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

Cellular and Molecular Life Sciences - Tập 67 - Trang 2787-2798 - 2010
Tommy Baumann1, Urs Kämpfer2, Stefan Schürch2, Johann Schaller2, Carlo Largiadèr3, Wolfgang Nentwig1, Lucia Kuhn-Nentwig1
1Institute of Ecology and Evolution, University of Bern, Bern, Switzerland
2Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland
3Institute of Clinical Chemistry, Bern University Hospital, University of Bern, Bern, Switzerland

Tóm tắt

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.

Tài liệu tham khảo

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