Use this URL to cite or link to this record in EThOS: https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.785879
Title: Investigating the mechanisms of secretion of the moonlighting proteins Enolase and Fructose-1, 6-Bisphosphate Aldolase in Neisseria meningitidis
Author: Atwah, Banan
ISNI:       0000 0004 7971 3723
Awarding Body: University of Nottingham
Current Institution: University of Nottingham
Date of Award: 2019
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Abstract:
Neisseria meningitidis is an obligate commensal of humans that mainly colonises the nasopharynx. It is also an important cause of serious diseases, such as meningitis and sepsis. N. meningitidis uses several secretion systems (type I, type Va, type Vb, and type Vc) for secreting proteins, which enable the bacteria to modulate their cell surface and evade the human immune system. The moonlighting proteins fructose bis-1, 6-phosphate aldolase (FBA) and enolase were previously shown to localise to the surface of N. meningitidis. The mechanisms of secretion of both proteins were investigated in this study. Specifically, lysine residue 337 of enolase was substituted to investigate its role in secretion since in Escherichia coli mutation of the corresponding residue has been reported to decrease export efficiency. This study proposes that K337E substitution in meningococcal enolase causes a growth defect confirming an important functional role of this residue. However, its role in the localisation of the protein to the meningococcal cell surface is still not confirmed despite the several attempts to enhance enolase expression. The alanine residue 14 in the predicted cleavage site of the N-terminal region of FBA was substituted to investigate the role of the putative signal peptide in the surface localisation. Immunoblot analysis showed a reduction in FBA expression compared to the MC58ΔcbbA cbbAEct. Sub-cellular fractionation suggested that this mutation affected protein expression rather than its localisation to the meningococcal cell surface.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.785879  DOI: Not available
Keywords: QR Microbiology
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