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dc.contributor.authorCintron-Moret, Roxana
dc.date.accessioned2014-03-04T20:02:10Z
dc.date.available2014-03-04T20:02:10Z
dc.date.issued2011-08
dc.identifier.othercintron-moret_roxana_201108_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/cintron-moret_roxana_201108_ms
dc.identifier.urihttp://hdl.handle.net/10724/27424
dc.description.abstractToxoplasma gondii is an opportunistic organism in immunocompromised patients and an important cause of congenital disease. Our laboratory identified a new compartment in T. gondii which has several proteins homologous to plant vacuolar proteins, including the vacuolar proton pyrophosphatase and subunits of the vacuolar proton ATPase (V-H+-ATPase). The V-H+-ATPase is an enzyme involved in vacuolar acidification and vesicle trafficking in eukaryotic cells and we hypothesize it serves similar roles in the parasite. Two a subunits were found in the T. gondii genome and named as TgVHA-a1 and TgVHA-a2. We demonstrated that TgVHA-a1 localizes to the PLV, whereas TgVHA-a2 is associated with the plasma membrane of extracellular tachyzoites. Our studies revealed a possible role for the V-H+-ATPase in the T. gondii secretory pathway as both a subunits colocalize with TgMIC2 in a TgVP1 knockout line.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectToxoplasma gondii (T. gondii)
dc.subjectplant-like vacuole (PLV)
dc.subjectV-H+-ATPase subunit a
dc.subjectRab 7 (TgRab7)
dc.subjectvacuolar acidification
dc.subjectvesicle trafficking
dc.subjectendocytic pathway
dc.subjectbafilomycin A1
dc.subjectV-H+-PPase (TgVP1)
dc.subjectcathepsin L (TgCPL)
dc.titleThe Toxoplasma gondii vacuolar proton ATPase
dc.title.alternativecharacterization of Two proton-translocating subunits
dc.typeThesis
dc.description.degreeMS
dc.description.departmentCellular Biology
dc.description.majorCellular Biology
dc.description.advisorSilvia Moreno
dc.description.committeeSilvia Moreno
dc.description.committeeBoris Striepen
dc.description.committeeJessica Kissinger


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