Abstract
In the present study, we report the preliminary characterization of the epithelial cell receptor for Vibrio cholerae zonula occludens toxin (Zot). Zot receptor was purified by ligand-affinity chromatography. Analysis of affinity-purified preparations by polyacrylamide gel electrophoresis revealed a protein of ca. 66 kDa. Partial N-terminal sequence obtained from purified murine and human Zot receptor revealed homology between the two proteins and with human alpha-1-chimaerin. Zot protein domain(s) involved in receptor binding were also analyzed by constructing several in frame deletion derivatives of a recombinant fusion Zot protein tagged with maltose binding protein. Our results suggest that Zot binding to its cellular membrane receptor requires a sequence that spans between amino acids 118 and 299.
MeSH terms
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Amino Acid Sequence
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Animals
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Caco-2 Cells
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Carrier Proteins / genetics
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Carrier Proteins / metabolism
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Cattle
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Cell Line
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Chimerin 1 / genetics
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Cholera Toxin / metabolism*
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Dogs
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Endotoxins
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Epithelial Cells / metabolism
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Gene Deletion
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Humans
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Immunoblotting
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Intestinal Mucosa / cytology*
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Intestinal Mucosa / metabolism
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Maltose-Binding Proteins
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Molecular Sequence Data
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Rats
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Receptors, Cell Surface / genetics
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Receptors, Cell Surface / isolation & purification*
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Receptors, Cell Surface / metabolism
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Recombinant Fusion Proteins / genetics
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Recombinant Fusion Proteins / metabolism
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Vibrio cholerae / metabolism
Substances
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Carrier Proteins
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Chimerin 1
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Endotoxins
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Maltose-Binding Proteins
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Receptors, Cell Surface
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Recombinant Fusion Proteins
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zonula occludens toxin receptor
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zonula occludens toxin, Vibrio cholerae
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Cholera Toxin