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Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells

Kuhn-Nentwig, Lucia ; Willems, Jean ; Seebeck, Thomas ; Shalaby, Tarek ; Kaiser, Marcel ; Nentwig, Wolfgang

In: Amino Acids, 2011, vol. 40, no. 1, p. 69-76

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    Titre
    • Cupiennin 1a exhibits a remarkably broad, non-stereospecific cytolytic activity on bacteria, protozoan parasites, insects, and human cancer cells
    Auteur
    • Kuhn-Nentwig, Lucia. Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, 3012, Bern, Switzerland
    • Willems, Jean. Department of Medicine Laboratory of Biochemistry, Interdisciplinary Research Centre, K.U. Leuven, Campus Kortrijk, 8500, Kortrijk, Belgium
    • Seebeck, Thomas. Institute of Cell Biology, University of Bern, Baltzerstrasse 4, 3012, Bern, Switzerland
    • Shalaby, Tarek. Children's Hospital Zürich, University Children's Clinic, Steinwiesstrasse 75, 8032, Zurich, Switzerland
    • Kaiser, Marcel. Swiss Tropical Institute, Socinstrasse 57, P.O. Box 4002, Basel, Switzerland
    • Nentwig, Wolfgang. Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, 3012, Bern, Switzerland
    Type de document
    • Postprint
    Identifiant OAI-PMH
    • oai:doc.rero.ch:311086
    Summary
    Cupiennin 1a, a cytolytic peptide isolated from the venom of the spider Cupiennius salei, exhibits broad membranolytic activity towards bacteria, trypanosomes, and plasmodia, as well as human blood and cancer cells. In analysing the cytolytic activity of synthesised all-d- and all-l-cupiennin 1a towards pro- and eukaryotic cells, a stereospecific mode of membrane destruction could be excluded. The importance of negatively charged sialic acids on the outer leaflet of erythrocytes for the binding and haemolytic activity of l-cupiennin 1a was demonstrated. Reducing the overall negative charges of erythrocytes by partially removing their sialic acids or by protecting them with tri- or pentalysine results in reduced haemolytic activity of the peptide