ReviewToxins2014
Disorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretion.
Review in Toxins, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed, 41 citations in OpenAlex.
- Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Ion-selective conformational stabilization of a disordered repeats-in-toxin protein domain.Biophysical journal · 2025Article
- RfeA from Streptococcus suis serotype 2 triggers NLRP3/Caspase-1-dependent pyroptosis leading to blood-brain barrier disruption.Veterinary research · 2025Article
- Co-cultivation of Lactobacillus acidophilus and Bacillus subtilis mediates the gut-muscle axis affecting pork quality and flavor.Journal of animal science and biotechnology · 2025Article
- CyaA translocation across eukaryotic cell membranes.Frontiers in molecular biosciences · 2024Article
- A High-Affinity Calmodulin-Binding Site in the CyaA Toxin Translocation Domain is Essential for Invasion of Eukaryotic Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Nucleobindin-2 consists of two structural components: The ZnComputational and structural biotechnology journal · 2021Article
- Article
- Review
- Topologically-guided continuous protein crystallization controls bacterial surface layer self-assembly.Nature communications · 2019Article
- Calcium-Dependent RTX Domains in the Development of Protein Hydrogels.Gels (Basel, Switzerland) · 2019Review
- The Adenylate Cyclase (CyaA) Toxin fromToxins · 2019Article
- Control of rotation of the FJournal of bioenergetics and biomembranes · 2018Review
- Calcium-Binding Proteins with Disordered Structure and Their Role in Secretion, Storage, and Cellular Signaling.Biomolecules · 2018Review
- Membrane localization of the Repeats-in-Toxin (RTX) Leukotoxin (LtxA) produced by Aggregatibacter actinomycetemcomitans.PloS one · 2018Article
- Membrane-Active Properties of an Amphitropic Peptide from the CyaA Toxin Translocation Region.Toxins · 2017Article
- Review
- Review
- Molecular Modeling of the Catalytic Domain of CyaA Deepened the Knowledge of Its Functional Dynamics.Toxins · 2017Review
- Environmental Calcium Controls Alternate Physical States of the Caulobacter Surface Layer.Biophysical journal · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The past decade has seen a fundamental reappraisal of the protein structure-to-function paradigm because it became evident that a significant fraction of polypeptides are lacking ordered structures under physiological conditions. Ligand-induced disorder-to-order transition plays a key role in the biological functions of many proteins that contain intrinsically disordered regions. This trait is exhibited by RTX (Repeat in ToXin) motifs found in more than 250 virulence factors secreted by Gram-negative pathogenic bacteria. We have investigated several RTX-containing polypeptides of different lengths, all derived from the Bordetella pertussis adenylate cyclase toxin, CyaA. Using a combination of experimental approaches, we showed that the RTX proteins exhibit the hallmarks of intrinsically disordered proteins in the absence of calcium. This intrinsic disorder mainly results from internal electrostatic repulsions between negatively charged residues of the RTX motifs. Calcium binding triggers a strong reduction of the mean net charge, dehydration and compaction, folding and stabilization of secondary and tertiary structures of the RTX proteins. We propose that the intrinsically disordered character of the RTX proteins may facilitate the uptake and secretion of virulence factors through the bacterial secretion machinery. These results support the hypothesis that the folding reaction is achieved upon protein secretion and, in the case of proteins containing RTX motifs, could be finely regulated by the calcium gradient across bacterial cell wall.
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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.