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Mutant Group B Streptococcus surface expressed Phosphoglycerate kinase (PGK) with reduced plasminogen binding Open Access


Other title
Phosphoglycerate kinase
Type of item
Degree grantor
University of Alberta
Author or creator
Siddiqua, Khalida
Supervisor and department
Tyrrell, Gregory (Laboratory Medicine and Pathology)
Examining committee member and department
Fuller, Jeff (Division of Medical Microbiology)
Chui, Linda (Laboratory Medicine and Pathology)
Keelan, Monika (Laboratory Medicine and Pathology)
Medical Sciences- Laboratory Medicine and Pathology

Date accepted
Graduation date
Master of Science
Degree level
Group B streptococcus (GBS) is a Gram-positive streptococcus bacterium that can cause severe invasive disease in the human neonate. This can manifest as pneumonia, septicemia and meningitis. While antibiotic prophylaxis has reduced the incidence GBS disease in the neonatal population, it is still the one of the leading cause of neonatal invasive disease in North America including Alberta. Phosphoglycerate kinase (PGK), a glycolytic enzyme, has been demonstrated to be on the surface of GBS. Surface expressed GBS-PGK interacts with the hostcell protein plasminogen, which is thought to help bacteria invade further into the host by destruction of host barriers. In this thesis, a triple mutant GBS-PGK molecule PGK-M9 was created based on information from a space-filled model of PGK-plasminogen interaction sites. PGK-M9 bound 95% less plasminogen than the wild type GBS-PGK. This mutant will permit further investigation into the role of surface GBS-PGK in vivo models of GBS infection.
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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