Document Detail


Cellular interactions of the cytolethal distending toxins from Escherichia coli and Haemophilus ducreyi.
MedLine Citation:
PMID:  23306199     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The cytolethal distending toxins (CDTs) compose a subclass of intracellularly acting genotoxins produced by many Gram-negative pathogenic bacteria that disrupt the normal progression of the eukaryotic cell cycle. Here, the intoxication mechanisms of CDTs from Escherichia coli (Ec-CDT) and Haemophilus ducreyi (Hd-CDT), which share limited amino acid sequence homology, were directly compared. Ec-CDT and Hd-CDT shared comparable in vitro DNase activities of the CdtB subunits, saturable cell surface binding with comparable affinities, and the requirement for an intact Golgi complex to induce cell cycle arrest. In contrast, disruption of endosome acidification blocked Hd-CDT-mediated cell cycle arrest and toxin transport to the endoplasmic reticulum and nucleus, while having no effects on Ec-CDT. Phosphorylation of the histone protein H2AX, as well as nuclear localization, was inhibited for Hd-CdtB, but not Ec-CdtB, in cells expressing dominant negative Rab7 (T22N), suggesting that Hd-CDT, but not Ec-CDT, is trafficked through late endosomal vesicles. In support of this idea, significantly more Hd-CdtB than Ec-CdtB co-localized with Rab9, which is enriched in late endosomal compartments. Competitive binding studies suggested that Ec-CDT and Hd-CDT bind to discrete cell surface determinants. These results suggest that Ec-CDT and Hd-CDT are transported within cells by distinct pathways, possibly mediated by their interaction with different receptors at the cell surface.
Authors:
Amandeep Gargi; Batcha Tamilselvam; Brendan Powers; Michael G Prouty; Tommie Lincecum; Aria Eshraghi; Francisco J Maldonado-Arocho; Brenda A Wilson; Kenneth A Bradley; Steven R Blanke
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't     Date:  2013-01-10
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Mar 
Date Detail:
Created Date:  2013-03-18     Completed Date:  2013-05-14     Revised Date:  2014-03-26    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  7492-505     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Bacterial Toxins / metabolism*
Biotinylation
CHO Cells
Caco-2 Cells
Cell Cycle
Cell Nucleus / metabolism
Cloning, Molecular
Cricetinae
Deoxyribonucleases / metabolism
Escherichia coli / metabolism*
Gene Expression Regulation, Bacterial
Haemophilus ducreyi / metabolism*
HeLa Cells
Histones / chemistry,  metabolism
Humans
Protein Transport
Recombinant Proteins / chemistry
Grant Support
ID/Acronym/Agency:
AI0059095/AI/NIAID NIH HHS; AI038396/AI/NIAID NIH HHS; F31DE022485/DE/NIDCR NIH HHS; R01 GM098756/GM/NIGMS NIH HHS; R01GM098756/GM/NIGMS NIH HHS; T32DE007296/DE/NIDCR NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Toxins; 0/H2AFX protein, human; 0/Histones; 0/Recombinant Proteins; 0/cytolethal distending toxin; EC 3.1.-/Deoxyribonucleases
Comments/Corrections

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