Functional characterization of non structural proteins of bovine adenovirus 3

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Adenovirus consists of a naked icosahedral capsid, double stranded DNA genome with inverted terminal repeats and a polypeptide attached to the 5' ends of the genome. At least three non structural proteins are encoded by adenoviruses, which are believed to function in transactivation of different promoters, maturation and translation of late mRNAs, DNA encapsidation and viral capsid assembly. In bovine adenovirus (BAdV) -3, the non structural proteins are 52K, 100K and 33K. Of these, 100K and 33K are phosphonuclear proteins, which appear to be essential for BAdV-3 replication and, may be involved in DNA packaging, viral capsid assembly and efficient DNA/capsid interaction. We believe that involvement of 100K and 33K in different aspects of BAdV-3 virus assembly may require interaction of these proteins with other viral/cellular proteins. The hypothesis for this study is that non structural proteins contain multi-functions, which are important for viral replication and assembly. Moreover, ability of these proteins to perform multi-functions may require interactions with other viral / cellular protein(s). So the overall goal is to identify, characterize, map and determine the mechanism of performing different functions of 33K and 100K in the production of progeny virions. The specific goal of this grant is to investigate in detail the interaction of 33K and 100K with other viral/cellular proteins, which will help in determining the mechanism of performing different functions by these non structural proteins. The specific goal will be achieved by a) investigating the interaction of 33K and 100K with other viral proteins, b) investigating the interaction of 100K and 33K with cellular proteins, c) mapping the domains of 33K and 100K required for the interaction with other viral / cellular proteins and d) determining the importance of identified protein-protein interaction for BAdV-3 replication.