English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  The native structure of the assembled matrix protein 1 of influenza A virus

Peukes, J., Xiong, X. L., Erlendsson, S., Qu, K., Wan, W., Calder, L. J., et al. (2020). The native structure of the assembled matrix protein 1 of influenza A virus. Nature, 587(7834), 495-498. doi:10.1038/s41586-020-2696-8.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Peukes, J., Author
Xiong, X. L., Author
Erlendsson, S., Author
Qu, K., Author
Wan, W., Author
Calder, L. J., Author
Schraidt, O., Author
Kummer, S., Author
Freund, S. M. V., Author
Krausslich, H. G., Author
Briggs, John A. G.1, 2, Author           
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              
2European Molecular Biology Laboratory, External Organizations, Heidelberg, DE, ou_3346677              

Content

show
hide
Free keywords: beam-induced motion cryo-em m1 protein helical reconstruction electron-microscopy crystal-structure terminal domain membrane nmr visualization Science & Technology - Other Topics
 Abstract: Influenza A virus causes millions of severe cases of disease during annual epidemics. The most abundant protein in influenza virions is matrix protein 1 (M1), which mediates virus assembly by forming an endoskeleton beneath the virus membrane(1). The structure of full-length M1, and how it oligomerizes to mediate the assembly of virions, is unknown. Here we determine the complete structure of assembled M1 within intact virus particles, as well as the structure of M1 oligomers reconstituted in vitro. We find that the C-terminal domain of M1 is disordered in solution but can fold and bind intransto the N-terminal domain of another M1 monomer, thus polymerizing M1 into linear strands that coat the interior surface of the membrane of the assembling virion. In the M1 polymer, five histidine residues-contributed by three different monomers of M1-form a cluster that can serve as the pH-sensitive disassembly switch after entry into a target cell. These structures therefore reveal mechanisms of influenza virus assembly and disassembly. Structures of the assembled matrix protein 1 of influenza A virus in intact virus particles and of oligomers of this protein reconstituted in vitro reveal mechanisms of assembly and disassembly of influenza virus.

Details

show
hide
Language(s): eng - English
 Dates: 2020
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000567780300005
DOI: 10.1038/s41586-020-2696-8
ISSN: 0028-0836
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Nature
  Alternative Title : Nature
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 587 (7834) Sequence Number: - Start / End Page: 495 - 498 Identifier: -