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Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina
Author(s) -
Ovchinnikova Tatiana V.,
Aleshina Galina M.,
Balandin Sergey V.,
Krasnosdembskaya Anna D.,
Markelov Mikhail L.,
Frolova Elena I.,
Leonova Yulia F.,
Tagaev Andrey A.,
Krasnodembsky Eugeny G.,
Kokryakov Vladimir N.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.10.012
Subject(s) - arenicola , peptide , antimicrobial , biochemistry , antimicrobial peptides , peptide sequence , biology , amino acid , protein primary structure , gene isoform , complementary dna , signal peptide , microbiology and biotechnology , ecology , gene
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.