STRUCTURAL STUDIES OF VIRAL POLYMERASES

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Both crystals, influenza virus NP and DXV VP1, have been tested in our laboratory using the in-house X-ray diffraction facility. Due to the relative small sizes of these crystals, they only diffracted to ~4 angstrom resolution. Therefore, synchrotron radiation is urgently needed for better data collection and structure determination. We will use Se-MAD to determine the phases, and therefore we would like to obtain some beamtime at the F2 station at the most earliest possible dates. My laboratory focuses on studying the structure and function of viral proteins from influenza viruses and birnaviruses. My previous work in Dr. Steve Harrison's laboratory as postdoc as well in Dr. Michael Rossmann's laboratory as graduate student had also been focused on viral proteins and enzymes. I have already visited CHESS more than ten times both as an independent investigator as well as a postdoc or graduate student. I fully appreiciate the indispensible role of MacCHESS in virus structure determination both in the past as well in the future. Influenza virus nucleoprotein (NP) encapsidates the viral genomic RNA to form a ribonucleoprotein (RNP) complex. Much more than a structural RNA-binding protein, functional studies have shown that NP has important roles in mediating the transcription, replication and intracellular trafficking of the virus genomic RNPs. Our long term goal is to elucidate how NP mediates the formation of RNP and how NP-RNA interaction regulates viral genome replication. Your favorite consideration of the proposal is greatly appreciated!