Insight into the molecular assembly of a protein with a central role in infections paves the way to understanding how Rift Valley fever virus causes disease.

Analysis of naturally infected mosquitoes shows that ecosystem disturbance can lead to a turnover in host community composition and that more individuals of a single species are a key driver of virus emergence.

Llama-derived single-domain antibodies, formatted as bispecific antibodies with human Fc domains, reduce and prevent bunyavirus-induced morbidity and mortality in mice upon prophylactic and therapeutic administration.

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.

The high-resolution structure of a filamentous flexible plant virus shows that there is structural homology between its coat protein and the nucleoproteins of an unrelated group of enveloped RNA animal viruses.

A mouse-adapted strain of Crimean-Congo hemorrhagic fever virus that recapitulates human disease in wild-type mice significantly improves our ability to study Crimean-Congo hemorrhagic fever virus pathogenesis.

Conformational flexibility in HIV-1 capsid, provided by cyclophilin A binding, facilitates evasion of capsid-targeting restriction factor MxB, while allowing sequence change to facilitate cytotoxic T-cell evasion.

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.