ArticleProceedings of the National Academy of Sciences of the United States of America2000
Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- Cellular Activity ofToxins · 2021Article
- Cross-Kingdom Activation ofJournal of bacteriology · 2020Review
- Glycolipid Crosslinking Is Required for Cholera Toxin to Partition Into and Stabilize Ordered Domains.Biophysical journal · 2016Article
- The chromosomal nature of LT-II enterotoxins solved: a lambdoid prophage encodes both LT-II and one of two novel pertussis-toxin-like toxin family members in type II enterotoxigenic Escherichia coli.Pathogens and disease · 2016Article
- Comparison of Xenorhabdus bovienii bacterial strain genomes reveals diversity in symbiotic functions.BMC genomics · 2015Article
- Article
- ADP-ribosylation factor 6 acts as an allosteric activator for the folded but not disordered cholera toxin A1 polypeptide.Molecular microbiology · 2014Article
- Article
- Identification of host cell factors required for intoxication through use of modified cholera toxin.The Journal of cell biology · 2011Article
- Structural and functional studies on the interaction of GspC and GspD in the type II secretion system.PLoS pathogens · 2011Article
- Adjuvant activity of the catalytic A1 domain of cholera toxin for retroviral antigens delivered by GeneGun.Clinical and vaccine immunology : CVI · 2011Article
- Regulation and activity of a zinc uptake regulator, Zur, in Corynebacterium diphtheriae.Journal of bacteriology · 2009Article
- Order-disorder-order transitions mediate the activation of cholera toxin.Journal of molecular biology · 2008Article
- The monofunctional glycosyltransferase of Escherichia coli localizes to the cell division site and interacts with penicillin-binding protein 3, FtsW, and FtsN.Journal of bacteriology · 2008Article
- Conformational instability of the cholera toxin A1 polypeptide.Journal of molecular biology · 2007Article
- Sensitization of spinal cord nociceptive neurons with a conjugate of substance P and cholera toxin.BMC neuroscience · 2007Article
- Bacteriophage-based vectors for site-specific insertion of DNA in the chromosome of Corynebacteria.Gene · 2007Article
- Pirin regulates pyruvate catabolism by interacting with the pyruvate dehydrogenase E1 subunit and modulating pyruvate dehydrogenase activity.Journal of bacteriology · 2007Article
- The cholera toxin A1(3) subdomain is essential for interaction with ADP-ribosylation factor 6 and full toxic activity but is not required for translocation from the endoplasmic reticulum to the cytosol.Infection and immunity · 2006Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The latent ADP-ribosyltransferase activity of cholera toxin (CT) that is activated after proteolytic nicking and reduction is associated with the CT A1 subunit (CTA1) polypeptide. This activity is stimulated in vitro by interaction with eukaryotic proteins termed ADP-ribosylation factors (ARFs). We analyzed this interaction in a modified bacterial two-hybrid system in which the T18 and T25 fragments of the catalytic domain of Bordetella pertussis adenylate cyclase were fused to CTA1 and human ARF6 polypeptides, respectively. Direct interaction between the CTA1 and ARF6 domains in these hybrid proteins reconstituted the adenylate cyclase activity and permitted cAMP-dependent signal transduction in an Escherichia coli reporter system. We constructed improved vectors and reporter strains for this system, and we isolated variants of CTA1 that showed greatly decreased ability to interact with ARF6. Amino acid substitutions in these CTA1 variants were widely separated in the primary sequence but were contiguous in the three-dimensional structure of CT. These residues, which begin to define the ARF interaction motif of CTA1, are partially buried in the crystal structure of CT holotoxin, suggesting that a change in the conformation of CTA1 enables it to bind to ARF. Variant CTA polypeptides containing these substitutions assembled into holotoxin as well as wild-type CTA, but the variant holotoxins showed greatly reduced enterotoxicity. These findings suggest functional interaction between CTA1 and ARF is required for maximal toxicity of CT in vivo.
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