Structure of a classical broadly neutralizing stem antibody in complex with a pandemic H2 influenza virus hemagglutinin

C Dreyfus, DC Ekiert, IA Wilson - Journal of virology, 2013 - Am Soc Microbiol
C Dreyfus, DC Ekiert, IA Wilson
Journal of virology, 2013Am Soc Microbiol
We report the structural characterization of the first antibody identified to cross-neutralize
multiple subtypes of influenza A viruses. The crystal structure of mouse antibody C179
bound to the pandemic 1957 H2N2 hemagglutinin (HA) reveals that it targets an epitope on
the HA stem similar to those targeted by the recently identified human broadly neutralizing
antibodies. C179 also inhibits the low-pH conformational change of the HA but uses a
different angle of approach and both heavy and light chains.
Abstract
We report the structural characterization of the first antibody identified to cross-neutralize multiple subtypes of influenza A viruses. The crystal structure of mouse antibody C179 bound to the pandemic 1957 H2N2 hemagglutinin (HA) reveals that it targets an epitope on the HA stem similar to those targeted by the recently identified human broadly neutralizing antibodies. C179 also inhibits the low-pH conformational change of the HA but uses a different angle of approach and both heavy and light chains.
American Society for Microbiology