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dc.contributor.authorBuchanan, Susan
dc.date.accessioned2012-10-30T18:49:04Z
dc.date.available2012-10-30T18:49:04Z
dc.date.issued2012-10-16
dc.identifier.urihttp://hdl.handle.net/1853/45213
dc.descriptionSusan Buchanan of the National Institutes of Health presented a lecture on Tuesday, October 16, 2012 from 11:00 am to 12:00 pm in the Klaus Advanced Computing Building, Room 1116E.en_US
dc.descriptionRuntime: 52:04 minutes.en_US
dc.description.abstractNeisseria are obligate human pathogens causing bacterial meningitis, septicemia, and gonorrhea. Neisseria require iron for survival and can extract it directly from human transferrin for transport across the outer membrane. The transport system consists of TbpA, an integral outer membrane protein, and TbpB, a co-receptor attached to the cell surface; both proteins are potentially important vaccine and therapeutic targets. Two key questions driving Neisseria research are: 1) how human transferrin is specifically targeted, and 2) how the bacteria liberate iron from transferrin at neutral pH. To address them, we solved crystal structures of the TbpA-transferrin complex and of the corresponding co-receptor TbpB. We characterized the TbpB-transferrin complex by small angle X-ray scattering and the TbpA-TbpB-transferrin complex by electron microscopy. Collectively, our studies provide a rational basis for the specificity of TbpA for human transferrin, show how TbpA promotes iron release from transferrin, and elucidate how TbpB facilitates this process.en_US
dc.format.extent52:04 minutes
dc.language.isoen_USen_US
dc.publisherGeorgia Institute of Technologyen_US
dc.subjectProtein crystallographyen_US
dc.subjectBacterial pathogensen_US
dc.subjectHost-pathogen interactionsen_US
dc.titleStructural Basis for Iron Piracy by Pathogenic Neisseriaen_US
dc.typeLectureen_US
dc.typeVideoen_US
dc.contributor.corporatenameNational Institutes of Health (U.S.)


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