English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2 acute respiratory syndrome coronavirus 2

Zinzula, L., Basquin, J., Bohn, S., Beck, F., Klumpe, S., Pfeifer, G., et al. (2021). High-resolution structure and biophysical characterization of the nucleocapsid phosphoprotein dimerization domain from the Covid-19 severe acute respiratory syndrome coronavirus 2 acute respiratory syndrome coronavirus 2. Biochemical and Biophysical Research Communications, 538, 54-62. doi:10.1016/j.bbrc.2020.09.131.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Zinzula, Luca1, Author              
Basquin, Jerome2, Author              
Bohn, Stefan1, Author              
Beck, Florian1, Author              
Klumpe, Sven1, Author              
Pfeifer, Günter1, Author              
Nagy, Istvan1, Author              
Bracher, Andreas3, Author              
Hartl, F. Ulrich3, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
3Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

Content

show
hide
Free keywords: Biochemistry & Molecular Biology; Biophysics; Covid-19; SARS coronavirus; Nucleocapsid; Oligomerization; RNA binding;
 Abstract: Unprecedented by number of casualties and socio-economic burden occurring worldwide, the corona virus disease 2019 (Covid-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the worst health crisis of this century. In order to develop adequate countermeasures against Covid-19, identification and structural characterization of suitable antiviral targets within the SARS-CoV-2 protein repertoire is urgently needed. The nucleocapsid phosphoprotein (N) is a multifunctional and highly immunogenic determinant of virulence and pathogenicity, whose main functions consist in oligomerizing and packaging the single-stranded RNA (ssRNA) viral genome. Here we report the structural and biophysical characterization of the SARS-CoV-2 N C-terminal domain (CTD), on which both N homo-oligomerizati on and ssRNA binding depend. Crystal structures solved at 1.44 angstrom and 1.36 angstrom resolution describe a rhombus-shape N CTD dimer, which stably exists in solution as validated by size exclusion chromatography coupled to multi-angle light scattering and analytical ultracentrifugation. Differential scanning fluorimetry revealed moderate thermal stability and a tendency towards conformational change. Microscale thermophoresis demonstrated binding to a 7-bp SARS-CoV-2 genomic ssRNA fragment at micromolar affinity. Furthermore, a low-resolution preliminary model of the fulllength SARS-CoV N in complex with ssRNA, obtained by cryo-electron microscopy, provides an initial understanding of self-associating and RNA binding functions exerted by the SARS-CoV-2 N. (c) 2020 Elsevier Inc. All rights reserved.

Details

show
hide
Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biochemical and Biophysical Research Communications
  Other : Biochem. Biophys. Res. Commun.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 538 Sequence Number: - Start / End Page: 54 - 62 Identifier: ISSN: 0006-291X
CoNE: https://pure.mpg.de/cone/journals/resource/954922652205_1