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High Bactericidal Efficiency of Type IIA Phospholipase A₂ against Bacillus anthracis and Inhibition of Its Secretion by the Lethal Toxin¹

Alejandro Piris Gimenez^*, Yong-Zheng Wu, Miguel Paya, Christophe Delclaux, Lhousseine Touqui and Pierre L. Goossens^2,*

^* Unité Toxines et Pathogénie Bactérienne/Centre National de la Recherche Scientifique, and Unité de Défense Innée et Inflammation/Unité Associée, Institut National de la Santé et de la Recherche Médicale, Institut Pasteur, Paris, France; and Institut National de la Santé et de la Recherche Médicale, Unité 492, Service de Physiologie-Explorations Fonctionnelles, Hôpital Henri Mondor, Créteil, France

There is a considerable body of evidence supporting the role of secretory type II-A phospholipase A₂ (sPLA₂-IIA) as an effector of the innate immune response. This enzyme also exhibits bactericidal activity especially toward Gram-positive bacteria. In this study we examined the ability of sPLA₂-IIA to kill Bacillus anthracis, the etiological agent of anthrax. Our results show that both germinated B. anthracis spores and encapsulated bacilli were sensitive to the bactericidal activity of recombinant sPLA₂-IIA in vitro. In contrast, nongerminated spores were resistant. This bactericidal effect was correlated to the ability of sPLA₂-IIA to hydrolyze bacterial membrane phospholipids. Guinea pig alveolar macrophages, the major source of sPLA₂-IIA in an experimental model of acute lung injury, released enough sPLA₂-IIA to kill extracellular B. anthracis. The production of sPLA₂-IIA was significantly inhibited by B. anthracis lethal toxin. Human bronchoalveolar lavage fluids from acute respiratory distress syndrome patients are known to contain sPLA₂-IIA; bactericidal activity against B. anthracis was detected in a high percentage of these samples. This anthracidal activity was correlated to the levels of sPLA₂-IIA and was abolished by an sPLA₂-IIA inhibitor. These results suggest that sPLA₂-IIA may play a role in innate host defense against B. anthracis infection and that lethal toxin may help the bacteria to escape from the bactericidal action of sPLA₂-IIA by inhibiting the production of this enzyme.

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