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J. Biol. Chem., Vol. 278, Issue 21, 19159-19163, May 23, 2003

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A Receptor-binding Region in Escherichia coli -Haemolysin^*

Aitziber L. Cortajarena , Félix M. Goñi and Helena Ostolaza 

From the Unidad de Biofísica (Consejo Superior de Investigaciones Científicas-Universidad del País Vasco/Euskal Herriko Unibertsitatea) and Departamento de Bioquímica, Universidad del País Vasco, Aptdo. 644, 48080 Bilbao, Spain

Escherichia coli -hemolysin (HlyA) is a 107-kDa protein toxin with a wide range of mammalian target cells. Previous work has shown that glycophorin is a specific receptor for HlyA in red blood cells (Cortajarena, A. L., Goñi, F. M., and Ostolaza, H. (2001) J. Biol. Chem. 276, 12513–12519). The present study was aimed at identifying the glycophorin-binding region in the toxin. Data in the literature pointed to a short amino acid sequence near the C terminus as a putative receptor-binding domain. Previous sequence analyses of several homologous toxins that belong, like HlyA, to the so-called RTX toxin family revealed a conserved region that corresponded to residues 914–936 of HlyA. We therefore prepared a deletion mutant lacking these residues (HlyA914–936) and found that its hemolytic activity was decreased by 10,000-fold with respect to the wild type. This deletion mutant was virtually unable to bind human and horse red blood cells or to bind pure glycophorin in an affinity column. The peptide Trp⁹¹⁴–Arg⁹³⁶ had no lytic activity of its own, but it could bind glycophorin reconstituted in lipid vesicles. Moreover, the peptide Trp⁹¹⁴–Arg⁹³⁶ protected red blood cells from hemolysis induced by wild type HlyA. It was concluded that amino acid residues 914–936 constitute a major receptor-binding region in -hemolysin.

Received for publication, August 21, 2002 , and in revised form, February 10, 2003.

To whom correspondence should be addressed. Tel.: 34-94-601-26-25; Fax: 34-94-601-33-60; E-mail: gbzoseth{at}lg.ehu.es.

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