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 Jacobs, T.
Right arrow Articles by Leippe, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jacobs, T.
Right arrow Articles by Leippe, M.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, February 2003, p. 607-613, Vol. 47, No. 2
0066-4804/03/$08.00+0     DOI: 10.1128/AAC.47.2.607-613.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

NK-Lysin and Its Shortened Analog NK-2 Exhibit Potent Activities against Trypanosoma cruzi

Thomas Jacobs,1* Heike Bruhn,2 Iris Gaworski,1 Bernhard Fleischer,1 and Matthias Leippe2

Department of Immunology, Bernhard Nocht Institute for Tropical Medicine, Hamburg,1 Molecular Parasitology Group, Research Center for Infectious Diseases, Wuerzburg, Germany2

Received 9 August 2002/ Returned for modification 3 October 2002/ Accepted 30 October 2002

Antimicrobial peptides are widespread in nature and have been evolutionarily conserved as essential tools for combating a variety of pathogens. Among the plethora of natural peptides and synthetic analogs thereof studied in recent years for their antimicrobial activities, only a very few are known to be effective against protozoan parasites. In the present study we investigated the activity of NK-lysin, a broad-spectrum effector polypeptide of mammalian cytotoxic lymphocytes, against trypomastigotes of the human pathogen Trypanosoma cruzi in vitro. Moreover, the activity of a synthetic peptide named NK-2 that corresponds to the cationic core region of NK-lysin was tested in parallel against this parasite. T. cruzi was found to be highly susceptible to both peptides, as evidenced by inhibition of the mobility of trypomastigotes. The peptides rapidly permeabilized the plasma membrane of the parasite since micromolar concentrations resulted in the release of cytosolic enzymes within minutes. NK-lysin and NK-2 were even found to kill trypanosomes residing inside the human glioblastoma cell line 86HG39, but only NK-2 left the host cells apparently unharmed.

* Corresponding author. Mailing address: Department of Immunology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany. Phone: 49-(0)40-42818-243. Fax: 49-(0)40-42818-400. E-mail: tjacobs{at}bni.uni-hamburg.de.

Antimicrobial Agents and Chemotherapy, February 2003, p. 607-613, Vol. 47, No. 2
0066-4804/03/$08.00+0     DOI: 10.1128/AAC.47.2.607-613.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gelhaus, C., Jacobs, T., Andra, J., Leippe, M. (2008). The Antimicrobial Peptide NK-2, the Core Region of Mammalian NK-Lysin, Kills Intraerythrocytic Plasmodium falciparum. Antimicrob. Agents Chemother. 52: 1713-1720 [Abstract] [Full Text]  
  • Banerjee, A., Roychoudhury, J., Ali, N. (2008). Stearylamine-bearing cationic liposomes kill Leishmania parasites through surface exposed negatively charged phosphatidylserine. J Antimicrob Chemother 61: 103-110 [Abstract] [Full Text]  
  • Lieke, T., Graefe, S. E. B., Klauenberg, U., Fleischer, B., Jacobs, T. (2004). NK Cells Contribute to the Control of Trypanosoma cruzi Infection by Killing Free Parasites by Perforin-Independent Mechanisms. Infect. Immun. 72: 6817-6825 [Abstract] [Full Text]  
  • Endsley, J. J., Furrer, J. L., Endsley, M. A., McIntosh, M. A., Maue, A. C., Waters, W. R., Lee, D. R., Estes, D. M. (2004). Characterization of Bovine Homologues of Granulysin and NK-lysin. J. Immunol. 173: 2607-2614 [Abstract] [Full Text]  
  • Andra, J., Koch, M. H. J., Bartels, R., Brandenburg, K. (2004). Biophysical Characterization of Endotoxin Inactivation by NK-2, an Antimicrobial Peptide Derived from Mammalian NK-Lysin. Antimicrob. Agents Chemother. 48: 1593-1599 [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»