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Organisation of the orthobunyavirus tripodal spike and the structural changes induced by low pH and K + during entry
Open accessPreprint — published as 10.1038/s41467-023-41205-w · Paper page
Abstract
Following internalisation, viruses employ the changing environment of maturing endosomes as cues to promote endosomal escape, a process mediated by viral glycoproteins. Specifically, we previously showed that both high [K + ] and low pH promote entry of Bunyamwera virus (BUNV), the prototypical bunyavirus. Here, we used sub-tomogram averaging combined with AlphaFold, to generate a pseudo-atomic model of the whole glycoprotein envelope of BUNV. This allowed us to unambiguously locate the Gc fusion domain and its chaperone Gn within the floor domain of the spike. We also confirmed that low pH and high [K + ] alters the viral glycoproteins, resulting in an activated intermediate state functionally-distinct from the highly ordered ground state, and we localize these changes to the floor domain. Biochemical data suggests that in this intermediate state the viral fusion loops are partially exposed and selectively interact with host cell membranes. Taken together, we reveal new mechanistic understanding of the requirements for virus entry.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Metadata
- Authors
- Hover, S., Charlton, F. W., Hellert, J., Barr, J. N., Mankouri, J., & Fontana, J.
- Affiliations
- University of Leeds (GB)
- Leibniz Institute of Virology (LIV) (DE)
- Corresponding author
- Barr, John N
- Mankouri, Jamel
- Fontana, Juan
- Venue
- Nature Communications
- Publisher
- openRxiv
- Published
- 2022-08-12
- Volume
- 14
- Issue
- 1
- Pages
- 5885-5885
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC10514341
- OpenAlex
- W4386923313
- Cited by
- 24
- References
- 1
- Citations by year
- 2026: 9 · 2025: 8 · 2024: 4 · 2023: 3
- FWCI
- 4.97
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- Nature Communications (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- White Rose Research Online (University of Leeds, The University of Sheffield, University of York) (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Desy Publications Database (Deutsches Elektronen-Synchrotron DESY) (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- DESY Publication Database (PUBDB) (Deutsches Elektronen-Synchrotron)
- Funders
- University of Hull
- Wellcome Trust (090932/Z/09/Z, WT104918MA, 108466, 221524/Z/20/Z, 108466/Z/15/Z)
- Research Councils UK (BB/P001459/1, MR/T016159/1)
- Academy of Medical Sciences (SBF002\1029)
- University of Leeds
- Rosetrees Trust (A1618)
- University of Glasgow
- Human Frontier Science Program (RGP0040/2019)
- Medical Research Council (MR/T016159/1)
- Biotechnology and Biological Sciences Research Council (BB/P001459/1)
- Medical Research Foundation (MR/T016159/1)
- Topics
- Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Infectious Diseases › Viral Infections and Vectors
- Keywords
- Bunyamwera virus, Orthobunyavirus, viral entry, endosomal escape, low pH, potassium ions, membrane fusion, endocytosis
- MeSH terms
- Biological Assay, Bunyamwera virus, Cues, Hydrogen-Ion Concentration, Orthobunyavirus
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