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.
The mechanism of membrane-fusion catalysis in influenza viral infection of target cells is robust against the presence of a large fraction of non-productive viral fusion proteins.
Rigorous assays of membrane fusion show that a distinct tethering step is required for lumenal compartment mixing in a manner that extends beyond simply increasing the amount of total trans-SNARE complex.
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.
The West Nile Virus envelope protein catalyzes membrane fusion through low-pH induced conformational rearrangement, with a rate determined by the formation of two trimeric complexes at the contact zone between the virus and target membrane.
Whereas SARS-CoV-2 utilizes cathepsins to enter most cell lines, human airway organoids revealed that entry into relevant cells is dependent on serine proteases, which can be targeted for treatment.
