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蛙科两栖动物皮肤抗菌肽的分子多样性及功能
引用本文:金莉莉,王秋雨. 蛙科两栖动物皮肤抗菌肽的分子多样性及功能[J]. 遗传, 2008, 30(10): 1241-1248. DOI: 10.3724/SP.J.1005.2008.01241
作者姓名:金莉莉  王秋雨
作者单位:辽宁大学生命科学院, 沈阳 110036
摘    要:摘要: 蛙科(Ranidae)是全球分布最广泛的两栖动物, 种类超过650种。为开拓和适应广阔的栖息地及多样的生态环境, 其皮肤腺体中进化产生了结构复杂、种类繁多的抗菌肽。它们除具有广谱抗菌活性外, 还有抗肿瘤、抗病毒等生物学活性。蛙科动物皮肤抗菌肽起源于共同祖先, 在漫长的进化过程中, 基因发生了多重复制和突变, 形成了天然抗菌肽的巨大资源库。这些肽在模拟膜的溶剂中几乎都是疏水的, 并带正电荷, 以一种两亲性的α-螺旋的构象存在。根据氨基酸组成及结构的相似性, 可以将蛙科动物抗菌肽分成brevinin-1、esculentin-1、esculentin-2、temporin、ranalexin、ranatuerin-1、ranatuerin-2、plaustrin、brevinin-2、tigerinin、japonicin、nigrocin和melittin相关肽等若干个家族。文章结合作者的研究工作, 综述了目前已经鉴定的蛙科动物皮肤抗菌肽的分子多样性特点、家族性质和生物学活性的研究进展, 并阐述了东北林蛙新家族抗菌肽的特点。 关键词: 蛙科; 抗菌肽家族; 分子多样性; 生物学活性

关 键 词:分子多样性  生物学活性  蛙科  抗菌肽家族  
收稿时间:2008-02-22
修稿时间:2008-05-14

Molecular diversities and functions of antibacterial peptides from the skins of Ranidae of amphibians
JIN Li-Li,WANG Qiu-Yu. Molecular diversities and functions of antibacterial peptides from the skins of Ranidae of amphibians[J]. Hereditas, 2008, 30(10): 1241-1248. DOI: 10.3724/SP.J.1005.2008.01241
Authors:JIN Li-Li  WANG Qiu-Yu
Affiliation:School of Life Science, Liaoning University, Shenyang 110036, China
Abstract:Abstract: Granular glands in the frog skins of Ranidae of amphibians, a widely distributed group with over 650 spe-cies, synthesize and secrete a remarkably diverse array of peptides with the broad-spectrum antibacterial, antifungal and other biologic activities to protect the organism against a wide range of pathogens, which are believed to have arisen as a result of multiple gene duplication events. Almost without exception, these components are hydrophobic, cationic and form an amphipathic α-helix in a membrane-mimetic solvent. The peptides can be grouped into families on the basis of structural similarity. To date, brevinin-1, esculentin-1, esculentin-2, and temporin peptides, ranalexin, ranatuerin-1, ranatuerin-2 and palustrin, brevinin-2, tigerinin, japonicin, nigrocin and melittin-related peptides have been found in amphibians of Ranidae. In this paper, the molecular diversity, structural feature and the biological ac-tivity of Ranidae antibacterial peptides were reviewed.
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