Journal
CELL
Volume 183, Issue 2, Pages 442-+Publisher
CELL PRESS
DOI: 10.1016/j.cell.2020.08.023
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Funding
- WellcomeTrust JIF award [060208/Z/00/Z]
- WT [093305/Z/10/Z]
- National French Research Agency (ANR) [ANR-18-CE11-0011]
- French Fondation pour la Recherche Medicale (FRM) [FDM20170638040]
- Labex IBEID [ANR-10-LABX-62-IBEID]
- Infect-ERA ANR
- European Research Council under the European Union Horizon 2020 Research and Innovation Program [649053]
- National Institutes of Health (NIH) [R01AI132633]
- Institut Pasteur
- CNRS
- Chilean Agencia Nacional de Investigacion y Desarrollo (ANID, Chile) [FONDECYT 1181799]
- ANID Programa de Apoyo a Centros con Financiamiento Basal [170004]
- Tsinghua University
- Agence Nationale de la Recherche (ANR) [ANR-18-CE11-0011] Funding Source: Agence Nationale de la Recherche (ANR)
- Wellcome Trust [093305/Z/10/Z] Funding Source: Wellcome Trust
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Hantaviruses are rodent-borne viruses causing serious zoonotic outbreaks worldwide for which no treatment is available. Hantavirus particles are pleomorphic and display a characteristic square surface lattice. The envelope glycoproteins Gn and Gc form heterodimers that further assemble into tetrameric spikes, the lattice building blocks. The glycoproteins, which are the sole targets of neutralizing antibodies, drive virus entry via receptor-mediated endocytosis and endosomal membrane fusion. Here we describe the high-resolution X-ray structures of the heterodimer of Gc and the Gn head and of the homotetrameric Gn base. Docking them into an 11.4-angstrom-resolution cryoelectron tomography map of the hantavirus surface accounted for the complete extramembrane portion of the viral glycoprotein shell and allowed a detailed description of the surface organization of these pleomorphic virions. Our results, which further revealed a built-in mechanism controlling Gc membrane insertion for fusion, pave the way for immunogen design to protect against pathogenic hantaviruses.
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