Antimicrobial peptides in insects; structure and function

Antimicrobial peptides in insects; structure and function
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DOI:
10.1016/s0145-305x(99)00015-4
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发表时间:
1999-06-01
影响因子:
2.9
通讯作者:
Hoffmann, D
Hoffmann, D
中科院分区:
生物学3区
文献类型:
--
作者:
Bulet, P;Hetru, C;Hoffmann, D

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抗菌肽是原核生物和真核生物天然免疫防御系统中普遍存在的多能成分。在过去的15年中,大量的这些肽已被分离出来,主要是从昆虫。尽管在大小、氨基酸组成和结构上存在很大差异,但大多数昆虫抗菌肽可分为三类之一,数量最多的一类含有分子内二硫键形成发夹样β-折叠或α-螺旋-β-折叠混合结构的肽。第二个最重要的基团由形成两亲性α-螺旋的肽组成。第三组包含脯氨酸和/或甘氨酸残基过量的肽。一般而言,昆虫抗微生物肽具有广泛的活性并且没有细胞毒性。尽管有大量关于其抗微生物活性的结构要求的信息。这些肽的作用方式尚未完全了解。然而,一些数据表明存在两种类型的作用模式:1。通过肽-脂质相互作用或2.通过受体介导的识别过程,本文综述了近四年来昆虫抗菌肽的研究进展,重点介绍了富含脯氨酸和半胱氨酸的昆虫抗菌肽。(C)1999 Elsevier Science Ltd.保留所有权利。
Antimicrobial peptides appear to be ubiquitous and multipotent components of the innate immune defense arsenal used by both prokaryotic and eukaryotic organisms. During the past 15 years a multitude of these peptides have been isolated largely from insects. In spite of great differences in size, amino acid composition and structure, most of the antimicrobial peptides from insects can be grouped into one of three categories, The largest category in number contains peptides with intramolecular disulfide bonds forming hairpin-like beta-sheets or alpha-helical-beta-sheet mixed structures. The second most important group is composed of peptides forming amphipathic alpha-helices. The third group comprises peptides with an overrepresentation in proline and/or glycine residues. In general, the insect antimicrobial peptides have a broad range of activity and are not cytotoxic. Despite a wealth of information on structural requirements for their antimicrobial activity. the mode of action of these peptides is not yet fully understood. However, some data suggest the existence of two types of mode of action:1. through peptide-lipid interaction or2. through receptor-mediated recognition processes.This review presents the main results obtained during the last four years in the field of antimicrobial peptides from insects with a special focus on the proline-rich and cysteine-rich peptides. (C) 1999 Elsevier Science Ltd. All rights reserved.