ArticleThe Journal of biological chemistry2012
Defining function of lipopolysaccharide O-antigen ligase WaaL using chemoenzymatically synthesized substrates.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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Who cites it
40 citing papers in PubMed.
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- Dual function of the O-antigen WaaL ligase of Aggregatibacter actinomycetemcomitans.Molecular oral microbiology · 2023Article
- Burkholderia contaminans Bacteriophage CSP3 Requires O-Antigen Polysaccharides for Infection.Microbiology spectrum · 2023Article
- Bioinformatic analysis of structures and encoding genes of Escherichia coli surface polysaccharides sheds light on the heterologous biosynthesis of glycans.BMC genomics · 2023Article
- Lipopolysaccharide biosynthesis and traffic in the envelope of the pathogen Brucella abortus.Nature communications · 2023Article
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- Inflammation-type dysbiosis of the oral microbiome associates with the duration of COVID-19 symptoms and long COVID.JCI insight · 2021Article
- Exopolysaccharide anchoring creates an extreme resistance to sedimentation.Journal of bacteriology · 2021Article
- Assembly and Maintenance of Lipids at the Bacterial Outer Membrane.Chemical reviews · 2021Review
- Border Control: Regulating LPS Biogenesis.Trends in microbiology · 2021Review
- Bacterial Glycoengineering as a Biosynthetic Route to Customized Glycomolecules.Advances in biochemical engineering/biotechnology · 2021Article
- Structure and genetics of Escherichia coli O antigens.FEMS microbiology reviews · 2020Review
- Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020Review
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9 authors.
Funding
Abstract
The WaaL-mediated ligation of O-antigen onto the core region of the lipid A-core block is an important step in the lipopolysaccharide (LPS) biosynthetic pathway. Although the LPS biosynthesis has been largely characterized, only a limited amount of in vitro biochemical evidence has been established for the ligation reaction. Such limitations have primarily resulted from the barriers in purifying WaaL homologues and obtaining chemically defined substrates. Accordingly, we describe herein a chemical biology approach that enabled the reconstitution of this ligation reaction. The O-antigen repeating unit (O-unit) of Escherichia coli O86 was first enzymatically assembled via sequential enzymatic glycosylation of a chemically synthesized GalNAc-pyrophosphate-undecaprenyl precursor. Subsequent expression of WaaL through use of a chaperone co-expression system then enabled the demonstration of the in vitro ligation between the synthesized donor (O-unit-pyrophosphate-undecaprenyl) and the isolated lipid A-core acceptor. The previously reported ATP and divalent metal cation dependence were not observed using this system. Further analyses of other donor substrates revealed that WaaL possesses a highly relaxed specificity toward both the lipid moiety and the glycan moiety of the donor. Lastly, three conserved amino acid residues identified by sequence alignment were found essential for the WaaL activity. Taken together, the present work represents an in vitro systematic investigation of the WaaL function using a chemical biology approach, providing a system that could facilitate the elucidation of the mechanism of WaaL-catalyzed ligation reaction.
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