This subproject is one of many research subprojects utilizing theresources provided by a Center grant funded by NIH/NCRR. The subproject andinvestigator (PI) may have received primary funding from another NIH source,and thus could be represented in other CRISP entries. The institution listed isfor the Center, which is not necessarily the institution for the investigator.Influenza B viruses are important pathogens in human. They gain entrance into host cells via a membrane fusion process mediated by hemagglutinin (HA). This process involves a large conformational change of HA, from neutral-pH, pre-fusion state to low-pH post-fusion state. Our group has successfully determined the crystal structures of influenza B HA at pre-fusion state in unliganded state, as well as in complexes with two receptors of different linkages (GUP-5050). That study has yielded important insights into pre-fusion state structures of influenza B HA and into its antigenic variation and receptor binding. The last piece of missing information is of the low-pH structure of influenza B HA. In the past, we have also obtained the crystals of influenza B HA at post-fusion state. A complete set of diffraction data has been collected to 1.88 (GUP-5637). However, the crystals suffered from contamination of small crystals so that we were unable to solve the structures by molecular replacement or heavy-atom derivatives.After extensive trials, we have now succeeded in growing crystals of low-pH influenza B HA in different conditions. These crystals gave good diffractions up to 4 angstroms at local X-ray sources. So the use of a synchrotron X-ray source is needed to collect diffraction data for atomic structure determination.
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