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J. Biol. Chem., Vol. 279, Issue 39, 41028-41037, September 24, 2004

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Crystal Structure of Leucotoxin S Component

NEW INSIGHT INTO THE STAPHYLOCOCCAL -BARREL PORE-FORMING TOXINS^*

Valérie Guillet, Pierre Roblin, Sandra Werner, Manuela Coraiola¶, Gianfranco Menestrina¶, Henri Monteil, Gilles Prévost||, and Lionel Mourey**

From the Groupe de Biophysique Structurale, Département Mécanismes Moléculaires des Infections Mycobactériennes, CNRS-IPBS, 205 route de Narbonne, 31077 Toulouse Cedex, France, the Laboratoire de Physiopathologie et d'Antibiologie des Infections Bactériennes Emergentes et Nosocomiales-EA 3432, Institut de Bactériologie de la Faculté de Médecine, Hôpitaux Universitaires de Strasbourg, 3 rue Koeberlé, 67000 Strasbourg, France, and the ^¶CNR-ITC Istituto di Biofisica Sezione di Trento, Via Sommarive 18 I-38050 Povo, Italy

Staphylococcal leucocidins and -hemolysins (leucotoxins) are bi-component toxins that form lytic transmembrane pores. Their cytotoxic activities require the synergistic association of a class S component and a class F component, produced as water-soluble monomers that form hetero-oligomeric membrane-associated complexes. Strains that produce the Panton-Valentine leucocidin are clinically associated with cutaneous lesions and community-acquired pneumonia. In a previous study, we determined the crystal structure of the F monomer from the Panton-Valentine leucocidin. To derive information on the second component of the leucotoxins, the x-ray structure of the S protein from the Panton-Valentine leucocidin was solved to 2.0 Å resolution using a tetragonal crystal form that contains eight molecules in the asymmetric unit. The structure demonstrates the different conformation of the domain involved in membrane contacts and illustrates sequence and tertiary structure variabilities of the pore-forming leucotoxins. Mutagenesis studies at a key surface residue (Thr-28) further support the important role played by these microheterogeneities for the assembly of the bipartite leucotoxins.

Received for publication, June 21, 2004 , and in revised form, July 14, 2004.

The atomic coordinates and structure factors (code 1t5r) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

This paper is dedicated to the memory of Dr. Gianfranco Menestrina who died accidentally on July 8, 2004 concurrently with the acceptation of this article. He was a true friend and a brilliant and fair mind who inspired respect from the scientific community. We are deeply affected by this fatality.

^* This work was supported by Grant EA-3432 from the Direction de la Recherche et des Etudes Doctorales of the UPRES EA-3432 at the Institut de Bactériologie de la Faculté de Médecine de Strasbourg (to G. P.) and funds from the Consiglio Nazionale delle Ricerche and Provincia Autonoma di Trento Fondo Progetti Project Stawars (to G. M. and G. P.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^|| To whom correspondence may be addressed. Tel.: 33-390-243-757; Fax: 33-388-251-113; E-mail: gilles.prevost{at}medecine.u-strasbg.fr.

^** To whom correspondence may be addressed. Tel.: 33-561-175-436; Fax: 33-561-175-994; E-mail: lionel.mourey{at}ipbs.fr.

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