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J. Biol. Chem., Vol. 279, Issue 50, 51760-51768, December 10, 2004

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Identification and Biochemical Characterization of Two Novel Collagen Binding MSCRAMMs of Bacillus anthracis^*

Yi Xu, Xiaowen Liang, Yahua Chen, Theresa M. Koehler¶, and Magnus Höök

From the The Center for Extracellular Matrix Biology, Texas A&M University System Health Science Center, Albert B. Alkek Institute of Biosciences and Technology, Houston, Texas 77030 and ^¶Department of Microbiology and Molecular Genetics, University of Texas Health Science Center, Houston, Texas 77030

Cell wall-anchored proteins play critical roles in the pathogenesis of infections caused by Gram-positive bacteria. Through the analysis of the genome of Bacillus anthracis Ames strain, we identified two novel putative cell wall-anchored proteins, BA0871 and BA5258, which have sequence homology to CNA, a cell wall-anchored collagen adhesin of Staphylococcus aureus. The two proteins have similar domain organization to that of CNA, with typical signal peptide sequences, a non-repetitive A region followed by repeats, and a characteristic cell wall-anchoring region. They are expressed on the surface of B. anthracis. The A regions of the two proteins were predicted to adopt similar structural folds as CNA. Circular dichroism analysis of the recombinant A regions of the two proteins (rBA0871A and rBA5258A) indicate that their secondary structure compositions are similar to those of the A regions of CNA and other cell wall-anchored adhesins. We demonstrate through solid phase binding assays and surface plasmon resonance analyses that rBA0871A and rBA5258A specifically bound type I collagen in a dose-dependent and saturable manner. Their dissociation constants (K_D) for collagen are 1.6–3.2 µM for rBA0871A and 0.6–0.9 µM for rBA5258A, respectively. We further demonstrate that BA0871 and BA5258 can mediate cell attachment to collagen when expressed on the surface of a heterologous host bacterium. To our knowledge these are the first two adhesins of B. anthracis described, which may have important implications for our understanding of the pathogenic mechanisms explored by this organism.

Received for publication, June 9, 2004 , and in revised form, September 20, 2004.

^* This work was supported by National Institutes of Health Grants AI020624-21 and AR44415 (to M. H.) by AIO6155501 (to Y. X.), and by a grant through the Western Regional Center of Excellence for Biodefense and Emerging Infectious Disease Research, National Institutes of Health Grant U54 AI057156 (to T. M. K.). 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 should be addressed: The Center for Extracellular Matrix Biology, Texas A&M University System Health Science Center, Institute of Biosciences and Technology, 2121 West Holcombe Blvd., Suite 603, Houston, TX 77030. Tel.: 713-677-7555; Fax: 713-677-7576; E-mail: yxu{at}ibt.tamushsc.edu.

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