Source:http://linkedlifedata.com/resource/pubmed/id/18060735
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2008-3-24
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| pubmed:abstractText |
Clostridium perfringens iota-toxin is a binary toxin composed of an enzymatic component (Ia) and a binding component (Ib). We investigated the role of the conserved Ca(2+)-binding motif of Ib in the cytotoxicity of iota-toxin. The cytotoxicity of iota-toxin increased with an increase in the concentration of extracellular Ca(2+). A surface plasmon resonance analysis showed that the binding of Ia to the oligomer of Ib is dependent on the concentration of Ca(2+). However, the addition of Ca(2+) had no effect on the binding of (125)I-labeled Ib to the cells. We replaced Asp-8, -10, and -12 in the Ca(2+)-binding motif of Ib with alanine. D8A, D10A, and D12A bound to the cell and formed an oligomer at about half of the wild-type Ib. The cytotoxicity of Ib variants in the presence of Ia was about 500-fold less than that of wild-type Ib. Immunofluorescence study showed that these variants were internalized in the early endosomes like wild-type Ib. However, wild-type Ib-induced internalization of Ia in the cells, but these variants did not. The result indicates that the conserved Ca(2+)-binding motif in the N-terminal region of Ib plays a role in the interaction of Ib with Ia in the presence of Ca(2+).
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical | |
| pubmed:status |
MEDLINE
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| pubmed:month |
Apr
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| pubmed:issn |
0882-4010
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
44
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
265-70
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| pubmed:meshHeading |
pubmed-meshheading:18060735-ADP Ribose Transferases,
pubmed-meshheading:18060735-Amino Acid Motifs,
pubmed-meshheading:18060735-Amino Acid Sequence,
pubmed-meshheading:18060735-Amino Acid Substitution,
pubmed-meshheading:18060735-Animals,
pubmed-meshheading:18060735-Bacterial Toxins,
pubmed-meshheading:18060735-Binding Sites,
pubmed-meshheading:18060735-Calcium,
pubmed-meshheading:18060735-Cercopithecus aethiops,
pubmed-meshheading:18060735-Clostridium perfringens,
pubmed-meshheading:18060735-Conserved Sequence,
pubmed-meshheading:18060735-Dogs,
pubmed-meshheading:18060735-Molecular Sequence Data,
pubmed-meshheading:18060735-Mutagenesis, Site-Directed,
pubmed-meshheading:18060735-Protein Binding,
pubmed-meshheading:18060735-Sequence Alignment,
pubmed-meshheading:18060735-Surface Plasmon Resonance,
pubmed-meshheading:18060735-Vero Cells
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| pubmed:year |
2008
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| pubmed:articleTitle |
Role of Ca2+-binding motif in cytotoxicity induced by Clostridium perfringens iota-toxin.
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| pubmed:affiliation |
Department of Microbiology, Faculty of Pharmaceutical Sciences, Tokushima Bunri University, Yamashiro, Tokushima 7708514, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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