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

Julia Peukes, Xiaoli Xiong (), Simon Erlendsson, Kun Qu, William Wan, Leslie J. Calder, Oliver Schraidt, Susann Kummer, Stefan M. V. Freund, Hans-Georg Kräusslich and John A. G. Briggs ()
Additional contact information
Julia Peukes: Medical Research Council Laboratory of Molecular Biology
Xiaoli Xiong: Medical Research Council Laboratory of Molecular Biology
Simon Erlendsson: Medical Research Council Laboratory of Molecular Biology
Kun Qu: Medical Research Council Laboratory of Molecular Biology
William Wan: European Molecular Biology Laboratory
Leslie J. Calder: The Francis Crick Institute
Oliver Schraidt: European Molecular Biology Laboratory
Susann Kummer: Universitätsklinikum Heidelberg
Stefan M. V. Freund: Medical Research Council Laboratory of Molecular Biology
Hans-Georg Kräusslich: Universitätsklinikum Heidelberg
John A. G. Briggs: Medical Research Council Laboratory of Molecular Biology

Nature, 2020, vol. 587, issue 7834, 495-498

Abstract: 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 membrane1. 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 in trans to 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.

Date: 2020
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/s41586-020-2696-8 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:587:y:2020:i:7834:d:10.1038_s41586-020-2696-8

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/s41586-020-2696-8

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().