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.
","abstract_html":"<p>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.</p>","abstract_has_math":false,"creators":["Mangala Prasad, Vidya"],"institution":null,"degree_name":"Doctor of Philosophy (PhD)","degree_level":"Dissertation","degree_discipline":"Biological Science","degree_department":null,"school":null,"contributors":["Michael G. Rossmann","Wen Jiang","Michael Rossmann","Richard J. Kuhn","Marc Loudon"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2013,"date_issued":"2013-10-01T07:00:00Z","date_published":"2013-10-01T07:00:00Z","updated_at":"2026-07-24T03:53:11Z","subjects":["biological sciences","cryo-electron tomography","rubella virus","x-ray","crystallography","capsid proteins","Biophysics","Molecular Biology","Virology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://docs.lib.purdue.edu/open_access_dissertations/89","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Michael G. Rossmann","Wen Jiang","Michael Rossmann","Richard J. Kuhn","Marc Loudon"]},{"key":"dc:creator","label":"Author","values":["Mangala Prasad, Vidya"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"thesis:degree_discipline","label":"Discipline","values":["Biological Science"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Dissertation"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy (PhD)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["biological sciences","cryo-electron tomography","rubella virus","x-ray","crystallography","capsid proteins","Biophysics","Molecular Biology","Virology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://docs.lib.purdue.edu/open_access_dissertations/89"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["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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