ArticleMolecular microbiology2012
Isopeptide bonds of the major pilin protein BcpA influence pilus structure and bundle formation on the surface of Bacillus cereus.
Article in Molecular microbiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Matrix plasticity and the molecular basis of extracellular filament assembly inScience advances · 2026Article
- The major toxins of Bacillus cereus - Current knowledge on distribution, regulation and mechanism of action.EXCLI journal · 2026Review
- A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025Article
- Electron cryo-microscopy reveals the structure of the archaeal thread filament.Nature communications · 2022Article
- Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.Current research in microbial sciences · 2021Review
- Article
- Isopeptide bond in collagen- and fibrinogen-binding MSCRAMMs.Biophysical reviews · 2016Review
- Article
- Structural conservation, variability, and immunogenicity of the T6 backbone pilin of serotype M6 Streptococcus pyogenes.Infection and immunity · 2014Article
- A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly.Acta crystallographica. Section D, Biological crystallography · 2014Article
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
Abstract
Bacillus cereus strains elaborate pili on their surface using a mechanism of sortase-mediated cross-linking of major and minor pilus components. Here we used a combination of electron microscopy and atomic force microscopy to visualize these structures. Pili occur as single, double or higher order assemblies of filaments formed from monomers of the major pilin, BcpA, capped by the minor pilin, BcpB. Previous studies demonstrated that within assembled pili, four domains of BcpA - CNA(1), CNA(2), XNA and CNA(3) - each acquire intramolecular lysine-asparagine isopeptide bonds formed via catalytic glutamic acid or aspartic acid residues. Here we showed that mutants unable to form the intramolecular isopeptide bonds in the CNA(2) or CNA(3) domains retain the ability to form pilus bundles. A mutant lacking the CNA(1) isopeptide bond assembled deformed pilin subunits that failed to associate as bundles. X-ray crystallography revealed that the BcpA variant Asp(312) Ala, lacking an aspartyl catalyst, did not generate the isopeptide bond within the jelly-roll structure of XNA. The Asp(312) Ala mutant was also unable to form bundles and promoted the assembly of deformed pili. Thus, structural integrity of the CNA(1) and XNA domains are determinants for the association of pili into higher order bundle structures and determine native pilus structure.
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