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Journal of Bacteriology, April 1999, p. 2455-2458, Vol. 181, No. 8
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Distinct Affinity of Binding Sites for S-Layer Homologous Domains in Clostridium thermocellum and Bacillus anthracis Cell Envelopes

Sylvie Chauvaux,^* Markus Matuschek, and Pierre Beguin

Unité de Physiologie Cellulaire, Département des Biotechnologies, Institut Pasteur, 75724 Paris Cedex 15, France

Received 28 September 1998/Accepted 1 February 1999

Binding parameters were determined for the SLH (S-layer homologous) domains from the Clostridium thermocellum outer layer protein OlpB, from the C. thermocellum S-layer protein SlpA, and from the Bacillus anthracis S-layer proteins EA1 and Sap, using cell walls from C. thermocellum and B. anthracis. Each SLH domain bound to C. thermocellum and B. anthracis cell walls with a different K_D, ranging between 7.1 × 10⁷ and 1.8 × 10⁸ M. Cell wall binding sites for SLH domains displayed different binding specificities in C. thermocellum and B. anthracis. SLH-binding sites were not detected in cell walls of Bacillus subtilis. Cell walls of C. thermocellum lost their affinity for SLH domains after treatment with 48% hydrofluoric acid but not after treatment with formamide or dilute acid. A soluble component, extracted from C. thermocellum cells by sodium dodecyl sulfate treatment, bound the SLH domains from C. thermocellum but not those from B. anthracis proteins. A corresponding component was not found in B. anthracis.

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^* Corresponding author. Mailing address: Unité de Physiologie Cellulaire, Département des Biotechnologies, Institut Pasteur, 25, rue du Dr. Roux, 75724 Paris Cedex 15, France. Phone: 33 1 40 61 37 04. Fax: 33 1 45 68 87 90. E-mail: chauvaux{at}pasteur.fr.

Present address: ZHF/D-A30, BASF Aktiengesellschaft, 67056 Ludwigshafen, Germany.

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Journal of Bacteriology, April 1999, p. 2455-2458, Vol. 181, No. 8
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

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