Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers
Abstract Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro...
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-07-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-06062-w |
| _version_ | 1819042863452782592 |
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| author | Yingying Cong Franziska Kriegenburg Cornelis A. M. de Haan Fulvio Reggiori |
| author_facet | Yingying Cong Franziska Kriegenburg Cornelis A. M. de Haan Fulvio Reggiori |
| author_sort | Yingying Cong |
| collection | DOAJ |
| description | Abstract Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs. |
| first_indexed | 2024-12-21T09:47:39Z |
| format | Article |
| id | doaj.art-1bd9db3283e34102b0ac19f4492e089d |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-21T09:47:39Z |
| publishDate | 2017-07-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-1bd9db3283e34102b0ac19f4492e089d2022-12-21T19:08:17ZengNature PortfolioScientific Reports2045-23222017-07-017111010.1038/s41598-017-06062-wCoronavirus nucleocapsid proteins assemble constitutively in high molecular oligomersYingying Cong0Franziska Kriegenburg1Cornelis A. M. de Haan2Fulvio Reggiori3Department of Cell Biology, University Medical Center Groningen, University of GroningenDepartment of Cell Biology, University Medical Center Groningen, University of GroningenVirology Division, Department of Infectious Diseases & Immunology, Faculty of Veterinary Medicine, Utrecht UniversityDepartment of Cell Biology, University Medical Center Groningen, University of GroningenAbstract Coronaviruses (CoV) are enveloped viruses and rely on their nucleocapsid N protein to incorporate the positive-stranded genomic RNA into the virions. CoV N proteins form oligomers but the mechanism and relevance underlying their multimerization remain to be fully understood. Using in vitro pull-down experiments and density glycerol gradients, we found that at least 3 regions distributed over its entire length mediate the self-interaction of mouse hepatitis virus (MHV) and severe acute respiratory syndrome coronavirus (SARS-CoV) N protein. The fact that these regions can bind reciprocally between themselves provides a possible molecular basis for N protein oligomerization. Interestingly, cytoplasmic N molecules of MHV-infected cells constitutively assemble into oligomers through a process that does not require binding to genomic RNA. Based on our data, we propose a model where constitutive N protein oligomerization allows the optimal loading of the genomic viral RNA into a ribonucleoprotein complex via the presentation of multiple viral RNA binding motifs.https://doi.org/10.1038/s41598-017-06062-w |
| spellingShingle | Yingying Cong Franziska Kriegenburg Cornelis A. M. de Haan Fulvio Reggiori Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers Scientific Reports |
| title | Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers |
| title_full | Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers |
| title_fullStr | Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers |
| title_full_unstemmed | Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers |
| title_short | Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers |
| title_sort | coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers |
| url | https://doi.org/10.1038/s41598-017-06062-w |
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