ArticleThe Journal of biological chemistry2015
Interaction of the Clostridium difficile Binary Toxin CDT and Its Host Cell Receptor, Lipolysis-stimulated Lipoprotein Receptor (LSR).
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 43 citations in OpenAlex.
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- Host factor Rab4b mediates internalization and intoxication of 3D4/21 cells by the active subunit of theFrontiers in microbiology · 2025Article
- Tight junction protein LSR is a host defense factor against SARS-CoV-2 infection in the small intestine.The EMBO journal · 2024Article
- Review
- Exploring the Toxin-Mediated Mechanisms inMicroorganisms · 2024Review
- An Updated View on the Cellular Uptake and Mode-of-Action of Clostridioides difficile Toxins.Advances in experimental medicine and biology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
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- The Effects of a High-Fat Diet on Inflammatory Bowel Disease.Biomolecules · 2023Review
- Structural Basis for Binding of Neutralizing Antibodies toJournal of bacteriology · 2023Article
- Review
- CDT ofToxins · 2023Article
- The Importance of Therapeutically Targeting the Binary Toxin fromInternational journal of molecular sciences · 2021Review
- CRISPA: A Non-viral, Transient Cas9 Delivery System Based on Reengineered Anthrax Toxin.Frontiers in pharmacology · 2021Article
- Leptin Downregulates Angulin-1 in Active Crohn's Disease via STAT3.International journal of molecular sciences · 2020Article
- Article
- Human intestinal enteroids as a model ofAmerican journal of physiology. Gastrointestinal and liver physiology · 2020Article
- The Inflammasome and Type-2 Immunity inClinics in colon and rectal surgery · 2020Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
CDT (Clostridium difficile transferase) is a binary, actin ADP-ribosylating toxin frequently associated with hypervirulent strains of the human enteric pathogen C. difficile, the most serious cause of antibiotic-associated diarrhea and pseudomembranous colitis. CDT leads to the collapse of the actin cytoskeleton and, eventually, to cell death. Low doses of CDT result in the formation of microtubule-based protrusions on the cell surface that increase the adherence and colonization of C. difficile. The lipolysis-stimulated lipoprotein receptor (LSR) is the host cell receptor for CDT, and our aim was to gain a deeper insight into the interplay between both proteins. We show that CDT interacts with the extracellular, Ig-like domain of LSR with an affinity in the nanomolar range. We identified LSR splice variants in the colon carcinoma cell line HCT116 and disrupted the LSR gene in these cells by applying the CRISPR-Cas9 technology. LSR truncations ectopically expressed in LSR knock-out cells indicated that intracellular parts of LSR are not essential for plasma membrane targeting of the receptor and cellular uptake of CDT. By generating a series of N- and C-terminal truncations of the binding component of CDT (CDTb), we found that amino acids 757-866 of CDTb are sufficient for binding to LSR. With a transposon-based, random mutagenesis approach, we identified potential LSR-interacting epitopes in CDTb. This study increases our understanding about the interaction between CDT and its receptor LSR, which is key to the development of anti-toxin strategies for preventing cell entry of the toxin.
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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.