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Structural characterization of Human Coronavirus NL63 N-protein

DOI: 10.1128/JVI.02503-16 DOI Help

Authors: Bozena Szelazek (Jagiellonian University) , Wojciech Kabala (Jagiellonian University) , Krzysztof Kus (Instituto Gulbenkian de Ciencia) , Michal Zdzalik (Jagiellonian University) , Aleksandra Twarda-clapa (Jagiellonian University) , Przemyslaw Golik (Jagiellonian University) , Michal Burmistrz (Jagiellonian University) , Dominik Florek (Jagiellonian University) , Benedykt Wladyka (Jagiellonian University) , Krzysztof Pyrc (Jagiellonian University) , Grzegorz Dubin (Jagiellonian University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Virology

State: Published (Approved)
Published: March 2017

Abstract: Coronaviruses are responsible for upper and lower respiratory tract infections in humans. It is estimated that 1—10% of the population suffers annually from cold-like symptoms related to infection with HCoV-NL63, an alphacoronavirus. The nucleocapsid (N) protein, the major structural component of the capsid, facilitates RNA packing, links the capsid to the envelope and is also involved in multiple other processes including viral replication and evasion of the immune system. Although the role of N protein in viral replication is relatively well described, no structural data are currently available regarding the N proteins of alphacoronaviruses. Moreover, our understanding of the mechanisms of RNA binding and nucleocapsid formation remains incomplete. In this study, we solved the crystal structures of the N- and C-terminal domains (NTD, residues 10—140, and CTD, residues 221—340, respectively) of the N protein of HCoV-NL63, both at 1.5 Å resolution. Based on our structure of NTD solved here, we proposed and experimentally evaluated a model of RNA binding. The structure of the CTD reveals the mode of N protein dimerization. Overall, this study expands our understanding of the initial steps of N protein/nucleic acid interaction, and may facilitate future efforts to control the associated infections.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I23-Long wavelength MX

Other Facilities: DESY; Swiss Light Source; BESSY II

Added On: 13/04/2017 11:30

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