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Inhibition of Membrane-Bound Lytic Transglycosylases A, B and F by Membrane-Bound Lysozyme Inhibitor of C-type Lysozyme

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dc.contributor.advisor Clarke, Dr. Anthony
dc.contributor.author Ciufo, Joseph
dc.date.accessioned 2017-12-13T13:45:17Z
dc.date.available 2019-01-01T06:00:47Z
dc.date.copyright 2017-11
dc.date.created 2017-11-29
dc.date.issued 2017-12-13
dc.identifier.uri http://hdl.handle.net/10214/12066
dc.description.abstract Peptidoglycan (PG) is an essential component of bacterial cells that forms a mesh-like sacculus that surrounds the cell. Lytic transglycosylases (LTs) are space-making enzymes that are essential for the cleavage of glycosidic linkages in the PG sacculus. This study proposes that the physiological function of the proteinaceous inhibitor, membrane-bound lysozyme inhibitor of C-type lysozyme (MliC) from P. aeruginosa, is to control LT activity from the same bacterium. This study examined the role of MliC as an inhibitor of the soluble-derivatives of membrane-bound lytic transglycosylases A (sMltA), B (sMltB) and F (sMltF). Inhibition of sMltA and sMltF was demonstrated in vitro at a 1:1 equivalent molar ratio (inhibitor: LT), and inhibition of sMltB was found at a 4:1 equivalent molar ratio using the turbidimetric assay. These results provide the first experimental evidence supporting the hypothesis that the true physiological function of MliC is to control the autolytic activity of LTs. en_US
dc.language.iso en en_US
dc.subject Peptidoglycan en_US
dc.subject Lytic Transglycosylases en_US
dc.subject MliC en_US
dc.subject Pseudomonas aeruginosa en_US
dc.subject Proteinaceous Inhibitor en_US
dc.title Inhibition of Membrane-Bound Lytic Transglycosylases A, B and F by Membrane-Bound Lysozyme Inhibitor of C-type Lysozyme en_US
dc.type Thesis en_US
dc.degree.programme Molecular and Cellular Biology en_US
dc.degree.name Master of Science en_US
dc.degree.department Department of Molecular and Cellular Biology en_US
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