Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers

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

*Bijbehorende auteur voor dit werk

OnderzoeksoutputAcademicpeer review

33 Citaten (Scopus)
518 Downloads (Pure)

Samenvatting

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.

Originele taal-2English
Artikelnummer5740
Aantal pagina's10
TijdschriftScientific Reports
Volume7
DOI's
StatusPublished - 18-jul-2017

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