ArticleNature communications2023
Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM.
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 8 papers.
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Who cites it
8 citing papers in PubMed.
- The Effect ofMicroorganisms · 2026Article
- Synthesis of Ultra-Large Fibrous Proteins from Bacteria via a Looped-Translation System.bioRxiv : the preprint server for biology · 2026Article
- Ultrastructural and atomic characterization of biofilm-associated extracellular filaments in Shewanella oneidensis MR-1.Nature communications · 2026Article
- Structure first - exploration and discovery with cryo-electron microscopy.Journal of cell science · 2026Review
- An innovative strategy for overcoming ultra-high ammonia nitrogen inhibition on anaerobic methanogenesis via stepwise domestication.Microbiome · 2025Article
- Article
- Cryo-EM reconstruction of helical polymers: Beyond the simple cases.Quarterly reviews of biophysics · 2024Review
- Molecular architecture of the assembly of Bacillus spore coat protein GerQ revealed by cryo-EM.Nature communications · 2024Article
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Authors and funding
5 authors.
Funding
Abstract
Bacteria develop a variety of extracellular fibrous structures crucial for their survival, such as flagella and pili. In this study, we use cryo-EM to identify protein fibrils surrounding lab-cultured Bacillus amyloiquefaciens and discover an unreported fibril species in addition to the flagellar fibrils. These previously unknown fibrils are composed of Vpr, an extracellular serine peptidase. We find that Vpr assembles into fibrils in an enzymatically active form, potentially representing a strategy of enriching Vpr activities around bacterial cells. Vpr fibrils are also observed under other culture conditions and around other Bacillus bacteria, such as Bacillus subtilis, which may suggest a general mechanism across all Bacillus bacterial groups. Taken together, our study reveals fibrils outside the bacterial cell and sheds light on the physiological role of these extracellular fibrils.
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