ArticleScientific reports2018
Disruption of the open conductance in the β-tongue mutants of Cytolysin A.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Pore-Forming Toxin-Like Proteins in the Anti-Parasitoid Immune Response of Drosophila.Journal of innate immunity · 2025Article
- Nanopore-Based Fingerprint Immunoassay Based on Rolling Circle Amplification and DNA Fragmentation.ACS nano · 2023Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Cytolysin A (ClyA) is a water-soluble alpha pore-forming toxin that assembles to form an oligomeric pore on host cell membranes. The ClyA monomer possesses an α-helical bundle with a β-sheet subdomain (the β-tongue) previously believed to be critical for pore assembly and/or insertion. Oligomerization of ClyA pores transforms the β-tongue into a helix-turn-helix that embeds into the lipid bilayer. Here, we show that mutations of the β-tongue did not prevent oligomerization or transmembrane insertion. Instead, β-tongue substitution mutants yielded pores with decreased conductance while a deletion mutation resulted in pores that rapidly closed following membrane association. Our results suggest that the β-tongue may play an essential structural role in stabilizing the open conformation of the transmembrane domain.
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Registered trials
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