Baumann, TommyTommyBaumann0000-0002-5950-4137Kämpfer, UrsUrsKämpferSchürch, StefanStefanSchürchSchaller, JohannJohannSchallerLargiadèr, Carlo RodolfoCarlo RodolfoLargiadèrNentwig, WolfgangWolfgangNentwigKuhn-Nentwig, Lucia GerdaLucia GerdaKuhn-Nentwig2024-12-132024-12-132010https://boris-portal.unibe.ch/handle/20.500.12422/191840Three 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.en500 - Science::570 - Life sciences; biology500 - Science::590 - Animals (Zoology)500 - Science::580 - Plants (Botany)500 - Science::540 - Chemistryarticle10.7892/boris.31942036927200028056460000710.1007/s00018-010-0364-0