Show simple item record

dc.contributor.authorStokes, John Vincent
dc.date.accessioned2014-03-04T02:52:54Z
dc.date.available2014-03-04T02:52:54Z
dc.date.issued2007-12
dc.identifier.otherstokes_john_v_200712_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/stokes_john_v_200712_ms
dc.identifier.urihttp://hdl.handle.net/10724/24506
dc.description.abstractWhile heterologous expression has replaced biochemical purification as the principle method for obtaining purified, authentic proteins for characterization, no single expression system has proven appropriate for all applications. Heterologous expression of Plasmodium falciparum genes has proven especially challenging due to their extreme A+T codon bias and inappropriate post-translational modifications to product made by existing expression systems. These issues have generated interest in developing a novel heterologous expression system for P. falciparum. Here, we have transfected the ciliate Tetrahymena thermophila with a novel secretion vector bearing the R2 binding region of the P. falciparum genes, ebl-1 and jsebl. In addition, we demonstrated successful expression of the R2 region. This is the first demonstration of secreted P. falciparum antigens expressed by T. thermophila. We believe T. thermophila shows promise as a heterologous expression system for P. falciparum genes.
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectPlasmodium falciparum
dc.subjectheterologous expression
dc.subjectebl-1
dc.subjectjsebl
dc.titleFunctional characterization of heterologously expressed Plasmodium falciparum ebl proteins
dc.typeThesis
dc.description.degreeMS
dc.description.departmentInfectious Diseases
dc.description.majorInfectious Diseases
dc.description.advisorDavid Peterson
dc.description.committeeDavid Peterson
dc.description.committeeHarry Dickerson
dc.description.committeeJulie Moore


Files in this item

FilesSizeFormatView

There are no files associated with this item.

This item appears in the following Collection(s)

Show simple item record