Coronavirus nucleocapsid proteins assemble constitutively in high molecular oligomers

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

For glycerol gradient sedimentation, 100 µl of either the S45 fraction or bacterial extracts expressing 6xHis-tagged full-length or truncated proteins were loaded on the top of a 2,2 ml continuous 5-20% glycerol gradient in lysis buffer (w/v) prepared using the Gradient Master machine (Biocomp, New Brunswick, Canada). Figure 5 . Models for the role of CoV N proteins over the course of an infection. After synthesis, CoV N proteins constitutively assemble into oligomers with loose or more compact intertwined filament shapes 48 , which are recruited to the RTCs localized on double-membrane vesicles (DMVs) and convoluted membranes via their interaction with nsp3. At these replication platforms, newly synthesized gRNA is engaged by N protein oligomers, which co-operate with the rest of the structural proteins to form the viral particles at the ERGIC/ Golgi compartments.