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- W2946880900 abstract "If you want to thwart infection by influenza viruses, a good bet is to block the pathogen’s exterior hemagglutinin proteins from binding with a host cell’s sialic acid-containing sugars. Nature already uses this interference strategy: Antibodies bind influenza hemagglutinin, preventing infection by obstructing the host-pathogen interaction in a variety of ways, sometimes at the sialic acid binding site and other times with just the antibody’s sheer physical bulk. This bulk has its downside, though: Only one antibody can bind a hemagglutinin site at a time. David Baker and Eva-Maria Strauch of the University of Washington and colleagues wondered if they could design a protein that bound hemagglutinin in three places simultaneously instead of just one, to improve on nature’s avidity—the overall strength of binding. They theorized this would be possible because hemagglutinin forms regular trimers on the surface of the virus. First, the team used a computational strategy to design" @default.
- W2946880900 created "2019-06-07" @default.
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- W2946880900 date "2017-06-26" @default.
- W2946880900 modified "2023-09-27" @default.
- W2946880900 title "Custom peptide neutralizes influenza" @default.
- W2946880900 doi "https://doi.org/10.1021/cen-09526-scicon004" @default.
- W2946880900 hasPublicationYear "2017" @default.
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