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  Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans

Urban, C. F., Ermert, D., Schmid, M., Abu-Abed, U., Goosmann, C., Nacken, W., et al. (2009). Neutrophil Extracellular Traps Contain Calprotectin, a Cytosolic Protein Complex Involved in Host Defense against Candida albicans. PLoS Pathogens, 5(10): e1000639.

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PLoS_Pathogens_2009_5_e1000639.pdf (Publisher version), 2MB
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© 2009 Urban et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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Urban, Constantin F.1, Author              
Ermert, David1, Author              
Schmid, Monika2, Author              
Abu-Abed, Ulrike1, 3, Author              
Goosmann, Christian1, 3, Author              
Nacken, Wolfgang, Author
Brinkmann, Volker3, Author              
Jungblut, Peter R.2, Author              
Zychlinsky, Arturo1, Author              
Affiliations:
1Department of Cellular Microbiology, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664145              
2Core Facilities / Proteinanalysis, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664143              
3Core Facilities / Microscopy, Max Planck Institute for Infection Biology, Max Planck Society, ou_1664142              

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 Abstract: Neutrophils are the first line of defense at the site of an infection. They encounter and kill microbes intracellularly upon phagocytosis or extracellularly by degranulation of antimicrobial proteins and the release of Neutrophil Extracellular Traps (NETs). NETs were shown to ensnare and kill microbes. However, their complete protein composition and the antimicrobial mechanism are not well understood. Using a proteomic approach, we identified 24 NET-associated proteins. Quantitative analysis of these proteins and high resolution electron microscopy showed that NETs consist of modified nucleosomes and a stringent selection of other proteins. In contrast to previous results, we found several NET proteins that are cytoplasmic in unstimulated neutrophils. We demonstrated that of those proteins, the antimicrobial heterodimer calprotectin is released in NETs as the major antifungal component. Absence of calprotectin in NETs resulted in complete loss of antifungal activity in vitro. Analysis of three different Candida albicans in vivo infection models indicated that NET formation is a hitherto unrecognized route of calprotectin release. By comparing wild-type and calprotectin-deficient animals we found that calprotectin is crucial for the clearance of infection. Taken together, the present investigations confirmed the antifungal activity of calprotectin in vitro and, moreover, demonstrated that it contributes to effective host defense against C. albicans in vivo. We showed for the first time that a proportion of calprotectin is bound to NETs in vitro and in vivo.

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Language(s): eng - English
 Dates: 2009-10
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: eDoc: 572808
ISI: 000272033300043
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Title: PLoS Pathogens
Source Genre: Journal
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Pages: - Volume / Issue: 5 (10) Sequence Number: e1000639 Start / End Page: - Identifier: ISSN: 1553-7366