The development of a new reporter system to study the interaction between FbpA and FbpBC

Bacteria require efficient iron acquisition systems to infect and colonize the mammalian host. Neisseriaceae and Pasteurellaceae have developed an iron uptake system that involves iron removal from host glycoproteins. The human pathogen, Haemophilus influenzae, has a surface receptor complex containing transferrin binding proteins (TbpA and TbpB). This complex facilitates the release of iron from host transferrin and into the periplasm, where it binds to a periplasmic binding protein, ferric binding protein (FbpA). FbpA is part of the ABC transporter, FbpABC that transports iron from the periplasm into the cytoplasm. The interaction between FbpA and FbpBC is currently unknown. A series of site directed mutants were created to study this interaction based on models of other ABC transporters. We have developed a new novel reporter system to study this interaction. The results of this study have shown the lux reporter system to be more advantageous than past methods that evaluated iron uptake systems.

Name thesis:degree_name

Master of Science (MSc)

Discipline thesis:degree_discipline

Biochemistry and Molecular Biology

Grantor dc:publisher.institution

Graduate Studies

Year dc:date.issued

2013

Author dc:creator

• Tang, Alexander

Advisor dc:contributor.advisor

• Schryvers, Anthony

• Microbiology
• Biology--Molecular

Statement dc:rights

• University of Calgary graduate students retain copyright ownership and moral rights for their thesis. You may use this material in any way that is permitted by the Copyright Act or through licensing that has been assigned to the document. For uses that are not allowable under copyright legislation or licensing, you are required to seek permission.

Language dc:language.iso

eng

DOI

http://dx.doi.org/10.11575/PRISM/28055

OAI identifier oai:identifier

oai:ucalgary.scholaris.ca:11023/1200