Investigation of antibody responses to variant Dengue virus proteins demonstrate new mechanisms that could increase the potential for vaccines to protect against mutable pathogens such as Flu, Dengue and HIV.
A new software developed for high-throughput antibody, T cell receptor, and MHC repertoire analysis uncovers neutrality of the binding interface and intramolecular crosstalk as distinguishing properties of polyreactive antibodies.
A comprehensive structural analysis of inhibitory murine antibody 3D11 binding to Plasmodium berghei circumsporozoite protein reveals common mechanisms of antibody evolution in mammals against Plasmodium parasites.
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 combination of computational modeling and protein design can reveal key determinants of antibody–antigen binding and optimize small sets of antigen variants for efficient experimental localization of epitopes.