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SUMMARY:Defining Structural Interactions Between Cellular Focal Adhesion Ki
 nase and the Influenza Virus Nucleoprotein
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20190201T000000
UID:2026-05-05-23-05-17@natsci.colostate.edu
DTSTAMP:20260505T230517
Description:About the Seminar\nInfluenza A viruses (IAV) are major human re
 spiratory pathogens that cause annual epidemics and occasional pandemics g
 lobally. IAV has evolved its viral proteins to interact with cellular prot
 eins to aid in the regulation of viral replication and ultimately cause di
 sease pathogenesis. More specifically\, the ribonucleoprotein complexes (R
 NPs) interact with many host cell kinases that have been shown to regulate
  viral replication. These host cell kinases can interact with any one of t
 he components of the ribonucleoprotein complexes: the viral genomic RNA se
 gment\, the viral polymerase (PA\, PB1\, PB2) or the viral nucleoprotein (
 NP). Focal adhesion kinase (FAK) is a non-receptor tyrosine kinase that ha
 s been shown to co-localize with NP in infected cells\, and when FAK is in
 hibited viral RNA levels are low suggesting that FAK upregulates viral rep
 lication through NP interactions. However\, how the specific interactions 
 between FAK and NP contribute to disease is not well understood primarily 
 due to the unknown nature of how FAK and NP associate together. Ultimately
 \, there is a gap in the knowledge of whether or not 1) FAK directly inter
 acts with NP alone or if FAK associates with NP through interactions with 
 the viral genomic RNA or the viral polymerase proteins within the ribonucl
 eoprotein complex\, and 2) if FAK interacts with NP in a common region acr
 oss all subtypes of NP found in IAV strains. Therefore\, this proposal aim
 s to define the interactions between FAK and viral NP. First\, we will det
 ermine if FAK and NP directly interact through cross-linking/mass spectrom
 etry. We will utilize multiple antibodies to isolate various FAK complexes
  generated from a formaldehyde cross-linking treatment in vitro. These com
 plexes will be digested into small peptides in order to identify the cross
 -linked peptides via liquid chromatography electrospray ionization tandem 
 mass spectrometry. Additionally\, we will corroborate the specific interac
 tions of FAK and NP determined from cross-linking/mass spectrometry throug
 h cryo electron microscopy. Furthermore\, bioinformatic analysis will be u
 tilized to identify common regions between NP subtypes that interact with 
 FAK. By understanding how the ribonucleoprotein complexes interact with ce
 llular kinases during replication\, we can target specific virus-host inte
 ractions in the development of universal therapeutics for the treatment in
 fluenza A virus infection. 4:00 pm
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