CSDB: Search results

Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Campylobacter jejuni [ICD11: XN4Q5

]

NCBI PubMed ID: 34905344
Publication DOI: 10.1021/acs.chemrev.1c00729
Journal NLM ID: 2985134R
Publisher: Chem Rev
Correspondence: ben.swarts

cmich.edu
Institutions: Department of Chemistry and Biochemistry, Central Michigan University, Mount Pleasant, Michigan 48859, United States, Biochemistry, Cell, and Molecular Biology Program, Central Michigan University, Mount Pleasant, Michigan 48859, United States

Bacteria possess an extraordinary repertoire of cell envelope glycans that have critical physiological functions. Pathogenic bacteria have glycans that are essential for growth and virulence but are absent from humans, making them high-priority targets for antibiotic, vaccine, and diagnostic development. The advent of metabolic labeling with bioorthogonal chemical reporters and small-molecule fluorescent reporters has enabled the investigation and targeting of specific bacterial glycans in their native environments. These tools have opened the door to imaging glycan dynamics, assaying and inhibiting glycan biosynthesis, profiling glycoproteins and glycan-binding proteins, and targeting pathogens with diagnostic and therapeutic payload. These capabilities have been wielded in diverse commensal and pathogenic Gram-positive, Gram-negative, and mycobacterial species-including within live host organisms. Here, we review the development and applications of chemical reporters for bacterial glycans, including peptidoglycan, lipopolysaccharide, glycoproteins, teichoic acids, and capsular polysaccharides, as well as mycobacterial glycans, including trehalose glycolipids and arabinan-containing glycoconjugates. We cover in detail how bacteria-targeting chemical reporters are designed, synthesized, and evaluated, how they operate from a mechanistic standpoint, and how this information informs their judicious and innovative application. We also provide a perspective on the current state and future directions of the field, underscoring the need for interdisciplinary teams to create novel tools and extend existing tools to support fundamental and translational research on bacterial glycans.

biosynthesis, polysaccharides, glycoconjugates, glycan, Gram-negative bacteria, gram-positive bacteria

Structure type: oligomer
Location inside paper: p. 3370, Fig. 25, C. jejuni
Aglycon: Asn-X-Ser/Thr-protein
Compound class: N-glycoprotein
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_142488,IEDB_146664,IEDB_885822,IEDB_983931,SB_192

Comments, role: review;

NCBI Taxonomy refs (TaxIDs): 197
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@H]1[C@@H](NC(=O)CC(N)C(=O)O)O[C@H](C)[C@@H](NC(C)=O)[C@@H]1O[C@H]1O[C@H](CO)[C@H](O[C@H]2O[C@H](CO)[C@H](O[C@H]3O[C@H](CO)[C@H](O[C@H]4O[C@H](CO)[C@H](O[C@H]5O[C@H](CO)[C@H](O)[C@H](O)[C@H]5NC(C)=O)[C@H](O)[C@H]4NC(C)=O)[C@H](O[C@@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O)[C@H]3NC(C)=O)[C@H](O)[C@H]2NC(C)=O)[C@H](O)[C@H]1NC(C)=O

SVG MW SMILES 3D mol Ionize