Nick S. Laursen

TL;DR: Two antibodies, which bind to distinct regions of the viral hemagluttinin (HA) molecule, neutralize multiple strains from both lineages of influenza B virus, whereas the third antibody binds to the stem region of HA and is able to neutralize both influenza A and B strains.

TL;DR: The results represent a proof of concept for the design of HA stem mimics that elicit bnAbs against influenza A group 1 viruses and completely protects mice in lethal heterologous and heterosubtypic challenge models, and reduces fever after sublethal challenge in cynomolgus monkeys.

TL;DR: Despite available antivirals and vaccines, influenza continues to be a major cause of mortality worldwide and the sporadic emerging resistance to neuraminidase inhibitors among circulating strains suggests an urgent need for new therapeutic agents.

TL;DR: These findings demonstrate that multidomain antibodies targeting multiple epitopes exhibit enhanced virus cross-reactivity and potency, and may provide an effective strategy to prevent infection with influenza virus and other highly variable pathogens.

TL;DR: The crystal structure of 5J8 Fab in complex with a bacterially expressed and refolded globular head domain from the hemagglutinin (HA) of the A/California/07/2009 (H1N1) pandemic virus is presented and consistent with previous studies, the bacterially expression H1 HA properly refolds, retaining its antigenic structure, and presents a low-cost and rapid alternative for engineering and manufacturing candidate flu vaccines.