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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

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.

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