Skip to Main content Skip to Navigation
Journal articles

Molecular organization and dynamics of the fusion protein Gc at the hantavirus surface

Abstract : The hantavirus envelope glycoproteins Gn and Gc mediate virion assembly and cell entry, with Gc driving fusion of viral and endosomal membranes. Although the X-ray structures and overall arrangement of Gn and Gc on the hantavirus spikes are known, their detailed interactions are not. Here we show that the lateral contacts between spikes are mediated by the same 2-fold contacts observed in Gc crystals at neutral pH, allowing the engineering of disulfide bonds to cross-link spikes. Disrupting the observed dimer interface affects particle assembly and overall spike stability. We further show that the spikes display a temperature-dependent dynamic behavior at neutral pH, alternating between ‘open’ and ‘closed’ forms. We show that the open form exposes the Gc fusion loops but is off-pathway for productive Gc-induced membrane fusion and cell entry. These data also provide crucial new insights for the design of optimized Gn/Gc immunogens to elicit protective immune responses.
Complete list of metadata
Contributor : Pablo GUARDADO-CALVO Connect in order to contact the contributor
Submitted on : Monday, April 26, 2021 - 11:29:14 AM
Last modification on : Thursday, April 7, 2022 - 10:10:44 AM
Long-term archiving on: : Tuesday, July 27, 2021 - 6:41:57 PM


Publication funded by an institution


Distributed under a Creative Commons Attribution 4.0 International License




Eduardo Bignon, Amelina Albornoz, Pablo Guardado-Calvo, Félix Rey, Nicole Tischler. Molecular organization and dynamics of the fusion protein Gc at the hantavirus surface. eLife, eLife Sciences Publication, 2019, 8, pp.e46028. ⟨10.7554/eLife.46028⟩. ⟨pasteur-03207972⟩



Record views


Files downloads