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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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Title: Inhibition of Membrane-Bound Lytic Transglycosylases A, B and F by Membrane-Bound Lysozyme Inhibitor of C-type Lysozyme
Author: Ciufo, Joseph
Department: Department of Molecular and Cellular Biology
Program: Molecular and Cellular Biology
Advisor: Clarke, Dr. Anthony
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.
URI: http://hdl.handle.net/10214/12066
Date: 2017-11


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