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Structure and mechanism of viral and cellular membrane fusion machineries

Total Cost €


EC-Contrib. €






 MEMBRANEFUSION project word cloud

Explore the words cloud of the MEMBRANEFUSION project. It provides you a very rough idea of what is the project "MEMBRANEFUSION" about.

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Project "MEMBRANEFUSION" data sheet

The following table provides information about the project.


There are not information about this coordinator. Please contact Fabio for more information, thanks.

 Coordinator Country United Kingdom [UK]
 Total cost 1˙965˙961 €
 EC max contribution 1˙965˙961 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2014-CoG
 Funding Scheme ERC-COG
 Starting year 2015
 Duration (year-month-day) from 2015-09-01   to  2021-08-31


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 Project objective

Fusion of two biological membranes is essential to life. It is required during organism development, for trafficking of material between cellular compartments, for transfer of information across synapses, and for entry of viruses into cells. Fusion must be carefully controlled and the core fusion components are typically found within a complex regulatory machine. There have been decades of research on the structure and function of individual components, on the dynamics and biophysics of fusion, and on phenotypes resulting from mutating or inhibiting component proteins. These have led to a model for fusion in which regulated refolding or assembly of proteins draws two membranes closer together until they fuse. Despite this breadth of study, we know very little about how the components of the fusion machinery function in context: How are they arranged on the membrane around the site of fusion? How do they respond structurally to regulation? How does the fully assembled machinery rearrange to reshape the membrane and drive fusion? These gaps in knowledge can be attributed to a shortage of structural biology methods able to derive structural data on proteins assembled within complex, heterogeneous or dynamic environments such as a fusion site. Here I propose to apply a combination of state-of-the-art cryo-electron tomography, image processing and correlative fluorescence and electron microscopy methods to obtain detailed structural information on assembled fusion machineries and of fusion intermediates both in vitro and in vivo. I will study how influenza virus fuses with a target membrane, complemented by studies on fusion of HIV-1 and of synaptic vesicles. By determining how viral and synaptic fusion complexes reposition and restructure prior to fusion, how they arrange around the fusion site, how they reshape the membrane to induce fusion, and how these processes can be regulated and inhibited, I will derive a mechanistic model of membrane fusion in situ.


year authors and title journal last update
List of publications.
2020 Robert A. Dick, Chaoyi Xu, Dustin R. Morado, Vladyslav Kravchuk, Clifton L. Ricana, Terri D. Lyddon, Arianna M. Broad, J. Ryan Feathers, Marc C. Johnson, Volker M. Vogt, Juan R. Perilla, John A. G. Briggs, Florian K. M. Schur
Structures of immature EIAV Gag lattices reveal a conserved role for IP6 in lentivirus assembly
published pages: e1008277, ISSN: 1553-7374, DOI: 10.1371/journal.ppat.1008277
PLOS Pathogens 16/1 2020-03-05
2019 Lauren Ann Metskas, John A. G. Briggs
Fluorescence-Based Detection of Membrane Fusion State on a Cryo-EM Grid using Correlated Cryo-Fluorescence and Cryo-Electron Microscopy
published pages: 1-8, ISSN: 1431-9276, DOI: 10.1017/s1431927619000606
Microscopy and Microanalysis 2019-06-06
2017 William Wan, Larissa Kolesnikova, Mairi Clarke, Alexander Koehler, Takeshi Noda, Stephan Becker & John A. G. Briggs
Structure and assembly of the Ebola virus nucleocapsid
published pages: , ISSN: 0028-0836, DOI:
Nature 2019-06-06
2017 Beata Turoňová, Florian K.M. Schur, William Wan, John A.G. Briggs
Efficient 3D-CTF correction for cryo-electron tomography using NovaCTF improves subtomogram averaging resolution to 3.4 Ã…
published pages: 187-195, ISSN: 1047-8477, DOI: 10.1016/j.jsb.2017.07.007
Journal of Structural Biology 199/3 2019-06-06

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