Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers

Yingying Cong, Franziska Kriegenburg, Cornelis A. M. de Haan, Fulvio Reggiori*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

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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.

Original languageEnglish
Article number5740
Number of pages10
JournalScientific Reports
Volume7
DOIs
Publication statusPublished - 18-Jul-2017

Keywords

  • MOUSE HEPATITIS-VIRUS
  • RESPIRATORY SYNDROME CORONAVIRUS
  • N-TERMINAL DOMAIN
  • REPLICASE-TRANSCRIPTASE COMPLEX
  • INFECTIOUS-BRONCHITIS VIRUS
  • SARS CORONAVIRUS
  • RNA-BINDING
  • DIMERIZATION DOMAIN
  • SELF-ASSOCIATION
  • CRYSTAL-STRUCTURE

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