The crystal structure of the Bacillus anthracis spore surface protein BclA shows remarkable similarity to mammalian proteins.

J Biol Chem

Laboratoire de Biotechnologies et Pharmacologie Génétique Appliquées, CNRS, Unité Mixte de Recherche 8113, Ecole Normale Supérieure de Cachan, 61 Avenue du Président Wilson, 94235 Cachan, France.

Published: December 2005

AI Article Synopsis

  • Anthrax is a deadly disease caused by Bacillus anthracis spores, which can enter the body through inhalation and lead to severe outcomes.
  • Researchers have determined the three-dimensional structure of a key surface protein called BclA on these spores, finding that it resembles a mammalian protein called C1q, despite having no genetic similarities.
  • Although BclA does not function exactly like C1q in lab tests, it can still interact with elements in the lung, suggesting that this bacterium may have adapted to better infect its hosts by evolving a surface protein similar in shape to those found in mammals.

Article Abstract

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 outcome. We have solved the three-dimensional structure of the major surface protein BclA on B. anthracis spores. Surprisingly, the structure resembles C1q, the first component of complement, despite there being no sequence homology. Although 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, to better recognize and invade its hosts, this pathogenic soil bacterium may have evolved a surface protein whose structure is strikingly close to a mammalian protein.

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http://dx.doi.org/10.1074/jbc.M510087200DOI Listing

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