title: Sweet Talk: Protein Glycosylation in Bacterial Interaction With the Host.
abstract: Pathogenic bacteria encode virulent glycosyltransferases that conjugate various glycans onto substrate proteins via the N- or O-linkage. The HMW system in nontypeable Haemophilus influenzae and the Pgl system in Campylobacter jejuni glycosylate bacterial surface or periplasmic proteins at the eukaryotic-like Asn-X-Ser/Thr motif. The NleB effector from enterobacteria mediates arginine GlcNAcylation of host death-domain proteins to block inflammation, representing an atypical N-glycosylation. The large clostridial cytotoxins and related glucosyltransferase toxins from Legionella and Photorhabdus monoglycosylate a serine/threonine or tyrosine in host Rho GTPase or elongation factor 1A (eEF1A). The emerging bacterial autotransporter heptosyltransferase (BAHT) family of heptosyltransferases also catalyses O-glycosylation and modifies autotransporters for adhesion to the host. These glycosylations, diverse in linkages and glycan structures, determine appropriate functioning of bacterial virulence factors or hijack host cellular processes in pathogenesis.
authors.affiliation: National Institute of Biological Sciences, #7 Science Park Rd, Zhongguancun Life Science Park, Beijing, 102206, China.
authors.forename: Qiuhe
authors.initials: Q
authors.lastname: Lu
authors.affiliation: National Institute of Biological Sciences, #7 Science Park Rd, Zhongguancun Life Science Park, Beijing, 102206, China; Taihe Hospital, Hubei University of Medicine, Shiyan, Hubei, 442000, China.
authors.forename: Shan
authors.initials: S
authors.lastname: Li
authors.affiliation: National Institute of Biological Sciences, #7 Science Park Rd, Zhongguancun Life Science Park, Beijing, 102206, China. Electronic address: shaofeng@nibs.ac.cn.
authors.forename: Feng
authors.initials: F
authors.lastname: Shao
mesh_terms: D000818:Animals; D001422:Bacterial Adhesion / Q000502:physiology*; D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D006031:Glycosylation; D016695:Glycosyltransferases / Q000235:genetics / Q000378:metabolism; D006801:Humans
chemical_list: D001426:Bacterial Proteins; D016695:Glycosyltransferases
keywords: arginine GlcNAcylation; autotransporters; bacterial adhesion; heptosylation; inflammatory responses; protein glycosylation