ArticleProceedings of the National Academy of Sciences of the United States of America2004
Identification of a domain within the multifunctional Vibrio cholerae RTX toxin that covalently cross-links actin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 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
73 citing papers in PubMed, 140 citations in OpenAlex.
- Please inhibit responsibly: Natural and synthetic actin toxins as useful tools in cell biology.Molecular biology of the cell · 2025Review
- Cysteine proteases and how YabG fits into clan CD of the MEROPS database.Journal of bacteriology · 2025Review
- Article
- Biantennary N-glycans As Receptors for MARTX Toxins inbioRxiv : the preprint server for biology · 2024Article
- T6SS in plant pathogens: unique mechanisms in complex hosts.Infection and immunity · 2024Review
- Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024Article
- Acquisition of Type I methyltransferase via horizontal gene transfer increases the drug resistance ofMicrobial genomics · 2023Article
- Actin Cross-Linking Effector Domain of theInfection and immunity · 2022Article
- A deep-sea bacterium related to coastal marine pathogens.Environmental microbiology · 2021Article
- Intein-mediated cytoplasmic reconstitution of a split toxin enables selective cell ablation in mixed populations and tumor xenografts.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Phenotypic and Genotypic Properties ofMicroorganisms · 2020Article
- TheScience signaling · 2020Article
- TheFrontiers in microbiology · 2020Article
- Makes caterpillars floppy-like effector-containing MARTX toxins require host ADP-ribosylation factor (ARF) proteins for systemic pathogenicity.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Environmental and Clinical Strains ofFrontiers in microbiology · 2019Article
- The Modes of Action of MARTX Toxin Effector Domains.Toxins · 2018Review
- The Xylella fastidosa RTX operons: evidence for the evolution of protein mosaics through novel genetic exchanges.BMC genomics · 2018Article
- Accessory Toxins ofFrontiers in microbiology · 2018Review
- Vibrio vulnificus MARTX cytotoxin causes inactivation of phagocytosis-related signaling molecules in macrophages.Journal of biomedical science · 2017Article
- DeActs: genetically encoded tools for perturbing the actin cytoskeleton in single cells.Nature methods · 2017Article
13 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The Gram-negative pathogen Vibrio cholerae causes diarrheal disease through the export of enterotoxins. The V. cholerae RTX toxin was previously identified and characterized by its ability to round human laryngeal epithelial (HEp-2) cells. Further investigation determined that cell rounding is caused by the depolymerization of actin stress fibers, through the unique mechanism of covalent actin cross-linking. In this study, we identify a domain within the full-length RTX toxin that is capable of mediating the cross-linking reaction when transiently expressed within eukaryotic cells. A structure/function analysis of the actin cross-linking domain (ACD) reveals that a 412-aa, or a 47.8-kDa, region is essential for cross-linking activity. When this domain is deleted from the full-length toxin gene, actin cross-linking, but not cell rounding, is eliminated, indicating that this toxin carries multiple dissociable activities. The ACD shares 59% amino acid identity with a hypothetical protein from V. cholerae, VC1416, and transient expression of the C-terminal domain of VC1416 also results in actin cross-linking in eukaryotic cells. The presence of this second ACD linked to an Rhs-like element suggests that V. cholerae acquired the domain by horizontal gene transfer and the ACD was inserted into the RTX toxin by gene duplication through the evolution of V. cholerae.
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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.