Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina

Tatiana V. Ovchinnikova*, Galina M. Aleshina, Sergey V. Balandin, Anna Krasnodembskaya, Mikhail L. Markelov, Elena I. Frolova, Yulia F. Leonova, Andrey A. Tagaev, Eugeny G. Krasnodembsky, Vladimir N. Kokryakov

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

101 Citations (Scopus)

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 languageEnglish
Pages (from-to)209-214
Number of pages6
JournalFEBS Letters
Volume577
Issue number1-2
DOIs
Publication statusPublished - 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

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