Computer simulations of the evolution of broadly neutralizing antibodies against HIV suggest that non-traditional pathways involving framework mutations which lead initially to increased antibody flexibility do occur, but can be avoided by appropriate vaccine design.

A fully synthetic library of humanized single domain antibodies yields in vitro high affinity antibodies usable in cell biology and translational projects.

Single particle cryoEM structure of antibody complex with HIV-1 envelope trimer reveals new mode of asymmetric recognition of trimer apex.

Combining pre-erythrocytic and transmission blocking antibodies enhances the overall control and potential elimination of malaria within both mosquito and vertebrate populations.

Electron cryo-microscopy has been used to determine the structure of Chikungunya virus-like particles and to provide new insights into their interactions with four different antibodies.

The absolute affinities of thousands of variant antibodies are measured in parallel using a combination of cell sorting and high-throughput DNA sequencing.

Structural and computational analyses of germline antibody/HIV-1 gp120 complexes provide both general principles relevant to the unusual evolution of potent CD4-binding site antibodies and guidelines for structure-based immunogen design.

Phosphorylation deactivates TRIM21 B Box autoinhibition to licence proinflammatory signalling by cytosolic antibodies.

Synthetic single domain antibody libraries and a binder selection cascade encompassing ribosome and phage display enable the selection of conformation-specific binders against previously intractable membrane proteins within three weeks.

Proteomics and functional genomics coupled to an antibody discovery pipeline revealed the influence of oncogenic RAS signaling on the cell-surface proteome and resulted in the discovery of potential therapeutic targets for RAS-driven cancers.