ArticleThe Journal of biological chemistry2009
A bifunctional enzyme in a single gene catalyzes the incorporation of GlcN into the Aeromonas core lipopolysaccharide.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 12 citations in OpenAlex.
- Bifunctional and monofunctional α-neoagarooligosaccharide hydrolases from Streptomyces coelicolor A3(2).Applied microbiology and biotechnology · 2023Article
- Comparative Genomics of the Aeromonadaceae Core Oligosaccharide Biosynthetic Regions.International journal of molecular sciences · 2017Article
- The FlgT Protein Is Involved in Aeromonas hydrophila Polar Flagella Stability and Not Affects Anchorage of Lateral Flagella.Frontiers in microbiology · 2016Article
- Polar Glycosylated and Lateral Non-Glycosylated Flagella from Aeromonas hydrophila Strain AH-1 (Serotype O11).International journal of molecular sciences · 2015Article
- The polar and lateral flagella from Plesiomonas shigelloides are glycosylated with legionaminic acid.Frontiers in microbiology · 2015Article
- The Polymerization of Aeromonas hydrophila AH-3 O-Antigen LPS: Concerted Action of WecP and Wzy.PloS one · 2015Article
- Role of Aeromonas hydrophila flagella glycosylation in adhesion to Hep-2 cells, biofilm formation and immune stimulation.International journal of molecular sciences · 2014Article
- A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new subgroup of the enzyme family.Journal of bacteriology · 2011Article
- Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: an update for 2009-2010.Mass spectrometry reviewsReview
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The core lipopolysaccharide (LPS) of Aeromonas hydrophila AH-3 and Aeromonas salmonicida A450 is characterized by the presence of the pentasaccharide alpha-d-GlcN-(1-->7)-l-alpha-d-Hep-(1-->2)-l-alpha-d-Hep-(1-->3)-l-alpha-d-Hep-(1-->5)-alpha-Kdo. Previously it has been suggested that the WahA protein is involved in the incorporation of GlcN residue to outer core LPS. The WahA protein contains two domains: a glycosyltransferase and a carbohydrate esterase. In this work we demonstrate that the independent expression of the WahA glycosyltransferase domain catalyzes the incorporation of GlcNAc from UDP-GlcNAc to the outer core LPS. Independent expression of the carbohydrate esterase domain leads to the deacetylation of the GlcNAc residue to GlcN. Thus, the WahA is the first described bifunctional glycosyltransferase enzyme involved in the biosynthesis of core LPS. By contrast in Enterobacteriaceae containing GlcN in their outer core LPS the two reactions are performed by two different enzymes.
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