Baumann, Tommy; Kämpfer, Urs; Schürch, Stefan; Schaller, Johann; Largiadèr, Carlo; Nentwig, Wolfgang; Kuhn-Nentwig, Lucia (2010). Ctenidins: antimicrobial glycine-rich peptides from the hemocytes of the spider Cupiennius salei. Cellular and molecular life sciences, 67(16), pp. 2787-2798. Basel: SP Birkhäuser Verlag Basel 10.1007/s00018-010-0364-0
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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.
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