Review of phosphocholine substituents on bacterial pathogen glycans: Synthesis, structures and interactions with host proteins

From National Research Council Canada

DOI	Resolve DOI: https://doi.org/10.1016/j.molimm.2013.05.237
Author	Search for: Young, N.M.¹; Search for: Foote, S.J.¹; Search for: Wakarchuk, W.W.
Affiliation	National Research Council of Canada. Human Health Therapeutics
Format	Text, Article
Subject	C reactive protein; citicoline; glycan; major histocompatibility antigen class 2; phosphorylcholine; protein; teichoic acid; toll like receptor 4; adaptive immunity; Haemophilus influenzae; Histophilus somni; innate immunity; Morganella morganii; Pasteurella multocida; protein protein interaction; protein structure; protein synthesis; review; Streptococcus pneumoniae
Abstract	Among the non-carbohydrate components of glycans, the addition of phosphocholine (ChoP) to the glycans of pathogens occurs more rarely than acetylation or methylation, but it has far more potent biological consequences. These arise from ChoP's multiple interactions with host proteins, which are important at all stages of the infection process. These stages include initial adherence to cells, encountering the host's innate immune system and then the adaptive immune system. Thus, in the initial stages of an infection, ChoP groups are an asset to the pathogen, but they can turn into a disadvantage subsequently. In this review, we have focussed on structural aspects of these phenomena. We describe the biosynthesis of the ChoP modification, the structures of the pathogen glycans known to carry ChoP groups and the host proteins that recognize ChoP. © 2013 The Authors.
Publication date	2013
In	Molecular Immunology 56, no. 4 (2013): 563–573.
Language	English
Peer reviewed	Yes
NPARC number	21269731
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Record identifier	461798e6-f7eb-4b15-89db-b8a9291baf50
Record created	2013-12-13
Record modified	2020-04-22

Date modified:: 2024-10-31