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.

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.

A critical role for glycosylation on viral entry and methods to use this knowledge to reduce SARS-CoV-2 infectivity has been demonstrated.

Viral evolution can lead to mutations that render specific glycosylation sites dispensable for folding and for supporting the protein's function, allowing changes in the shield, and in the immunogenic profile.

Insights from integrating evolutionary predictions and protein dynamics unveil how specific mutations in the SARS-CoV-2 spike protein epistatically interact in order to influence spike protein interaction with human cells, potentially altering the virus's infectivity and immune evasion capabilities.

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.

The SARS-CoV-2 Spike proteins demonstrate in vivo cellular tropism, ascertain targets within human mononuclear cells, and provide insights into their functional consequences, thereby enhancing comprehension of their impact on humans.

Non-neutralizing antibodies to the SARS-CoV-2 spike protein’s S2 domain that also recognize widely circulating endemic coronavirus strains are rapidly boosted by natural infection but not vaccination with stabilized spike-based vaccines.

De novo protein nanoparticles were designed from scratch to present viral glycoprotein antigens, providing a systematic way to study the influence of antigen presentation geometry on immune response.

Molecular dynamics simulation assisted engineering of recombinant soluble human ACE2 N-glycosylation by site-directed mutagenesis or glycosidase treatment yields a superior SARS-CoV-2 decoy receptor.