Journal
FEBS LETTERS
Volume 577, Issue 1-2, Pages 209-214Publisher
WILEY
DOI: 10.1016/j.febslet.2004.10.012
Keywords
antimicrobial peptide; arenicin; lugworm; marine invertebrate; innate immunity; primary structure; cDNA; precursor; Arenicola marina
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Two novel 21-residue antimicrobial peptides, arenicin-1 and arenicin-2, exhibiting activity against Gram-positive and Gram-negative bacteria and fungi, were purified from coelomocytes of marine polychaeta Arenicola marina (lugworm) by preparative gel electrophoresis and RP-HPLC. Molecular masses (2758.3 and 2772.3 Da) and complete amino acid sequences (RWCVYAYVRVRGVLVRYRRCW and RWCVYAYVRIRGVLVRYRRCW)(1) were determined for each isoform. Each arenicin has one disulfide bond (Cys3-Cys20). The total RNA was isolated from the lugworm coelomocytes, RT-PCR and cloning were performed, and cDNA was sequenced. A 202-residue preproarenicin contains a putative signal peptide (25 amino acids) and a long prodomain. Arenicins have no structure similarity to any previously identified antimicrobial peptides. (C) 2004 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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