Biochem Biophys Res Commun, 2006, 348(2):514-523

Aurelin, a novel antimicrobial peptide from jellyfish Aurelia aurita with structural features of defensins and channel-blocking toxins

A novel 40-residue antimicrobial peptide, aurelin, exhibiting activity against Gram-positive and Gram-negative bacteria, was purified from the mesoglea of a scyphoid jellyfish Aurelia aurita by preparative gel electrophoresis and RP-HPLC. Molecular mass (4296.95 Da) and complete amino acid sequence of aurelin (AACSDRAHGHICESFKSFCKDSGRNGVKLRANCKKTCGLC)1The protein sequence data reported in this paper will appear in the UniProt Knowledge base under the Accession No. P84891 and in the GenBank under the Accession No. DQ837210.1were determined. Aurelin has six cysteines forming three disulfide bonds. The total RNA was isolated from the jellyfish mesoglea, RT-PCR and cloning were performed, and cDNA was sequenced. A 84-residue preproaurelin contains a putative signal peptide (22 amino acids) and a propiece of the same size (22 amino acids). Aurelin has no structural homology with any previously identified antimicrobial peptides but reveals partial similarity both with defensins and K+channel-blocking toxins of sea anemones and belongs to ShKT domain family. © 2006 Elsevier Inc. All rights reserved.

Ovchinnikova TV, Balandin SV, Aleshina GM, Tagaev AA, Leonova YF, Krasnodembsky ED, Menshenin AV, Kokryakov VN

IBCH: 5298
Ссылка на статью в журнале: http://linkinghub.elsevier.com/retrieve/pii/S0006291X06016305
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