## Abstract Antimicrobial peptides (AMPs), named lycocitin 1, 2 and 3, and a peptide with a monoisotopic molecular mass of 3038.70 Da were detected in the venom glands of the wolf spider __Lycosa singoriensis__. Two of the peptides, lycocitin 1 and 2, are new AMPs whereas lycocitin 3 is highly homo
A defensin-like antimicrobial peptide from the venoms of spider, Ornithoctonus hainana
✍ Scribed by Hongwen Zhao; Yi Kong; Hanjin Wang; Tianhua Yan; Feifei Feng; Jianmin Bian; Yan Yang; Haining Yu
- Publisher
- John Wiley and Sons
- Year
- 2011
- Tongue
- English
- Weight
- 188 KB
- Volume
- 17
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.1370
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✦ Synopsis
Abstract
The defensin‐like antimicrobial peptides have been characterized from various other arthropods including insects, scorpions, and ticks. But no natural spider defensin‐like antimicrobial peptides have ever been isolated from spiders, except couple of cDNA and DNA sequences of five spider species revealed by previous genomic study. In this work, a defensin‐like antimicrobial peptide named Oh‐defensin was purified and characterized from the venoms of the spider, Ornithoctonus hainana. Oh‐defensin is composed of 52 amino acid (aa) residues including six Cys residues that possibly form three disulfide bridges. Its aa sequence is MLCKLSMFGAVLGV PACAIDCLPMGKTGGSCEGGVCGCRKLTFKILWDKKFG. By BLAST search, Oh‐defensin showed significant sequence similarity to other arthropod antimicrobial peptides of the defensin family. Oh‐defensin exerted potent antimicrobial activities against tested microorganisms including Gram‐positive bacteria, Gram‐negative bacteria, and fungi. The cDNA encoding Oh‐defensin precursor was also cloned from the cDNA library of O. hainana. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.
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