Hantaan virus nucleocapsid cryo-EM structure determined at 3.3 Å resolution reveals how nucleoproteins assemble into a metastable helix containing a continuous RNA-binding groove compatible with genome encapsidation and compaction.

Hantavirus spikes are related laterally by 2-fold Gc contacts that can be disulfide-linked and display a temperature-dependent dynamic behavior at neutral pH, exposing and masking the Gc fusion loops.

Human antibodies that neutralize New World hantaviruses are promising for prevention or treatment of these high-priority emerging pathogens carried by rodents and transmitted to humans by aerosolized excreta or, in rare cases, person-to-person contact.

An integrated cryoEM and X-ray crystallography study resolves the structural basis for antibody-mediated targeting of the hantavirus fusion glycoprotein and provides insight into the conformational landscape of the hantavirion surface.

HIV-1 Vpr antagonises innate immune sensing of viral and non-viral stimuli by preventing activated IRF3 and NF-κB nuclear transport.

Several previously proposed cell-surface receptors for hantaviruses could be deleted in endothelial cells with little or no effect on infection, indicating that critical hantavirus entry factors remain undiscovered.