Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: nosocomial infections [ICD11:
XB25 
];
infection due to Acinetobacter baumannii [ICD11:
XN8LS ]
NCBI PubMed ID: 34630370Publication DOI: 10.3389/fmicb.2021.745702Journal NLM ID: 101548977Publisher: Lausanne: Frontiers Research Foundation
Correspondence: Marthe T.C. Walvoort <m.t.c.walvoort
rug.nl>
Institutions: Faculty of Science and Engineering, Stratingh Institute for Chemistry, University of Groningen, Groningen, The Netherlands
Glycosylation is a ubiquitous process that is universally conserved in nature. The various products of glycosylation, such as polysaccharides, glycoproteins, and glycolipids, perform a myriad of intra- and extracellular functions. The multitude of roles performed by these molecules is reflected in the significant diversity of glycan structures and linkages found in eukaryotes and prokaryotes. Importantly, glycosylation is highly relevant for the virulence of many bacterial pathogens. Various surface-associated glycoconjugates have been identified in bacteria that promote infectious behavior and survival in the host through motility, adhesion, molecular mimicry, and immune system manipulation. Interestingly, bacterial glycosylation systems that produce these virulence factors frequently feature rare monosaccharides and unusual glycosylation mechanisms. Owing to their marked difference from human glycosylation, bacterial glycosylation systems constitute promising antibacterial targets. With the rise of antibiotic resistance and depletion of the antibiotic pipeline, novel drug targets are urgently needed. Bacteria-specific glycosylation systems are especially promising for antivirulence therapies that do not eliminate a bacterial population, but rather alleviate its pathogenesis. In this review, we describe a selection of unique glycosylation systems in bacterial pathogens and their role in bacterial homeostasis and infection, with a focus on virulence factors. In addition, recent advances to inhibit the enzymes involved in these glycosylation systems and target the bacterial glycan structures directly will be highlighted. Together, this review provides an overview of the current status and promise for the future of using bacterial glycosylation to develop novel antibacterial strategies.
glycosylation, pathogenic bacteria, metabolic oligosaccharide engineering, antibacterial strategies, antivirulence
Structure type: polymer chemical repeating unit
Location inside paper: Fig. 4B, A. baumannii K83
The structure in this paper was incorrect:
Trivial name: K83 CPS
Compound class: CPS
Contained glycoepitopes: IEDB_135813,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_142488,IEDB_146664,IEDB_151531,IEDB_225177,IEDB_885823,IEDB_983931,SB_192,SB_74,SB_85
Comments, role: review
NCBI Taxonomy refs (TaxIDs): 470Reference(s) to other database(s): GTC:G20936VX
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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