ArticleThe Journal of biological chemistry2015
The protein BpsB is a poly-β-1,6-N-acetyl-D-glucosamine deacetylase required for biofilm formation in Bordetella bronchiseptica.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 36 citations in OpenAlex.
- Biochemical and Structural Characterization of Two-domain Glycoside Hydrolase PgaB fromACS infectious diseases · 2026Article
- Klebsiella aerogenes PgaB orthologue can efficiently hydrolyze Staphylococcus aureus biofilms.World journal of microbiology & biotechnology · 2025Article
- Article
- Variations of the NodB Architecture Are Attuned to Functional Specificities into and beyond the Carbohydrate Esterase Family 4.Biomolecules · 2024Article
- Small Molecule Inhibition of an Exopolysaccharide Modification Enzyme is a Viable Strategy To Block Pseudomonas aeruginosa Pel Biofilm Formation.Microbiology spectrum · 2023Article
- The deficiency of poly-β-1,6-N-acetyl-glucosamine deacetylase trigger A. baumannii to convert to biofilm-independent colistin-tolerant cells.Scientific reports · 2023Article
- The Pel polysaccharide is predominantly composed of a dimeric repeat of α-1,4 linked galactosamine and N-acetylgalactosamine.Communications biology · 2022Article
- Structural and biochemical characterization of the exopolysaccharide deacetylase Agd3 required for Aspergillus fumigatus biofilm formation.Nature communications · 2020Article
- Investigation of LuxS-mediated quorum sensing inJournal of medical microbiology · 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
- Deacetylated microbial biofilm exopolysaccharides: It pays to be positive.PLoS pathogens · 2018Review
- PgaB orthologues contain a glycoside hydrolase domain that cleaves deacetylated poly-β(1,6)-N-acetylglucosamine and can disrupt bacterial biofilms.PLoS pathogens · 2018Article
- Bordetella Pertussis virulence factors in the continuing evolution of whooping cough vaccines for improved performance.Medical microbiology and immunology · 2018Review
- Substrate Recognition and Specificity of Chitin Deacetylases and Related Family 4 Carbohydrate Esterases.International journal of molecular sciences · 2018Review
- Structural and chemical biology of deacetylases for carbohydrates, proteins, small molecules and histones.Communications biology · 2018Review
- Structural and functional analysis of de-N-acetylase PgaB from periodontopathogen Aggregatibacter actinomycetemcomitans.Molecular oral microbiology · 2017Article
- Biofilm Exopolysaccharides of Pathogenic Fungi: Lessons from Bacteria.The Journal of biological chemistry · 2016Review
- Bordetella biofilms: a lifestyle leading to persistent infections.Pathogens and disease · 2016Review
- Sph3 Is a Glycoside Hydrolase Required for the Biosynthesis of Galactosaminogalactan in Aspergillus fumigatus.The Journal of biological chemistry · 2015Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Bordetella pertussis and Bordetella bronchiseptica are the causative agents of whooping cough in humans and a variety of respiratory diseases in animals, respectively. Bordetella species produce an exopolysaccharide, known as the Bordetella polysaccharide (Bps), which is encoded by the bpsABCD operon. Bps is required for Bordetella biofilm formation, colonization of the respiratory tract, and confers protection from complement-mediated killing. In this report, we have investigated the role of BpsB in the biosynthesis of Bps and biofilm formation by B. bronchiseptica. BpsB is a two-domain protein that localizes to the periplasm and outer membrane. BpsB displays metal- and length-dependent deacetylation on poly-β-1,6-N-acetyl-d-glucosamine (PNAG) oligomers, supporting previous immunogenic data that suggests Bps is a PNAG polymer. BpsB can use a variety of divalent metal cations for deacetylase activity and showed highest activity in the presence of Ni(2+) and Co(2+). The structure of the BpsB deacetylase domain is similar to the PNAG deacetylases PgaB and IcaB and contains the same circularly permuted family four carbohydrate esterase motifs. Unlike PgaB from Escherichia coli, BpsB is not required for polymer export and has unique structural differences that allow the N-terminal deacetylase domain to be active when purified in isolation from the C-terminal domain. Our enzymatic characterizations highlight the importance of conserved active site residues in PNAG deacetylation and demonstrate that the C-terminal domain is required for maximal deacetylation of longer PNAG oligomers. Furthermore, we show that BpsB is critical for the formation and complex architecture of B. bronchiseptica biofilms.
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