Journal article
Mutagenesis and functional analysis of the bacterial arginine glycosyltransferase effector NleB1 from enteropathogenic Escherichia coli
T Wong Fok Lung, C Giogha, K Creuzburg, SY Ong, GL Pollock, Y Zhang, KY Fung, JS Pearson, EL Hartland
Infection and Immunity | AMER SOC MICROBIOLOGY | Published : 2016
DOI: 10.1128/IAI.01523-15
Abstract
Enteropathogenic Escherichia coli (EPEC) interferes with host cell signaling by injecting virulence effector proteins into enterocytes via a type III secretion system (T3SS). NleB1 is a novel T3SS glycosyltransferase effector from EPEC that transfers a single N-acetylglucosamine (GlcNAc) moiety in an N-glycosidic linkage to Arg117 of the Fas-associated death domain protein (FADD). GlcNAcylation of FADD prevents the assembly of the canonical death-inducing signaling complex and inhibits Fas ligand (FasL)-induced cell death. Apart from the DXD catalytic motif of NleB1, little is known about other functional sites in the enzyme. In the present study, members of a library of 22 random transposon..
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Awarded by Department of Health \ National Health and Medical Research Council (NHMRC)
Funding Acknowledgements
This work, including the efforts of Elizabeth L. Hartland, was funded by Department of Health vertical bar National Health and Medical Research Council (NHMRC) (APP1044061). This work, including the efforts of Jaclyn Pearson, was funded by Department of Health vertical bar National Health and Medical Research Council (NHMRC) (APP1090108).