ArticleThe Journal of biological chemistry2014
Structural basis for the De-N-acetylation of Poly-β-1,6-N-acetyl-D-glucosamine in Gram-positive bacteria.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
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- Biochemical and Structural Characterization of Two-domain Glycoside Hydrolase PgaB fromACS infectious diseases · 2026Article
- Bacillus cereus PelAThe Journal of biological chemistry · 2026Article
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- Enzyme therapy as a promising strategy to overcome multi-drug resistance in pathogens: current advances, key challenges, and future directions.RSC advances · 2026Review
- Structural and functional analysis of Pseudomonas aeruginosa PelA provides insight into the modification of the Pel exopolysaccharide.The Journal of biological chemistry · 2025Article
- Variations of the NodB Architecture Are Attuned to Functional Specificities into and beyond the Carbohydrate Esterase Family 4.Biomolecules · 2024Article
- Strategy to combat biofilms: a focus on biofilm dispersal enzymes.NPJ biofilms and microbiomes · 2023Review
- PplD is a de-N-acetylase of the cell wall linkage unit of streptococcal rhamnopolysaccharides.Nature communications · 2022Article
- Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation.Nature communications · 2020Article
- A systematic pipeline for classifying bacterial operons reveals the evolutionary landscape of biofilm machineries.PLoS computational biology · 2020Article
- Structural and biochemical insights into the catalytic mechanisms of two insect chitin deacetylases of the carbohydrate esterase 4 family.The Journal of biological chemistry · 2019Article
- Transcriptional Regulation ofJournal of bacteriology · 2019Article
- Substrate Recognition and Specificity of Chitin Deacetylases and Related Family 4 Carbohydrate Esterases.International journal of molecular sciences · 2018Review
- The antifungal caspofungin increases fluoroquinolone activity against Staphylococcus aureus biofilms by inhibiting N-acetylglucosamine transferase.Nature communications · 2016Article
- The exceptionally broad-based potential of active and passive vaccination targeting the conserved microbial surface polysaccharide PNAG.Expert review of vaccines · 2016Review
- Article
- Insights into the structure and function of membrane-integrated processive glycosyltransferases.Current opinion in structural biology · 2015Review
- The protein BpsB is a poly-β-1,6-N-acetyl-D-glucosamine deacetylase required for biofilm formation in Bordetella bronchiseptica.The Journal of biological chemistry · 2015Article
- Identification of Poly-N-acetylglucosamine as a Major Polysaccharide Component of the Bacillus subtilis Biofilm Matrix.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Exopolysaccharides are required for the development and integrity of biofilms produced by a wide variety of bacteria. In staphylococci, partial de-N-acetylation of the exopolysaccharide poly-β-1,6-N-acetyl-d-glucosamine (PNAG) by the extracellular protein IcaB is required for biofilm formation. To understand the molecular basis for PNAG de-N-acetylation, the structure of IcaB from Ammonifex degensii (IcaBAd) has been determined to 1.7 Å resolution. The structure of IcaBAd reveals a (β/α)7 barrel common to the family four carbohydrate esterases (CE4s) with the canonical motifs circularly permuted. The metal dependence of IcaBAd is similar to most CE4s showing the maximum rates of de-N-acetylation with Ni(2+), Co(2+), and Zn(2+). From docking studies with β-1,6-GlcNAc oligomers and structural comparison to PgaB from Escherichia coli, the Gram-negative homologue of IcaB, we identify Arg-45, Tyr-67, and Trp-180 as key residues for PNAG binding during catalysis. The absence of these residues in PgaB provides a rationale for the requirement of a C-terminal domain for efficient deacetylation of PNAG in Gram-negative species. Mutational analysis of conserved active site residues suggests that IcaB uses an altered catalytic mechanism in comparison to other characterized CE4 members. Furthermore, we identified a conserved surface-exposed hydrophobic loop found only in Gram-positive homologues of IcaB. Our data suggest that this loop is required for membrane association and likely anchors IcaB to the membrane during polysaccharide biosynthesis. The work presented herein will help guide the design of IcaB inhibitors to combat biofilm formation by staphylococci.
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Registered trials
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