Lab Research Focus
The assembly of protein subunits into polymeric supramolecular structures is controlled both temporally and positionally. Control is achieved through the use of highly specific protein/protein recognition events, and well-defined assembly pathways. The manner in which this information is encoded in the protein subunits is not well understood, despite the fact that interfering with these pathways holds promise therapeutically for indications as diverse as viral & bacterial infections, alzheimers disease, and neoplasia.
We take an interdisciplinary approach employing an array of biochemical, biophysical, genetic, and structural tools to study these processes. Two viral systems with distinctive assembly pathways are under active investigation. One system, the Salmonella bacteriophage P22 which assembles into well defined non-enveloped stable icosahedral capsids typifies tightly controlled assembly pathways while the other, HIV which forms fragile polymorphous enveloped capsids suggests more flexibility in assembly. Comparison of these systems will illuminate different biological strategies for control of capsid assembly, and will ultimately lead to novel antiviral approaches which directly target capsid assembly.
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