ArticleProceedings of the National Academy of Sciences of the United States of America2010
Identification of a conserved membrane localization domain within numerous large bacterial protein toxins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed.
- Mouse monoclonal antibodies againstInfection and immunity · 2025Article
- Dissemination of pathogenic bacteria is reinforced by a MARTX toxin effector duet.Nature communications · 2024Article
- Tyrosine-modifying glycosylation by Yersinia effectors.The Journal of biological chemistry · 2024Article
- Site-directed spin label EPR studies of the structure and membrane interactions of the bacterial phospholipase ExoU.Applied magnetic resonance · 2024Article
- Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024Article
- An Updated View on the Cellular Uptake and Mode-of-Action of Clostridioides difficile Toxins.Advances in experimental medicine and biology · 2024Article
- Article
- Clostridioides difficile Toxin A Remodels Membranes and Mediates DNA Entry Into Cells to Activate Toll-Like Receptor 9 Signaling.Gastroenterology · 2020Article
- TheFrontiers in microbiology · 2020Article
- Review
- Structure of the full-length Clostridium difficile toxin B.Nature structural & molecular biology · 2019Article
- Conformational Changes and Membrane Interaction of the Bacterial Phospholipase, ExoU: Characterization by Site-Directed Spin Labeling.Cell biochemistry and biophysics · 2019Article
- RRSP and RID Effector Domains Dominate the Virulence Impact of Vibrio vulnificus MARTX Toxin.The Journal of infectious diseases · 2019Article
- The Modes of Action of MARTX Toxin Effector Domains.Toxins · 2018Review
- Structural basis of inactivation of Ras and Rap1 small GTPases by Ras/Rap1-specific endopeptidase from the sepsis-causing pathogenThe Journal of biological chemistry · 2018Article
- The bacterial Ras/Rap1 site-specific endopeptidase RRSP cleaves Ras through an atypical mechanism to disrupt Ras-ERK signaling.Science signaling · 2018Article
- Coordinated delivery and function of bacterial MARTX toxin effectors.Molecular microbiology · 2018Review
- The role of toxins in Clostridium difficile infection.FEMS microbiology reviews · 2017Review
- The membrane localization domains of two distinct bacterial toxins form a 4-helix-bundle in solution.Protein science : a publication of the Protein Society · 2017Article
- Cooperative Substrate-Cofactor Interactions and Membrane Localization of the Bacterial Phospholipase AThe Journal of biological chemistry · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
Vibrio cholerae is the causative agent of the diarrheal disease cholera. Many virulence factors contribute to intestinal colonization and disease including the Multifunctional Autoprocessing RTX toxin (MARTX(Vc)). The Rho-inactivation domain (RID) of MARTX(Vc) is responsible for inactivating the Rho-family of small GTPases, which leads to depolymerization of the actin cytoskeleton. Based on a deletion analysis of RID to determine the minimal functional domain, we have identified a subdomain at the N terminus of RID that is homologous to the membrane targeting C1 domain of Pasteurella multocida toxin. A GFP fusion to this subdomain from RID colocalized with a plasma membrane marker when transiently expressed within HeLa cells and can be found in the membrane fraction following subcellular fractionation. This C1-like subdomain is present in multiple families of bacterial toxins, including all of the clostridial glucosyltransferase toxins and various MARTX toxins. GFP-fusions to these homologous domains are also membrane associated, indicating that this is a conserved membrane localization domain (MLD). We have identified three residues (Y23, S68, R70) as necessary for proper localization of one but not all MLDs. In addition, we found that substitution of the RID MLD with the MLDs from two different effector domains from the Vibrio vulnificus MARTX toxin restored RID activity, indicating that there is functional overlap between these MLDs. This study describes the initial recognition of a family of conserved plasma membrane-targeting domains found in multiple large bacterial toxins.
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