Journal article
NleB2 from enteropathogenic Escherichia coli is a novel arginine-glucose transferase effector
C Giogha, NE Scott, TWF Lung, GL Pollock, M Harper, ED Goddard-Borger, JS Pearson, EL Hartland
Plos Pathogens | PUBLIC LIBRARY SCIENCE | Published : 2021
Abstract
During infection, enteropathogenic Escherichia coli (EPEC) and enterohaemorrhagic E. coli (EHEC) directly manipulate various aspects of host cell function through the translocation of type III secretion system (T3SS) effector proteins directly into the host cell. Many T3SS effector proteins are enzymes that mediate post-translational modifications of host proteins, such as the glycosyltransferase NleB1, which transfers a single N-acetylglucosamine (GlcNAc) to arginine residues, creating an Arg-GlcNAc linkage. NleB1 glycosylates death-domain containing proteins including FADD, TRADD and RIPK1 to block host cell death. The NleB1 paralogue, NleB2, is found in many EPEC and EHEC strains but to d..
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Awarded by National Health and Medical Research Council of Australia (NHMRC)
Awarded by Australian Research Council
Funding Acknowledgements
This work was funded by the National Health and Medical Research Council of Australia (NHMRC) applications APP1098826 and APP1175976 awarded to ELH and applications APP1100164 and APP1037373 awarded to NES. Salary of NES was supported by APP1037373 and FT200100270. Salary of CG was supported by APP1175976. Salary of JSP was supported by APP1159230. The work was additionally supported by a Victoria Fellowship awarded to CG. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.