Abstract
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)The protein sequence data reported in this paper will appear in the Swiss-Prot and TrEMBL knowledgebase under the accession numbers P84105 for arenicin-1 and P84106 for arenicin-2.1 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.
Original language | English |
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Pages (from-to) | 209-214 |
Number of pages | 6 |
Journal | FEBS Letters |
Volume | 577 |
Issue number | 1-2 |
DOIs | |
Publication status | Published - 05 Nov 2004 |
Keywords
- Antimicrobial peptide
- Arenicin
- Arenicola marina
- cDNA
- Innate immunity
- Lugworm
- Marine invertebrate
- Precursor
- Primary structure
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology