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 Andersson, M.
Right arrow Articles by Cazenave, P.-A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Andersson, M.
Right arrow Articles by Cazenave, P.-A.

 Previous Article  |  Next Article 

Infection and Immunity, January 1999, p. 201-205, Vol. 67, No. 1
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Interaction of NK Lysin, a Peptide Produced by Cytolytic Lymphocytes, with Endotoxin

M. Andersson,1,* R. Girard,2 and P.-A. Cazenave1

Immunochimie Analytique1 and Immunophysiologie Moléculaire,2 URA CNRS 1961, Departement d'Immunologie, Institut Pasteur, Paris, France

Received 27 January 1998/Returned for modification 17 April 1998/Accepted 26 October 1998

NK lysin is a 9-kDa polypeptide that was originally isolated from porcine intestinal tissue based on its antibacterial activity. It is produced by cytolytic lymphocytes and is cytolytic against a number of different types of tumor cells. Here we report the binding of NK lysin to lipopolysaccharide (LPS) and its anti-LPS activity. NK lysin binds to matrix-coated LPS from Escherichia coli, Pseudomonas aeruginosa, and different strains of Salmonella enterica. Lipid A and polymyxin B inhibited the binding, demonstrating a preferential interaction of NK lysin with the lipid part of LPS. Chromium-labeled lymphoma cells were lysed by NK lysin, and LPS dose-dependently inhibited the cytolysis at equimolar amounts. In the same manner, NK lysin inhibited certain LPS-stimulated effects on mouse bone marrow cells as well as LPS binding to mouse granulocytes. These results suggest that NK lysin may be a another natural LPS-binding protein from lymphocytes that may participate in the endogenous defense response associated with elevated concentrations of LPS.

* Corresponding author. Present address: Chemistry I, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden. Phone: 46 8 728 76 99. Fax: 46 8 33 74 62. E-mail: mats.andersson{at}mbb.ki.se.

Infection and Immunity, January 1999, p. 201-205, Vol. 67, No. 1
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Andra, J., Gutsmann, T., Garidel, P., Brandenburg, K. (2006). Invited review: Mechanisms of endotoxin neutralization by synthetic cationic compounds. Innate Immunity 12: 261-277 [Abstract]  
  • Sordillo, L. M., Kendall, J. T., Corl, C. M., Cross, T. H. (2005). Molecular Characterization of a Saposin-Like Protein Family Member Isolated from Bovine Lymphocytes. J DAIRY SCI 88: 1378-1390 [Abstract] [Full Text]  
  • Levy, O. (2004). Antimicrobial proteins and peptides: anti-infective molecules of mammalian leukocytes. J. Leukoc. Biol. 76: 909-925 [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]  
  • Amoureux, M.-C., Hegyi, E., Le, D., Grandics, P., Tong, H., Szathmary, S. (2004). A new method for removing endotoxin from plasma using hemocompatible affinity chromatography technology, applicable for extracorporeal treatment of septic patients. Innate Immunity 10: 85-95 [Abstract]  
  • Herbst, R., Ott, C., Jacobs, T., Marti, T., Marciano-Cabral, F., Leippe, M. (2002). Pore-forming Polypeptides of the Pathogenic Protozoon Naegleria fowleri. J. Biol. Chem. 277: 22353-22360 [Abstract] [Full Text]  
  • Levy, O. (2000). Antimicrobial proteins and peptides of blood: templates for novel antimicrobial agents. Blood 96: 2664-2672 [Abstract] [Full Text]  
  • Kourie, J. I., Shorthouse, A. A. (2000). Properties of cytotoxic peptide-formed ion channels. Am. J. Physiol. Cell Physiol. 278: C1063-C1087 [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»