Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural basis for Clostridium perfringens enterotoxin targeting of claudins at tight junctions in mammalian gut

5 Apr 2021

Abstract excerpt

Significance Clostridium perfringens causes gas gangrene and is a leading cause of bacterial food poisoning, with 1,000,000 US cases annually. Food-poisoning strains produce an enterotoxin (CpE) that breaks apart tight junctions, protein assemblies composed of claudins that fortify the gut barrier. CpE selectively targets claudins via its C-terminal domain (cCpE) to disrupt the gut barrier—the basis for targeting...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Barrier Structure and Function Studies
Share to Clostridium difficile and Clostridium perfringens research
Share to Gut microbiota and health

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 33876770
DOI: 10.1073/pnas.2024651118

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis for Clostridium perfringens enterotoxin targeting of claudins at tight junctions in mammalian gutPMID 33876770Read ↗

Development, structure, and mechanism of synthetic antibodies that target claudin and Clostridium perfringens enterotoxin complexesSemantic proximity Read ↗

Structural basis for disruption of claudin assembly in tight junctions by an enterotoxin.Semantic proximity Read ↗

Human Claudin-8 and -14 Are Receptors Capable of Conveying the Cytotoxic Effects of Clostridium perfringens EnterotoxinSemantic proximity Read ↗

C. perfringens enterotoxin-claudin pore complex: Models for structure, mechanism of pore assembly and cation permeabilitySemantic proximity Read ↗

Development, Structure, and Mechanism of Synthetic Antibodies that Target Claudin and <i>Clostridium perfringens</i> Enterotoxin ComplexesSemantic proximity Read ↗

Mutated C-terminal fragments of Clostridium perfringens enterotoxin have increased affinity to claudin-4 and reversibly modulate tight junctions in vitro.Semantic proximity Read ↗

Identification of a Claudin-4 Residue Important for Mediating the Host Cell Binding and Action of <i>Clostridium perfringens</i> EnterotoxinSemantic proximity Read ↗

Structure of a C. perfringens enterotoxin mutant in complex with a modified Claudin-2 extracellular loop 2.Semantic proximity Read ↗

Directed structural modification of Clostridium perfringens enterotoxin to enhance binding to claudin-5.Semantic proximity Read ↗

Clostridium perfringens Enterotoxin: Action, Genetics, and Translational ApplicationsSemantic proximity Read ↗

Tissue distribution and safety evaluation of a claudin-targeting molecule, the C-terminal fragment of Clostridium perfringens enterotoxin.Semantic proximity Read ↗

The enteric toxins of Clostridium perfringens.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.