ArticleInfection and immunity2000
New method to generate enzymatically deficient Clostridium difficile toxin B as an antigen for immunization.
Article in Infection and immunity, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Low Density Lipoprotein Receptor-Related Protein-1 (LRP1) Is Involved in the Uptake ofFrontiers in cellular and infection microbiology · 2020Article
- Difference in Mono-O-Glucosylation of Ras Subtype GTPases Between Toxin A and Toxin B FromFrontiers in microbiology · 2018Article
- Expression and (Lacking) Internalization of the Cell Surface Receptors ofFrontiers in microbiology · 2018Article
- Role of p38Toxins · 2016Article
- Metal Ion Activation of Clostridium sordellii Lethal Toxin and Clostridium difficile Toxin B.Toxins · 2016Article
- Neutralization of Clostridium difficile Toxin B Mediated by Engineered Lactobacilli That Produce Single-Domain Antibodies.Infection and immunity · 2016Article
- Difference in the biological effects of Clostridium difficile toxin B in proliferating and non-proliferating cells.Naunyn-Schmiedeberg's archives of pharmacology · 2011Article
- Autoproteolytic cleavage mediates cytotoxicity of Clostridium difficile toxin A.Naunyn-Schmiedeberg's archives of pharmacology · 2011Article
- Clostridium difficile toxin A binds colonocyte Src causing dephosphorylation of focal adhesion kinase and paxillin.Experimental cell research · 2009Article
- Human monoclonal antibodies directed against toxins A and B prevent Clostridium difficile-induced mortality in hamsters.Infection and immunity · 2006Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The family of the large clostridial cytotoxins, encompassing Clostridium difficile toxins A and B as well as the lethal and hemorrhagic toxins from Clostridium sordellii, monoglucosylate the Rho GTPases by transferring a glucose moiety from the cosubstrate UDP-glucose. Here we present a new detoxification procedure to block the enzyme activity by treatment with the reactive UDP-2', 3'-dialdehyde to result in alkylation of toxin A and B. Alkylation is likely to occur in the catalytic domain, because the native cosubstrate UDP-glucose completely protected the toxins from inactivation and the alkylated toxin competes with the native toxin at the cell receptor. Alkylated toxins are good antigens resulting in antibodies recognizing only the C-terminally located receptor binding domain, whereas formaldehyde treatment resulted in antibodies recognizing both the receptor binding domain and the catalytic domain, indicating that the catalytic domain is concealed under native conditions. Antibodies against the native catalytic domain (amino acids 1 through 546) and those holotoxin antibodies recognizing the catalytic domain inhibited enzyme activity. However, only antibodies against the receptor binding domain protected intact cells from the cytotoxic activity of toxin B, whereas antibodies against the catalytic domain were protective only when inside the cell.
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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.