Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomersCong, Y., Kriegenburg, F., de Haan, C. A. M. & Reggiori, F. 18-Jul-2017 In : Scientific Reports. 7, 10 p., 5740
Research output: Scientific - peer-review › Article
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.
|Number of pages||10|
|State||Published - 18-Jul-2017|
- 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