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Originally published In Press as doi:10.1074/jbc.M009674200 on February 14, 2001

J. Biol. Chem., Vol. 276, Issue 22, 19160-19165, June 1, 2001
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Zonula Occludens Toxin Structure-Function Analysis
IDENTIFICATION OF THE FRAGMENT BIOLOGICALLY ACTIVE ON TIGHT JUNCTIONS AND OF THE ZONULIN RECEPTOR BINDING DOMAIN*

Mariarosaria Di PierroDagger §, Ruliang LuDagger , Sergio Uzzau, Wenle WangDagger , Klara MargarettenDagger , Carlo Pazzani§, Francesco Maimone§||, and Alessio FasanoDagger **Dagger Dagger

From the Dagger  Division of Pediatric Gastroenterology and Nutrition and Gastrointestinal Pathophysiology Section, Center for Vaccine Development, ** Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201,  Dipartimento di Scienze Biomediche, Sezione di Microbiologia Sperimentale e Clinica, Università di Sassari, Sassari, Italy 07100, || Centro Interuniversitario di Ricerca sui Paesi in via di Sviluppo, Università "La Sapienza," Rome, Italy 07100, and § Dipartimento di Anatomia Patologica e di Genetica, Univerisità degli Studi, Bari, Italy 70126

Zonula occludens toxin (Zot) is an enterotoxin elaborated by Vibrio cholerae that increases intestinal permeability by interacting with a mammalian cell receptor with subsequent activation of intracellular signaling leading to the disassembly of the intercellular tight junctions. Zot localizes in the bacterial outer membrane of V. cholerae with subsequent cleavage and secretion of a carboxyl-terminal fragment in the host intestinal milieu. To identify the Zot domain(s) directly involved in the protein permeating effect, several zot gene deletion mutants were constructed and tested for their biological activity in the Ussing chamber assay and their ability to bind to the target receptor on intestinal epithelial cell cultures. The Zot biologically active domain was localized toward the carboxyl terminus of the protein and coincided with the predicted cleavage product generated by V. cholerae. This domain shared a putative receptor-binding motif with zonulin, the Zot mammalian analogue involved in tight junction modulation. Amino acid comparison between the Zot active fragment and zonulin, combined with site-directed mutagenesis experiments, confirmed the presence of an octapeptide receptor-binding domain toward the amino terminus of the processed Zot.

* Partially supported by National Institutes of Health Grant DK-48373 (A. F.) and the European Commission Contract IC18-CT 97-0231 (F. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Dagger To whom correspondence should be addressed: Division of Pediatric Gastroenterology and Nutrition, University of Maryland School of Medicine, 685 W. Baltimore St., HSF Bldg., Rm. 465, Baltimore, MD 21201. Tel.: 410-328-0812; Fax: 410-328-1072; E-mail: afasano@umaryland.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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