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Viruses must enter host cells to replicate. For enveloped viruses, this requires specialized fusion proteins that undergo dramatic conformational changes to bring viral and cellular membranes together.
Our lab investigates these molecular machines using structural and virological approaches. We are particularly interested in how class III fusion proteins transition between prefusion to postfusion states to power viral entry.
Many viral fusion proteins are most vulnerable before they refold into their final postfusion form. However, prefusion states are often unstable, transient, and difficult to study.
We use structure-guided engineering and computational protein design to stabilize viral proteins in defined conformations. These stabilized proteins allow us to ask how antigen shape affects antibody responses and whether specific conformations can be used to improve protective immunity.
Not all antibody responses are equally protective. Our lab uses structural and functional approaches to identify where antibodies bind, which epitopes are immunodominant, and how different antigen designs reshape the immune response.
This work helps define the molecular features of effective vaccine antigens and guides the design of next-generation immunogens and antibody therapies.
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