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

The glucosyltransferase activity of C. difficile Toxin B is required for disease pathogenesis

22 Sept 2020

Abstract excerpt

Enzymatic inactivation of Rho-family GTPases by the glucosyltransferase domain of Clostridioides difficile Toxin B (TcdB) gives rise to various pathogenic effects in cells that are classically thought to be responsible for the disease symptoms associated with C. difficile infection (CDI). Recent in vitro studies have shown that TcdB can, under certain circumstances, induce cellular toxicities that are independent...

Read the complete abstract on PubMed

Topics

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

Share to Clostridium difficile and Clostridium perfringens research
Share to Pharmacological Effects of Natural Compounds
Share to Toxin Mechanisms and Immunotoxins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 32960931
DOI: 10.1371/journal.ppat.1008852

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 23 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The glucosyltransferase activity of C. difficile Toxin B is required for disease pathogenesisPMID 32960931Read ↗

Glucosyltransferase-dependent and independent effects of <i>Clostridioides difficile</i> toxins during infectionSemantic proximity Read ↗

Toxin B is essential for virulence of Clostridium difficile.Semantic proximity Read ↗

Identification of an Essential Region for Translocation of Clostridium difficile Toxin B.Semantic proximity Read ↗

Isofagomine inhibits multiple TcdB variants and protects mice from <i>Clostridioides difficile</i> induced mortalitySemantic proximity Read ↗

Clostridium difficile Toxins TcdA and TcdB Cause Colonic Tissue Damage by Distinct MechanismsSemantic proximity Read ↗

<i>Clostridioides difficile</i> toxin A and toxin B inhibit toxin-specific adaptive immune responses through glucosyltransferase-dependent activitySemantic proximity Read ↗

Analysis of TcdB Proteins within the Hypervirulent Clade 2 Reveals an Impact of RhoA Glucosylation on Clostridium difficile Proinflammatory Activities.Semantic proximity Read ↗

Application of mutated Clostridium difficile toxin A for determination of glucosyltransferase-dependent effects.Semantic proximity Read ↗

Cyclic diguanylate differentially regulates the expression of virulence factors and pathogenesis-related phenotypes in Clostridioides difficile.Semantic proximity Read ↗

Purified CDT toxins and a clean deletion within the CDT locus provide novel insights into the contribution of binary toxin in cellular inflammation and Clostridioides difficile infectionSemantic proximity Read ↗

Defective mutations within the translocation domain of Clostridium difficile toxin B impair disease pathogenesis.Semantic proximity Read ↗

Pathogenesis of Clostridium difficile infectionSemantic proximity Read ↗

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