The crystal structure of neutralizing antibody AR3X in complex with HCV E2 glycoprotein reveals unusual features of antibody recognition in which a conserved epitope is recognized by distinct antibody poses.
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.
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.
To quantify serum or antibody activity against HIV-1, logistic regression of single-dilution neutralization outcomes can efficiently summarize neutralization potency and indicate which samples may lack sufficient statistical support, for high-throughput screening in large-scale vaccine trials.
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.