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Large clostridial cytotoxins | SpringerLink
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The large clostridial cytotoxins are a family of structurally and functionally related exotoxins from Clostridium difficile (toxins A and B), C. sordellii (lethal and hemorrhagic toxin) and C. novyi (α-toxin). The exotoxins are major pathogenicity factors which...
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Topics {✒️}
cation-dependent udp-glucose hydrolases actin-specific adp-ribosyltransferase produced c-terminal structure homologous month download article/chapter toxin b-positive strain rho/rho-kinase mediated signaling small gtp-binding proteins il-1beta-dependent pathway activates dual caspase-dependent phorbol ester-stimulated phospholipase binding-active human glycosphingolipid toxin b-positive strains x-ray crystal structure clostridium novyi alpha-toxin toxin a-negative strains low ph-induced formation sequence galα1-3galβ1-4glcnac n-terminal region involved de vries-smits amm increases intestinal permeability actin-specific adp-ribosyltransferase complete receptor-binding domain clostridium novyi α-toxin streptococcal ligand-binding proteins n-terminal catalytic domain high n-terminal homology inhibit small gtpases rho-gtpases functionally inactive actin-adp-ribosylating toxins single-chain protein toxins von eichel-streiber cytotoxin l-encoding gene toxin a-negative ras-related protein ral metal binding sites tight junction permeability large clostridial cytotoxins large clostridial cytotoxins rhizoid tip growth human carbohydrate antigens privacy choices/manage cookies carbohydrate binding region complete binary toxin ph-induced conformational mediates monocytes necrosis chaves-olarte β-galactoside-a-1 sordellii lethal toxin n-terminal region device instant download
Questions {❓}
- Boquet P, Lemichez E (2003) Bacterial virulence factors targeting Rho GTPases: parasitism or symbiosis?
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ScholarlyArticle:
headline:Large clostridial cytotoxins
pageEnd:47
pageStart:23
image:https://media.springernature.com/w153/springer-static/cover/book/978-3-540-27115-4.jpg
genre:
Biomedical and Life Sciences
Biomedical and Life Sciences (R0)
isPartOf:
name:Reviews of Physiology, Biochemistry and Pharmacology
isbn:
978-3-540-27115-4
978-3-540-23131-8
type:Book
publisher:
name:Springer Berlin Heidelberg
logo:
url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
type:ImageObject
type:Organization
author:
name:I. Just
affiliation:
name:Medizinische Hochschlule Hannover
address:
name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
type:PostalAddress
type:Organization
email:[email protected]
type:Person
name:R. Gerhard
affiliation:
name:Medizinische Hochschlule Hannover
address:
name:Institut für Toxikologie, Medizinische Hochschlule Hannover, Hannover, Germany
type:PostalAddress
type:Organization
type:Person
keywords:Clostridium Difficile, Pseudomembranous Colitis, Lethal Toxin, Clostridium Difficile Toxin, Guanine Nucleotide Dissociation Inhibitor
description:The large clostridial cytotoxins are a family of structurally and functionally related exotoxins from Clostridium difficile (toxins A and B), C. sordellii (lethal and hemorrhagic toxin) and C. novyi (α-toxin). The exotoxins are major pathogenicity factors which in addition to their in vivo effects are cytotoxic to cultured cell lines causing reorganization of the cytoskeleton accompanied by morphological changes. The exotoxins are single-chain protein toxins, which are constructed of three domains: receptor-binding, translocation and catalytic domain. These domains reflect the self-mediated cell entry via receptor-mediated endocytosis, translocation into the cytoplasm, and execution of their cytotoxic activity by an inherent enzyme activity. Enzymatically, the toxins catalyze the transfer of a glucosyl moiety from UDP-glucose to the intracellular target proteins which are the Rho and Ras GTPases. The covalent attachment of the glucose moiety to a conserved threonine within the effector region of the GTPases renders the Rho-GTPases functionally inactive. Whereas the molecular mode of cytotoxic effects is fully understood, the mechanisms leading to inflammatory processes in the context of disease (e.g., antibiotic-associated pseudomembranous colitis caused by Clostridium difficile) are less clear.
datePublished:2004
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