Characterization of BKV agnoprotein and analysis of its function and regulation
Identifications of the function(s) and regulation of the viral protein, agnoprotein.
Project leader: Mona Johannessen
Co-workers: members of the virology research group
Main objects:
We want to identify the function(s) and regulation of the viral protein, agnoprotein.
Project outline:
Polyomaviruses are viruses that originally were identified as tumour-inducing viruses when inoculated in animal models and that could transform cells. Several members of the polyomavirus family exist, including the human BK and JC viruses. Primate polyomaviruses are small DNA viruses, encoding only a few proteins. The major early proteins are the regulatory proteins large T-ag and small t-ag, while the late proteins include the capsid proteins VP1, VP2, VP3 as well as a regulatory protein named agnoprotein. The agnoprotein is approximately 70 amino acids long and is conserved, especially in the N-terminal part of the protein. Agnoprotein is a phosphoprotein, and others and we have identified phospho-acceptor sites for cellular protein kinases. Our goal is to study the functions of the agnoprotein and to determine the biological role of these phosphorylation events. We also want to identify interaction partners of agnoprotein, and investigate the functional relevance of these interactions.Functional organization of the BK virus genome. The genome is divided in the early region, encoding the large T- and small t-ag; the late region, encoding the capsid proteins VP1, VP2, and VP3, and the agnoprotein (indicated by a red arrow); and the non-coding control region (NCRR) with origin of replication and promoter/enhancer sequences.