ArticleNature communications2023
Structure and function of the EA1 surface layer of Bacillus anthracis.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Self-assembly of surface layer protein SbsC from Geobacillus stearothermophilus and common principles of Bacilli S-layers.The Journal of biological chemistry · 2026Article
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae.Nature communications · 2025Article
- Cryo-EM structure and polar assembly of the PS2 S-layer ofProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Crystal structure of the C1 domain of the surface-layer protein SlpM from Lactobacillus brevis: a module involved in protein self-assembly.Acta crystallographica. Section F, Structural biology communications · 2025Article
- A new age in structural S-layer biology: Experimental and in silico milestones.The Journal of biological chemistry · 2025Review
- Mapping the ultrastructural topology of the corynebacterial cell surface.PLoS biology · 2025Article
- Architecture of the Sap S-layer ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular dynamics and machine learning stratify motion-dependent activity profiles of S-layer destabilizing nanobodies.PNAS nexus · 2024Article
- SymProFold: Structural prediction of symmetrical biological assemblies.Nature communications · 2024Article
- Determination of Dipicolinic Acid through the Antenna Effect of Eu(III) Coordination Polymer.Molecules (Basel, Switzerland) · 2024Article
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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 Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early and late growth phases, respectively. Here we report the nanobody-based structural characterization of EA1 and its native lattice contacts. The EA1 assembly domain consists of 6 immunoglobulin-like domains, where three calcium-binding sites structure interdomain contacts that allow monomers to adopt their assembly-competent conformation. Nanobody-induced depolymerization of EA1 S-layers results in surface defects, membrane blebbing and cell lysis under hypotonic conditions, indicating that S-layers provide additional mechanical stability to the cell wall. Taken together, we report a complete model of the EA1 S-layer and present a set of nanobodies that may have therapeutic potential against Bacillus anthracis.
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