Lipopolysaccharide induces amyloid formation of antimicrobial peptide HAL-2
Lipopolysaccharide induces amyloid formation of antimicrobial peptide HAL-2
复制标题
脂多糖诱导抗菌肽 HAL-2 淀粉样蛋白形成
DOI：
10.1016/j.bbamem.2014.07.028
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发表时间：
2014-11-01
影响因子：
3.4
通讯作者：
Wang, Junfeng
中科院分区：
文献类型：
--
作者：
Wang, Jiarong;Li, Yan;Wang, Junfeng
内毒素是革兰氏阴性菌外膜的重要组成部分，有助于维持外膜的完整性，保护细胞免受包括抗菌肽在内的杀菌剂的侵袭。然而，抗菌肽与内毒素相互作用的机制尚不清楚。Halictines-2(Halictines-2，HAL-2)是从蜜蜂Halictus sexinctus的毒液中分离得到的一种新型抗菌肽。HAL-2对革兰氏阳性和革兰氏阴性细菌，甚至对癌细胞都表现出了很强的抗菌活性。在此，我们研究了HAL-2与脂多糖的相互作用，以阐明HAL-2的体外抗菌机制。我们的结果表明，在内毒素存在的情况下，HAL-2具有明显的β-链结构。脂多糖能够诱导HAL-2淀粉样蛋白的形成，这可能在其抗菌活性中发挥重要作用。(C)2014爱思唯尔B.V.保留所有权利。
Lipopolysaccharide (LPS), the important component of the outer membrane of Gram-negative bacteria, contributes to the integrity of the outer membrane and protects the cell against bactericidal agents, including antimicrobial peptides. However, the mechanisms of interaction between antimicrobial peptides and LPS are not clearly understood. Halictines-2 (HAL-2), one of the novel antimicrobial peptides, was isolated from the venom of the eusocial bee Halictus sexcinctus. HAL-2 has exhibited potent antimicrobial activity against Gram-positive and Gram-negative bacteria and even against cancer cells. Here, we studied the interactions between HAL-2 and LPS to elucidate the antibacterial mechanism of HAL-2 in vitro. Our results show that HAL-2 adopts a significant degree of beta-strand structure in the presence of LPS. LPS is capable of inducing HAL-2 amyloid formation, which may play a vital role in its antimicrobial activity. (C) 2014 Elsevier B.V. All rights reserved.