutaka surname: Terada fullname: Terada, Yutaka organization: Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan – sequence: 4 givenname: Hiroko surname: Omori fullname: Omori, Hiroko organization: Core Instrumentation Facility, Research Institute for Microbial Diseases, Osaka University, Osaka, Japan – sequence: 5 givenname: Yoshiharu surname: Matsuura fullname: Matsuura, Yoshiharu organization: Department of Molecular Virology, Osaka, Japan – sequence: 6 givenname: Wataru surname: Kamitani fullname: Kamitani, Wataru email: wakamita@biken.osaka-u.ac.jp organization: Laboratory of Clinical Research on Infectious Diseases, Osaka, Japan |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/28738245$$D View this record in MEDLINE/PubMed |
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| Copyright | 2017 Elsevier Inc. Copyright © 2017 Elsevier Inc. All rights reserved. 2017 Elsevier Inc. 2017 Elsevier Inc. |
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| Keywords | Coronavirus Nsp4 Viral replication Severe acute respiratory syndrome |
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| Title | Two-amino acids change in the nsp4 of SARS coronavirus abolishes viral replication |
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