Patterns of sequence and structural variation within the Neisseria meningitidis transferrin and lactoferrin receptor systems
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AbstractInvasive meningococcal disease resulting from infection by Neisseria meningitidis is the source of a substantial burden of bacterimia and meningitis in both the developed and developing worlds. Within the human host, N. meningitdis encounters a hostile environment deficient in freely available iron. In order to survive, N. meningitidis has evolved two receptor systems that sequester iron from the host iron transport glycoproteins transferrin and lactoferrin. Both the meningococcal transferrin and lactoferrin receptor systems consist of an outer membrane embedded A protein and a membrane anchored B lipoprotein. Both proteins of these systems are highly immunogenic and functionally important. The opposing selective forces of host immunity and functional necessity have resulted in complex patterns of sequence variation in the genes for these receptors. The research discussed here investigates these patterns with a focus on understanding the functional and structural factors that constrain variability.
A thesis submitted to the faculty of graduate studies in partial fulfilment of the requirements for the degree of master of science