Fulltext

Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei

Baumann, Tommy ; Kämpfer, Urs ; Schürch, Stefan ; Schaller, Johann ; Largiadèr, Carlo ; Nentwig, Wolfgang ; Kuhn-Nentwig, Lucia

In: Cellular and Molecular Life Sciences, 2010, vol. 67, no. 16, p. 2787-2798

Ajouter à la liste personnelle
    Titre
    • Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei
    Auteur
    • Baumann, Tommy. Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, 3012, Bern, Switzerland
    • Kämpfer, Urs. Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland
    • Schürch, Stefan. Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland
    • Schaller, Johann. Department of Chemistry and Biochemistry, University of Bern, Freiestrasse 3, 3012, Bern, Switzerland
    • Largiadèr, Carlo. Institute of Clinical Chemistry, Bern University Hospital, University of Bern, INO F, 3010, Bern, Switzerland
    • Nentwig, Wolfgang. Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, 3012, Bern, Switzerland
    • Kuhn-Nentwig, Lucia. Institute of Ecology and Evolution, University of Bern, Baltzerstrasse 6, 3012, Bern, Switzerland
    Type de document
    • Postprint
    Langue
    • Anglais
    Publié dans
    • Cellular and Molecular Life Sciences, 2010, vol. 67, no. 16, p. 2787-2798. SP Birkhäuser Verlag Basel
    Autre version électronique
    Identifiant OAI-PMH
    • oai:doc.rero.ch:311845
    Summary
    Three novel glycine-rich peptides, named ctenidin 1-3, with activity against the Gram-negative bacterium E. coli, were isolated and characterized from hemocytes of the spider Cupiennius salei. Ctenidins have a high glycine content (>70%), similarly to other glycine-rich peptides, the acanthoscurrins, from another spider, Acanthoscurria gomesiana. A combination of mass spectrometry, Edman degradation, and cDNA cloning revealed the presence of three isoforms of ctenidin, at least two of them originating from simple, intronless genes. The full-length sequences of the ctenidins consist of a 19 amino acid residues signal peptide followed by the mature peptides of 109, 119, or 120 amino acid residues. The mature peptides are post-translationally modified by the cleavage of one or two C-terminal cationic amino acid residue(s) and amidation of the newly created mature C-terminus. Tissue expression analysis revealed that ctenidins are constitutively expressed in hemocytes and to a small extent also in the subesophageal nerve mass