Literature DB >> 15527787

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

Tatiana V Ovchinnikova1, Galina M Aleshina, Sergey V Balandin, Anna D Krasnosdembskaya, Mikhail L Markelov, Elena I Frolova, Yulia F Leonova, Andrey A Tagaev, Eugeny G Krasnodembsky, Vladimir N Kokryakov.   

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) 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.

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Year:  2004        PMID: 15527787     DOI: 10.1016/j.febslet.2004.10.012

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  28 in total

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8.  Identification and characterization of a chitin-binding protein purified from coelomic fluid of the lugworm Arenicola marina defining a novel protein sequence family.

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9.  Structure and Biological Functions of β-Hairpin Antimicrobial Peptides.

Authors:  P V Panteleev; I A Bolosov; S V Balandin; T V Ovchinnikova
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10.  Immune response of the Caribbean sea fan, Gorgonia ventalina, exposed to an Aplanochytrium parasite as revealed by transcriptome sequencing.

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