Physical and Biochemical Characterization of the Portal Complex of Bacteriophage Lambda

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DNA packaging is a critical step in the assembly of many double-stranded DNA viruses, including poxvirus, the herpesviruses, and many bacteriophages. In all cases, the viral genome is inserted into a pre-formed capsid by a terminase enzyme. DNA passes into the capsid through the portal, a doughnut-shaped structure found in the capsids of all of these viruses. The long-range goal of this lab is to understand, in detail, the process of viral genome packaging. The present project examines DNA packaging in bacteriophage lambda as a model system to understand the basic mechanisms of virus assembly. The lambda portal is extensively modified during the maturation of the viral capsid, and a major goal of this project is to characterize the chemical and structural modifications of the lambda portal, and to define the biological role of each modification. In addition, the viral protease responsible for capsid maturation will be identified and characterized. The recent emergence of "new" viral scourges, the potential of viral packaging systems in nanosciences and engineering, and the increasing threat of biological weapons underscore the need to understand virus development at the most fundamental level. The results of this research will contribute to this critical knowledge base, and make possible a rapid response to new and emerging biological threats. Broader Impacts: Pre-doctoral and post-doctoral students, including members of minority groups that have been underrepresented in science, will participate in this work. The project will thus serve to train a diverse group of future scientists.