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A more recent version of this article appeared on December 30, 2005
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280/52/43073    most recent
M510087200v1
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Papers In Press, published online ahead of print October 25, 2005
J. Biol. Chem, 10.1074/jbc.M510087200
Submitted on September 14, 2005
Accepted on October 25, 2005

The crystal structure of the bacillus anthracis spore surface protein, BCLA, shows remarquable similarity to mammalian proteins

Stéphane Réty, Sylvie Salamitou, Ignacio Garcia-Verdugo, David J.S. Hulmes, Françoise Le Hégarat, Richard Chaby, and Anita Lewit-Bentley

LBPA, UMR8113, CNRS, Cachan 94235

Corresponding Author: anita.bentley{at}lbpa.ens-cachan.fr

The lethal disease anthrax is propagated by spores of Bacillus anthracis which can penetrate into the mammalian host by inhalation, causing a rapid progression of the disease and a mostly fatal issue. We have solved the three-dimensional structure of the major surface protein on B. anthracis spores, BclA. Surprisingly, the structure resembles C1q, the first component of complement, in spite of there being no sequence homology. While most assays for C1q-like activity, including binding to C1q receptors, suggest that BclA does not mimic C1q, we show that BclA, as well as C1q, interacts with components of the lung alveolar surfactant layer. Thus this pathogenic soil bacterium may have evolved a surface protein whose structure is strikingly close to a mammalian protein in order to bettter recognise and invade its hosts.


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