ArticleScientific reports2017
Engineering a pH responsive pore forming protein.
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 14 papers.
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Who cites it
14 citing papers in PubMed, 32 citations in OpenAlex.
- Novel amino acid residues in listerolysin O drive phagosome escape and pathogenicity inVirulence · 2025Article
- Interaction of an Oomycete Nep1-like Cytolysin with Natural and Plant Cell-Mimicking Membranes.The Journal of membrane biology · 2025Article
- The membrane activity of the antimicrobial peptide caerin 1.1 is pH dependent.Biophysical journal · 2023Article
- Single-molecule tracking of perfringolysin O assembly and membrane insertion uncoupling.The FEBS journal · 2023Article
- Synthetic cells in biomedical applications.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnology · 2022Review
- Bacterial pore-forming toxins.Microbiology (Reading, England) · 2022Article
- Toxic proteins application in cancer therapy.Molecular biology reports · 2021Review
- Cytotoxic Activity of LLO Y406A Is Targeted to the Plasma Membrane of Cancer Urothelial Cells.International journal of molecular sciences · 2021Article
- Lysenin Channels as Sensors for Ions and Molecules.Sensors (Basel, Switzerland) · 2020Review
- Design of Protein Logic Gate System Operating on Lipid Membranes.ACS synthetic biology · 2020Article
- Advances on Tumor-Targeting Delivery of Cytotoxic Proteins.ACS pharmacology & translational science · 2020Review
- Engineering Allostery into Proteins.Advances in experimental medicine and biology · 2019Review
- Cholesterol-dependent cytolysins: from water-soluble state to membrane pore.Biophysical reviews · 2018Review
- Lysenin Toxin Membrane Insertion Is pH-Dependent but Independent of Neighboring Lysenins.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 1 country.
Funding
Abstract
Listeriolysin O (LLO) is a cytolysin capable of forming pores in cholesterol-rich lipid membranes of host cells. It is conveniently suited for engineering a pH-governed responsiveness, due to a pH sensor identified in its structure that was shown before to affect its stability. Here we introduced a new level of control of its hemolytic activity by making a variant with hemolytic activity that was pH-dependent. Based on detailed structural analysis coupled with molecular dynamics and mutational analysis, we found that the bulky side chain of Tyr406 allosterically affects the pH sensor. Molecular dynamics simulation further suggested which other amino acid residues may also allosterically influence the pH-sensor. LLO was engineered to the point where it can, in a pH-regulated manner, perforate artificial and cellular membranes. The single mutant Tyr406Ala bound to membranes and oligomerized similarly to the wild-type LLO, however, the final membrane insertion step was pH-affected by the introduced mutation. We show that the mutant toxin can be activated at the surface of artificial membranes or living cells by a single wash with slightly acidic pH buffer. Y406A mutant has a high potential in development of novel nanobiotechnological applications such as controlled release of substances or as a sensor of environmental pH.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.