Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein

• DOI: 10.1371/journal.ppat.1009100
• Publication Date: 2020-12-02T19:33:01Z
• Authors: Dhurvas Chandrase...; Dominika Chalupska; Jan Silhan; Eliska Koutna; Radim Nencka; Vaclav Veverka; Evzen Boura
• Keywords: Phosphoprotein; Coronavirus

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the causative agent of disease 2019 (COVID-19). SARS-CoV-2 a single-stranded positive-sense RNA virus. Like other coronaviruses, has an unusually large genome that encodes four structural proteins and sixteen nonstructural proteins. The nucleocapsid phosphoprotein N essential for linking viral to membrane. Both N-terminal binding (N-NTD) C-terminal dimerization domains are involved in capturing and, intrinsically disordered region between these anchors ribonucleoprotein complex Here, we characterized structure N-NTD its interaction with using NMR spectroscopy. We observed positively charged canyon on surface might serve as putative site similarly coronaviruses. subsequent titrations double-stranded revealed much more extensive U-shaped RNA-binding cleft lined regularly distributed arginines lysines. data supported by mutational analysis allowed us construct hybrid atomic models N-NTD/RNA provided detailed insight into recognition.