This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Fluckinger, M.
Right arrow Articles by Redl, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fluckinger, M.
Right arrow Articles by Redl, B.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, September 2004, p. 3367-3372, Vol. 48, No. 9
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.9.3367-3372.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Human Tear Lipocalin Exhibits Antimicrobial Activity by Scavenging Microbial Siderophores

Maria Fluckinger,1 Hubertus Haas,1 Petra Merschak,1 Ben J. Glasgow,2 and Bernhard Redl1*

Department of Molecular Biology, Innsbruck Medical University, Innsbruck, Austria,1 Department of Pathology and Ophthalmology, Jules Stein Eye Institute, School of Medicine, University of California at Los Angeles, Los Angeles, California2

Received 3 February 2004/ Returned for modification 19 March 2004/ Accepted 3 May 2004

Human tear lipocalin (TL; also known as Lcn1) is a secretory protein present in large amounts in fluids that cover epithelial surfaces such as tears and respiratory secretions. It is supposed to act as a physiological scavenger of hydrophobic, potentially harmful molecules, but there is evidence that it also inhibits bacterial growth. In the present study, we reconsidered the possibility that TL might interfere with microbial growth by scavenging of siderophores, as described for human neutrophil gelatinase-associated lipocalin (NGAL). Indeed, our experiments revealed that TL binds to microbial siderophores with high affinities. In contrast to NGAL, which was shown to have some specificity for bacterial catecholate-type siderophores, TL binds to a broad array of siderophores, including bacterial catecholate-type enterobactin and hydroxamate-type desferrioxamine B, and all major classes of fungal siderophores. By adding exogenous TL, bacterial and fungal growth could be inhibited under iron-limiting conditions. Thus, TL might be a novel member of the innate immune system especially involved in mucosal defense against fungal infections.

* Corresponding author. Mailing address: Department of Molecular Biology, Innsbruck Medical University, Peter-Mayr Strasse 4b, A-6020 Innsbruck, Austria. Phone: (43) 512-507-3603. Fax: (43) 512-507-2866. E-mail: bernhard.redl{at}uibk.ac.at.

Antimicrobial Agents and Chemotherapy, September 2004, p. 3367-3372, Vol. 48, No. 9
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.9.3367-3372.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Klein, L. L., Jonscher, K. R., Heerwagen, M. J., Gibbs, R. S., McManaman, J. L. (2008). Shotgun Proteomic Analysis of Vaginal Fluid From Women in Late Pregnancy. Reproductive Sciences 15: 263-273 [Abstract]  
  • Doyle, M. E., Boggs, L., Attia, R., Cooper, L. R., Saban, D. R., Nguyen, C. Q., Peck, A. B. (2007). Autoimmune Dacryoadenitis of NOD/LtJ Mice and Its Subsequent Effects on Tear Protein Composition. Am. J. Pathol. 171: 1224-1236 [Abstract] [Full Text]  
  • Miethke, M., Marahiel, M. A. (2007). Siderophore-Based Iron Acquisition and Pathogen Control. Microbiol. Mol. Biol. Rev. 71: 413-451 [Abstract] [Full Text]  
  • Krithika, R., Marathe, U., Saxena, P., Ansari, Mohd. Z., Mohanty, D., Gokhale, R. S. (2006). A genetic locus required for iron acquisition in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. USA 103: 2069-2074 [Abstract] [Full Text]  
  • Breustedt, D. A., Korndorfer, I. P., Redl, B., Skerra, A. (2005). The 1.8-A Crystal Structure of Human Tear Lipocalin Reveals an Extended Branched Cavity with Capacity for Multiple Ligands. J. Biol. Chem. 280: 484-493 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»