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Updated: Apr 1, 2026

Generation of Null Mutants to Elucidate the Role of Bacterial Glycosyltransferases in Bacterial Motility
Published on: March 11, 2022
Sweet Talk: Protein Glycosylation in Bacterial Interaction With the Host
Qiuhe Lu1, Shan Li2, Feng Shao1
1National Institute of Biological Sciences, #7 Science Park Rd, Zhongguancun Life Science Park, Beijing, 102206, China.
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.
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