期刊
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
卷 67, 期 -, 页码 310-321出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2016.09.002
关键词
Invertebrate; Antimicrobial activity; Secondary structure; Protein purification; Membrane binding; Defensins
资金
- IFS [F/5024-1, F/5024-2]
- VLIR-UOS [ZEIN2013Z134]
Beta_defensin have been solely found in vertebrates until beta-defensin-like peptides were described as transcript isoforms in two species of Panulirus genus. They were considered as putative antimicrobials since their biological activity have not been demonstrated. Here we purified and characterized a defensin-like peptide from the hemocytes of spiny lobster P. argus, hereafter named panusin. Structurally, panusin presents a cysteine-stabilized alpha/beta motif, and is prone to form homodimers. Biological activity of panusin showed broad-spectrum antimicrobial activity, characterized for being strikingly salt-resistant. Panusin did not showed hemolytic activity but was demonstrated its binding capacity to different lipid membrane models, indicating amphipathicity of beta-sheet core as driving force for its antimicrobial activity. Panusin is considered a new kind of arthropod defensin which share structural and biological features with beta-defensin from vertebrates. The presence of beta-defensin like peptides in crustacean might suggest the emergence of the evolutionary relationship of beta-defensins from vertebrates. (C) 2016 Elsevier Ltd. All rights reserved.
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