An anionic antimicrobial peptide from toad Bombina maxima

被引:141
作者
Lai, R [1 ]
Liu, H [1 ]
Lee, WH [1 ]
Zhang, Y [1 ]
机构
[1] Chinese Acad Sci, Kunming Inst Zool, Dept Anim Toxicol, Kunming 650223, Yunnan, Peoples R China
基金
中国国家自然科学基金;
关键词
anionic antimicrobial peptide; cationic antimicrobial peptide; amphibian; Bombina maxima; maximin H; cDNA clone;
D O I
10.1016/S0006-291X(02)00762-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Amphibian skin is a rich resource of antimicrobial peptides like maximins and maximins H from toad Bombina maxima. A novel cDNA clone encoding a precursor protein that comprises maximin 3 and a novel peptide. named maximin H5. was isolated from a skin cDNA library of B. maxima. The predicted primary structure of maximin H5 is ILGPVLGLVSDTLDDVLGIL-NH2,. Containing three aspartate residues and no basic amino acid residues. maximin H5 is characterized by an anionic property. Different from cationic maximin H peptides. only Gram-positive strain Staphylococcus aureus was sensitive to maximin H5. while the other bacteria] and fungal strains tested ere resistant to it. The presence of metal ions. like Zn2+ and Mg2+, did not increase its antimicrobial potency. Maximin H5 represents the first example of potential anionic antimicrobial peptides from amphibians, The results provide the first evidence that. together kith cationic antimicrobial peptides. anionic antimicrobial peptides may also exist naturally as part of the innate defense system. (C), 2002 Elsevier Science (USA). All rights reserved.
引用
收藏
页码:796 / 799
页数:4
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