NADPH-oxidase but not inducible nitric oxide synthase contributes to resistance in a murine Staphylococcus aureus Newman pneumonia model |
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Authors: | Köhler Jens Breitbach Katrin Renner Cäcilia Heitsch Anne-Katrin Bast Antje van Rooijen Nico Vogelgesang Silke Steinmetz Ivo |
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Institution: | aFriedrich Loeffler Institute of Medical Microbiology, Ernst Moritz Arndt University Greifswald, Martin-Luther Str. 6, 17489 Greifswald, Germany;bDepartment of Cell Biology and Immunology, Faculty of Medicine, Vrije Universiteit, Amsterdam, The Netherlands;cDepartment of Pathology, University of Greifswald, Friedrich-Loeffler Str. 23a, 17489 Greifswald, Germany |
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Abstract: | Staphylococcus aureus is a pathogen that often causes severe nosocomial infections including pneumonia. The present study was designed to examine innate phagocyte mediated immune mechanisms using a previously described murine S. aureus Newman pneumonia model. We found that BALB/c mice represent a more susceptible mouse strain compared to C57BL/6 mice after intranasal S. aureus Newman challenge. Depletion experiments revealed that neutrophils are a crucial determinant for resistance whereas depletion of alveolar macrophages protected mice to some degree from acute pulmonary S. aureus challenge. C57BL/6 mice lacking the subunit gp91phox of the NADPH-oxidase (gp91phox−/− mice) proved to be highly susceptible against the pathogen. In contrast, C57BL/6 inducible nitric oxidase synthase deficient (iNOS−/−) mice did not differ in their clinical outcome after infection. Neither bone marrow macrophages from iNOS−/− nor from gp91phox−/− mice were impaired in controlling intracellular persistence of S. aureus. Our data suggest that neutrophil and NADPH-oxidase mediated mechanisms are essential components in protecting the host against pulmonary S. aureus Newman challenge. On contrary, macrophages as well as NO mediated mechanisms do not seem to play a critical role for resistance in this model. |
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Keywords: | Staphylococcus aureus Macrophage Neutrophil Nitric oxide NADPH-oxidase |
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