ArticleMicrobial drug resistance (Larchmont, N.Y.)2014
N-acetylglucosamine deacetylases modulate the anchoring of the gamma-glutamyl capsule to the cell wall of Bacillus anthracis.
Article in Microbial drug resistance (Larchmont, N.Y.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Identification of sporulation genes in Bacillus anthracis highlights similarities and significant differences with Bacillus subtilis.PLoS biology · 2025Article
- Mechanisms conferring bacterial cell wall variability and adaptivity.Biochemical Society transactions · 2024Review
- Peptidoglycan from Bacillus anthracis Inhibits Human Macrophage Efferocytosis in Part by Reducing Cell Surface Expression of MERTK and TIM-3.ImmunoHorizons · 2024Article
- The capsule of Bacillus anthracis protects it from the bactericidal activity of human defensins and other cationic antimicrobial peptides.PLoS pathogens · 2022Article
- Peptidoglycan analysis reveals that synergistic deacetylase activity in vegetativeThe Journal of biological chemistry · 2020Article
- TheMicroorganisms · 2020Review
- Human Innate Immune Cells Respond Differentially to Poly-γ-Glutamic Acid Polymers fromJournal of immunology (Baltimore, Md. : 1950) · 2020Article
- Structural and Evolutionary Insights within the Polysaccharide Deacetylase Gene Family ofGenes · 2018Article
- Surfaceome and Proteosurfaceome in Parietal Monoderm Bacteria: Focus on Protein Cell-Surface Display.Frontiers in microbiology · 2018Review
- Microbial synthesis of poly-γ-glutamic acid: current progress, challenges, and future perspectives.Biotechnology for biofuels · 2016Review
- Two Putative Polysaccharide Deacetylases Are Required for Osmotic Stability and Cell Shape Maintenance in Bacillus anthracis.The Journal of biological chemistry · 2015Article
- Article
- Cell separation in Vibrio cholerae is mediated by a single amidase whose action is modulated by two nonredundant activators.Journal of bacteriology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus anthracis has a complex cell wall structure composed of a peptidoglycan (PG) layer to which major structures are anchored such as a neutral polysaccharide, an S-layer, and a poly-γ-D-glutamate (PDGA) capsule. Many of these structures have central roles in the biology of B. anthracis, particularly, in virulence. However, little attention has been devoted to structurally study the PG and how it is modified in the presence of these secondary cell wall components. We present here the fine structure of the PG of the encapsulated RPG1 strain harboring both pXO1 and pXO2 virulence plasmids. We show that B. anthracis has a high degree of cross-linking and its GlcNAc residues are highly modified by N-deacetylation. The PG composition is not dependent on the presence of either LPXTG proteins or the capsule. Using NMR analysis of the PG-PDGA complex, we provide evidence for the anchoring of the PDGA to the glucosamine residues. We show that anchoring of the PDGA capsule is impaired in two PG N-deacetylase mutants, Ba1961 and Ba3679. Thus, these multiple N-deactylase activities would constitute excellent drug targets in B. anthracis by simultaneously affecting its resistance to lysozyme and to phagocytosis impairing B. anthracis survival in the host.
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