LL-37 和 HNP1 的协同作用保护哺乳动物细胞膜免于溶解。
Cooperative Function of LL-37 and HNP1 Protects Mammalian Cell Membranes from Lysis.
机构信息
Department of Physical Chemistry, University of Geneva, Geneva, Switzerland.
Institute of Industrial Science, The University of Tokyo, Tokyo, Japan; Department of Physical Chemistry, University of Geneva, Geneva, Switzerland.
出版信息
Biophys J. 2020 Dec 15;119(12):2440-2450. doi: 10.1016/j.bpj.2020.10.031. Epub 2020 Nov 4.
Abstract
LL-37, cleaved from human cathelicidin, and human neutrophil peptide-1 (HNP1) from the defensin family are antimicrobial peptides that are occasionally co-released from neutrophils, which synergistically kill bacteria. We report that this couple presents another type of cooperativity against host eukaryotic cells, in which they antagonistically minimize cytotoxicity by protecting membranes from lysis. Our results describe the potential of the LL-37/HNP1 cooperativity that switches from membrane-destructive to membrane-protective functions, depending on whether the target is an enemy or a host.
摘要
LL-37 是人源杀菌肽和防御素家族的人中性粒细胞肽-1 的前体，是偶尔从嗜中性粒细胞中共同释放出来的抗菌肽，它们协同杀死细菌。我们报告说，这对物质针对宿主真核细胞呈现出另一种类型的协同作用，通过保护细胞膜免于裂解，它们拮抗地最小化细胞毒性。我们的结果描述了 LL-37/HNP1 协同作用的潜力，该协同作用根据目标是敌人还是宿主，从破坏膜的功能转换为保护膜的功能。
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