Date of Award

Fall 2013

Degree Type

Dissertation

Degree Name

Doctor of Philosophy (PhD)

Department

Biological Science

First Advisor

Michael G. Rossmann

Committee Chair

Wen Jiang

Committee Member 1

Michael Rossmann

Committee Member 2

Richard J. Kuhn

Committee Member 3

Marc Loudon

Abstract

Rubella virus is a leading cause of birth defects due to infectious agents. When contracted during pregnancy, rubella infection leads to severe damage in fetuses. Despite its medical importance, very little is known about the structure of the pleomorphic rubella virus as compared to its alphavirus relatives. The rubella capsid protein is a critical structural component of virions as well as a key factor in virus-host interactions. Three crystal structures of the structural domain of the rubella capsid protein have been described here. The polypeptide fold of the capsid protomer has not been observed previously. The capsid protein structure, along with cryo-electron tomograms of rubella virus particles and mutational studies on the capsid protein, provides a low resolution structure of the virus particle. Nucleocapsid assembly studies on the rubella capsid protein has given additional information on the factors affecting formation of the virion cores. Together, these studies enumerate critical differences between rubella virus and alphaviruses that might affect their specific pathogenicities.

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