ArticleToxins2015
Role of acidic residues in helices TH8-TH9 in membrane interactions of the diphtheria toxin T domain.
Article in Toxins, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Novel PE-DT-fusion toxin enhances internalization and target-dependently restores the cytotoxicity of recombinant immunotoxins.Frontiers in pharmacology · 2026Article
- The Role of a Conserved Arg-Asp Pair in the Structure and Function of Tetanus Neurotoxin.Toxins · 2025Article
- Constant-pH MD simulations of the protonation-triggered conformational switching in diphtheria toxin translocation domain.Biophysical journal · 2024Article
- An enhanced intracellular delivery platform based on a distant diphtheria toxin homolog that evades pre-existing antitoxin antibodies.EMBO molecular medicine · 2024Article
- Unconventional structure and mechanisms for membrane interaction and translocation of the NF-κB-targeting toxin AIP56.Nature communications · 2023Article
- Membrane interactions of apoptotic inhibitor Bcl-xL: What can be learned using fluorescence spectroscopy.BBA advances · 2023Article
- Spectroscopic evidence of tetanus toxin translocation domain bilayer-induced refolding and insertion.Biophysical journal · 2021Article
- Review
- Conformational switching, refolding and membrane insertion of the diphtheria toxin translocation domain.Methods in enzymology · 2021Article
- Review
- TheThe Journal of biological chemistry · 2018Article
- Refining Protein Penetration into the Lipid Bilayer Using Fluorescence Quenching and Molecular Dynamics Simulations: The Case of Diphtheria Toxin Translocation Domain.The Journal of membrane biology · 2018Article
- Article
- The pH-Dependent Trigger in Diphtheria Toxin T Domain Comes with a Safety Latch.Biophysical journal · 2016Article
- Microsecond Simulations of the Diphtheria Toxin Translocation Domain in Association with Anionic Lipid Bilayers.The journal of physical chemistry. B · 2015Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The pH-triggered membrane insertion of the diphtheria toxin translocation domain (T domain) results in transferring the catalytic domain into the cytosol, which is relevant to potential biomedical applications as a cargo-delivery system. Protonation of residues is suggested to play a key role in the process, and residues E349, D352 and E362 are of particular interest because of their location within the membrane insertion unit TH8-TH9. We have used various spectroscopic, computational and functional assays to characterize the properties of the T domain carrying the double mutation E349Q/D352N or the single mutation E362Q. Vesicle leakage measurements indicate that both mutants interact with the membrane under less acidic conditions than the wild-type. Thermal unfolding and fluorescence measurements, complemented with molecular dynamics simulations, suggest that the mutant E362Q is more susceptible to acid destabilization because of disruption of native intramolecular contacts. Fluorescence experiments show that removal of the charge in E362Q, and not in E349Q/D352N, is important for insertion of TH8-TH9. Both mutants adopt a final functional state upon further acidification. We conclude that these acidic residues are involved in the pH-dependent action of the T domain, and their replacements can be used for fine tuning the pH range of membrane interactions.
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