ArticleScientific reports2017
Structural, physicochemical and dynamic features conserved within the aerolysin pore-forming toxin family.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 66 citations in OpenAlex.
- Article
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- Aerolysin-like proteins fromFrontiers in fungal biology · 2026Article
- Single-Photon Single-Particle Tracking.bioRxiv : the preprint server for biology · 2025Article
- A nut-and-bolt assembly of the bimodular large progenitor botulinum neurotoxin complex.Science advances · 2025Article
- Structural insights into pre-pore intermediates of alpha-hemolysin in the lipidic environment.Nature communications · 2025Article
- The structural features and immunological role of biomphalysins in the snail Biomphalaria glabrata.PLoS pathogens · 2025Article
- Dissecting the Membrane Association Mechanism of Aerolysin Pores at Femtomolar Concentrations Using Water as a Probe.Nano letters · 2024Article
- The Molecular Architecture and Mode of Action ofToxins · 2024Review
- Deep Learning-Assisted Single-Molecule Detection of Protein Post-translational Modifications with a Biological Nanopore.ACS nano · 2024Article
- Lessons on fruiting body morphogenesis from genomes and transcriptomes ofStudies in mycology · 2023Article
- Article
- Article
- The Crystal Structure ofToxins · 2022Article
- Interaction ofToxins · 2022Article
- The choanoflagellate pore-forming lectin SaroL-1 punches holes in cancer cells by targeting the tumor-related glycosphingolipid Gb3.Communications biology · 2022Article
- Sanguinarine Protects Channel Catfish againstPathogens (Basel, Switzerland) · 2022Article
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Prevalence and genetic diversity ofFrontiers in microbiology · 2022Article
- The Natterin Proteins Diversity: A Review on Phylogeny, Structure, and Immune Function.Toxins · 2021Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aerolysin is the founding member of a major class of β-pore-forming toxins (β-PFTs) found throughout all kingdoms of life. PFTs are cytotoxic proteins produced as soluble monomers, which oligomerize at the membrane of target host cells forming pores that may lead to osmotic lysis and cell death. Besides their role in microbial infection, they have become interesting for their potential as biotechnological sensors and delivery systems. Using an approach that integrates bioinformatics with molecular modeling and simulation, we looked for conserved features across this large toxin family. The cell surface-binding domains present high variability within the family to provide membrane receptor specificity. On the contrary, the novel concentric double β-barrel structure found in aerolysin is highly conserved in terms of sequence, structure and conformational dynamics, which likely contribute to preserve a common transition mechanism from the prepore to the mature pore within the family.Our results point to the key role of several amino acids in the conformational changes needed for oligomerization and further pore formation, such as Y221, W227, P248, Q263 and L277, which we propose are involved in the release of the stem loop and the two adjacent β-strands to form the transmembrane β-barrel.
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