Journal Article

Purification and preliminary characterization of the zonula occludens toxin receptor from human (CaCo2) and murine (IEC6) intestinal cell lines

Sergio Uzzau, Ruliang Lu, Wenle Wang, Cara Fiore and Alessio Fasano

in FEMS Microbiology Letters

Volume 194, issue 1, pages 1-5
Published in print January 2001 |
Published online January 2006 | e-ISSN: 1574-6968 | DOI:

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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 α-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.

Keywords: Vibrio cholerae; Zonula occludens toxin; Tight junction; Receptor

Journal Article.  2894 words.  Illustrated.

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