Overexpression and secretion of proaerolysin by Aeromonas salmonicida by Sarah Ellen Burr.

Simple item page
dc.contributor.authorBurr, Sarah Ellenen_US
dc.date.accessioned2024-08-13T00:06:58Z
dc.date.available2024-08-13T00:06:58Z
dc.date.copyright2001en_US
dc.date.issued2001
dc.degree.departmentDepartment of Biochemistry and Microbiology
dc.degree.levelMaster of Science M.Sc.en
dc.description.abstractAerolysin, a pore-forming toxin produced by Aeromonas species, is secreted as an inactive protoxin (proaerolysin) via the General Secretion Pathway. Recombinant PCR was used to generate proaerolysin variants containing internal deletions in key regions of the protein. This provided a means by which to study the role these protein domains play in proaerolysin secretion. Three proaerolysin variants could not be secreted by A. salmonicida and were shown to fold incorrectly within the cell. Overexpression of proaerolysin by A. salmonicida resulted in an increase in toxin secretion into the extracellular medium and an accumulation of toxin within the cells. Further examination carried out using pulse-chase analysis indicated that the cells contain two distinct pools of proaerolysin; one that is rapidly secreted by the cell and a second that is not readily available for secretion. Electron microscopic examination of A. salmonicida indicated that intracellular proaerolysin accumulates within an enlarged periplasm. The results obtained suggest that there is a limit to the amount of protein that can be efficiently exported from the cell via the General Secretion Pathway.
dc.format.extent129 pages
dc.identifier.urihttps://hdl.handle.net/1828/17146
dc.rightsAvailable to the World Wide Weben_US
dc.titleOverexpression and secretion of proaerolysin by Aeromonas salmonicida by Sarah Ellen Burr.en_US
dc.typeThesisen_US

Files

Original bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
BURR_Sarah_Ellen_MSC_2001_1041711.pdf
Size:
39.78 MB
Format:
Adobe Portable Document Format
Download

Collections

Electronic Theses and Dissertations (ETD)
 
University of Victoria Libraries

We acknowledge and respect the Lək̓ʷəŋən (Songhees and Esquimalt) Peoples on whose territory the university stands, and the Lək̓ʷəŋən and W̱SÁNEĆ Peoples whose historical relationships with the land continue to this day.