English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structures of Ebola and Reston Virus VP35 Oligomerization Domains and Comparative Biophysical Characterization in All Ebolavirus Species

Zinzula, L., Nagy, I., Orsini, M., Weyher-Stingl, E., Bracher, A., & Baumeister, W. (2019). Structures of Ebola and Reston Virus VP35 Oligomerization Domains and Comparative Biophysical Characterization in All Ebolavirus Species. Structure, 27(1), 39-54.e6. doi:10.1016/j.str.2018.09.009.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0003-4074-2 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-4075-1
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Zinzula, Luca1, Author              
Nagy, Istvan1, Author              
Orsini, Massimiliano2, Author
Weyher-Stingl, Elisabeth3, Author              
Bracher, Andreas4, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              
3Scientific Service Groups, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565170              
4Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              

Content

show
hide
Free keywords: CIRCULAR-DICHROISM SPECTRA; HELICAL COILED-COILS; PRELIMINARY-X-RAY; MARBURG-VIRUS; ZAIRE-EBOLAVIRUS; REPLICATION; SYSTEM; DSRNA; TRANSCRIPTION; PREDICTIONBiochemistry & Molecular Biology; Biophysics; Cell Biology;
 Abstract: The multifunctional virion protein 35 (VP35) of ebolaviruses is a critical determinant of virulence and pathogenesis indispensable for viral replication and host innate immune evasion. Essential for VP35 function is homo-oligomerization via a coiled-coil motif. Here we report crystal structures of VP35 oligomerization domains from the prototypic Ebola virus (EBOV) and the non-pathogenic Reston virus (RESTV), together with a comparative biophysical characterization of the domains from all known species of the Ebolavirus genus. EBOV and RESTV VP35 oligomerization domains form bipartite parallel helix bundles with a canonical coiled coil in the N-terminal half and increased plasticity in the highly conserved C-terminal half. The domain assembles into trimers and tetramers in EBOV, whereas it exclusively forms tetramers in all other ebolavirus species. Substitution of coiled-coil leucine residues critical for immune antagonism leads to aberrant oligomerization. A conserved arginine involved in inter-chain salt bridges stabilizes the VP35 oligomerization domain and modulates between coiled-coil oligomeric states.

Details

show
hide
Language(s): eng - English
 Dates: 2019
 Publication Status: Published in print
 Pages: 22
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: ISI: 000454804900005
DOI: 10.1016/j.str.2018.09.009
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Structure
  Other : Structure
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: London : Cell Press
Pages: - Volume / Issue: 27 (1) Sequence Number: - Start / End Page: 39 - 54.e6 Identifier: ISSN: 0969-2126
CoNE: https://pure.mpg.de/cone/journals/resource/954927002244_1