In this study, we aim to functionally interrogate host-pathogen relationships in human influenza viruses. The Proteomics Core will employ a systematic affinity tag/purification-mass spectrometry approach to identify the viral-host protein complexes. The data generated using these initial, unbiased approaches will fuel more targeted, hypothesis-driven research in the subsequent projects. In tandem with this work and with more targeted downstream work, we will be closely monitoring for links to host factors involved in quality control processes, including chaperone function, protein ubiquitination, and protein degradation, which will link this work to the collaborations with Adolfa Garcia-Sastre, Sumit Chanda, and John Young.
Human influenza viruses infect millions of people worldwide each year, resulting in a wide range of clinical outcomes. To gain insight into the pathogenesis of these viruses, we aim to analyze the functional, genetic and biochemical relationships between several members of this class of virus and host cells, which will reveal key human pathways that are being hijacked during infection. This information can ultimately be used to generate novel anti-viral drugs and vaccines.
|Morris, John H; Knudsen, Giselle M; Verschueren, Erik et al. (2014) Affinity purification-mass spectrometry and network analysis to understand protein-protein interactions. Nat Protoc 9:2539-54|
|Rajsbaum, Ricardo; Versteeg, Gijs A; Schmid, Sonja et al. (2014) Unanchored K48-linked polyubiquitin synthesized by the E3-ubiquitin ligase TRIM6 stimulates the interferon-IKK? kinase-mediated antiviral response. Immunity 40:880-95|
|Rajsbaum, Ricardo; Garcia-Sastre, Adolfo; Versteeg, Gijs A (2014) TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity. J Mol Biol 426:1265-84|
|Schotsaert, Michael; García-Sastre, Adolfo (2014) Influenza vaccines: a moving interdisciplinary field. Viruses 6:3809-26|