ArticleScientific reports2016
New insights about pilus formation in gut-adapted Lactobacillus rhamnosus GG from the crystal structure of the SpaA backbone-pilin subunit.
Article in Scientific reports, 2016. 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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13 citing papers in PubMed, 25 citations in OpenAlex.
- Genomic and taxonomic characterization of strain CCM 2573: Uncovering unique genetic features and description of Macrococcus caseolyticus subsp. lactis subsp. nov.Folia microbiologica · 2026Article
- A global survey of intramolecular isopeptide bonds.Protein science : a publication of the Protein Society · 2025Article
- Determination of the Crystal Structure of the Cell Wall-Anchored Proteins and Pilins.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Variability of Genetic Characters Associated with Probiotic Functions inMicroorganisms · 2022Article
- Molecular and Cellular Mechanisms Influenced by Postbiotics.International journal of molecular sciences · 2021Review
- The divergent roles of sortase in the biology of Gram-positive bacteria.Cell surface (Amsterdam, Netherlands) · 2021Review
- LrpCBA pilus proteins of gut-dwelling Ligilactobacillus ruminis: crystallization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Crystal structure of the atypically adhesive SpaB basal pilus subunit: Mechanistic insights about its incorporation in lactobacillar SpaCBA pili.Current research in structural biology · 2020Article
- A Fast, Efficient and Easy to Implement Method to Purify Bacterial Pili FromFrontiers in microbiology · 2020Article
- SpaB, an atypically adhesive basal pilin from the lactobacillar SpaCBA pilus: crystallization and X-ray diffraction analysis.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Bent conformation of a backbone pilin N-terminal domain supports a three-stage pilus assembly mechanism.Communications biology · 2018Article
- Novel Molecular Insights about Lactobacillar Sortase-Dependent Piliation.International journal of molecular sciences · 2017Review
- Crystallization and X-ray diffraction analysis of SpaE, a basal pilus protein from the gut-adapted Lactobacillus rhamnosus GG.Acta crystallographica. Section F, Structural biology communications · 2017Article
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5 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Thus far, all solved structures of pilin-proteins comprising sortase-assembled pili are from pathogenic genera and species. Here, we present the first crystal structure of a pilin subunit (SpaA) from a non-pathogen host (Lactobacillus rhamnosus GG). SpaA consists of two tandem CnaB-type domains, each with an isopeptide bond and E-box motif. Intriguingly, while the isopeptide bond in the N-terminal domain forms between lysine and asparagine, the one in the C-terminal domain atypically involves aspartate. We also solved crystal structures of mutant proteins where residues implicated in forming isopeptide bonds were replaced. Expectedly, the E-box-substituted E139A mutant lacks an isopeptide bond in the N-terminal domain. However, the C-terminal E269A substitution gave two structures; one of both domains with their isopeptide bonds present, and another of only the N-terminal domain, but with an unformed isopeptide bond and significant conformational changes. This latter crystal structure has never been observed for any other Gram-positive pilin. Notably, the C-terminal isopeptide bond still forms in D295N-substituted SpaA, irrespective of E269 being present or absent. Although E-box mutations affect SpaA proteolytic and thermal stability, a cumulative effect perturbing normal pilus polymerization was unobserved. A model showing the polymerized arrangement of SpaA within the SpaCBA pilus is proposed.
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