Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Acinetobacter baumannii [ICD11:
XN8LS 
]
The structure was elucidated in this paperNCBI PubMed ID: 23747578Publication DOI: 10.1016/j.abb.2013.05.011Journal NLM ID: 0372430Correspondence: B. Imperiali <imper
mit.edu>
Institutions: Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, United States, Department of Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, United States
The Gram-negative, opportunistic pathogen Acinetobacter baumannii has recently captured headlines due to its ability to circumvent current antibiotic therapies. Herein we show that the multi-drug resistant (MDR) AYE strain of A. baumannii contains a gene locus that encodes three enzymes responsible for the biosynthesis of the highly-modified bacterial nucleotide sugar, UDP-N,N'-diacetylbacillosamine (UDP-diNAcBac). Previously, this UDP-sugar has been implicated in the pgl pathway of Campylobacter jejuni. Here we report the overexpression, purification, and biochemical characterization of the A. baumannii enzymes WeeK, WeeJ, and WeeI that are responsible for the production of UDP-diNAcBac. We also demonstrate the function of the phosphoglycosyltransferase (WeeH), which transfers the diNAcBac moiety to undecaprenyl-phosphate. UDP-diNAcBac biosynthesis in A. baumannii is also directly compared to the homologous pathways in the pathogens C. jejuni and Neisseria gonorrhoeae. This work demonstrates for the first time the ability of A. baumannii to generate the highly-modified, UDP-diNAcBac nucleotide sugar found previously in other bacteria adding to the growing list of pathogens that assemble glycoconjugates including bacillosamine. Additionally, characterization of these pathway enzymes highlights the opportunity for investigating the significance of highly-modified sugars in bacterial pathogenesis.
biosynthesis, Acinetobacter baumannii, bacillosamine, acetyltransferases, aminotransferase, bacterial O-linked glycosylation, UDP-diNAcBac
Structure type: monomer
Location inside paper: p.73, fig.1
Trivial name: UDP-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose, UDP-2,4-diacetamido-Bacillose, UDP-N,N-diacetylbacillosamine, UPD-2,4-diacetamido-2,4,6-trideoxy-α-D-glucopyranose, UDP-N,N'-diacetyl-bacillosamine, UDP-Bac2Ac4Ac, UDP-diNAcBac
Compound class: nucleoside diphosphate sugar
Methods: SDS-PAGE, DNA techniques, glycosyltransferase assays, kinetics assays, genetic methods, biochemical methods, CE
Enzymes that release or process the structure: Week, Weej, WeeI
NCBI Taxonomy refs (TaxIDs): 509173
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There is only one chemically distinct structure:
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