Structural and Functional Studies of the Human Astrovirus Capsid Protein
Physical and Biological Sciences
Senior Thesis Research (Chem 195A/B/C)
Astroviruses are the second most common cause of viral gastroenteritis, and are especially common among children, the immunocompromised, and people in institutional care settings. Despite their significant impact on human health, the life cycle
of the virus is not well understood, and there are no vaccines available. Each astrovirus is enveloped in a protein capsid, which is made up of 181 connected copies of the same protein molecule. This protein has the ability to form extremely stable capsid shells in solution, without assistance from the host cell. Because of this behavior, it may be possible to use the capsid as a drug-delivery system to the gastrointestinal tract. The first step in developing therapeutic interventions or using the capsid as a nanoparticle is to understand the basic structure and function of the capsid protein. Since for proteins, structure is intimately related to function, both questions were considered simultaneously. Specifically, this project involves determining what part the acidic domain (one end of the overall capsid protein) plays in the viral life cycle, while also working to solve its three-dimensional structure using x-ray crystallography.
