文献类型：期刊文献

英文题名：Negatively charged phospholipids accelerate the membrane fusion activity of the plant-specific insert domain of an aspartic protease

作者：Zhao, Xiaoli[1,2,6]; Ma, Xiaomin[3]; Dupius, John H.[4]; Qi, Ruxi[3]; Tian, Jenny[4]; Chen, Jiaxin[1]; Ou, Xiuyuan[5]; Qian, Zhaohui[5]; Liang, Dehai[1]; Wang, Peiyi[3]; Yada, Rickey Y.[4]; Wang, Shenlin[1,2,6]

机构：[1] College of chemistry and molecular engineering, Beijing NMR center, Peking University, Beijing, 100871, China; [2] State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Shanghai, 200237, China; [3] Cryo-EM center, Southern University of Science and Technology, Shenzhen, 518055, China; [4] Food Nutrition and Health Program, Faculty of Land and Food Systems, the University of British Columbia, Vancouver, BC, Canada; [5] MOH Key Laboratory, Institute of Pathogen Biology, Chinese Academy of Medical Science, Beijing, China; [6] Beijing National Laboratory for Molecular Sciences, Beijing, China

年份：2022

卷号：298

期号：1

外文期刊名：Journal of Biological Chemistry

收录：EI(收录号：20220111422475)

语种：英文

外文关键词：Phospholipids - Plants (botany) - Nuclear magnetic resonance spectroscopy - Cell membranes - Liposomes

摘要：Various plants use antimicrobial proteins/peptides as a means to resist phytopathogens. In the potato, Solanum tuberosum, the plant-specific insert (PSI) domain of an aspartic protease performs this role by disrupting phytopathogen plasma membranes. However, the mechanism by which PSI selects target membranes has not been elucidated. Here, we studied PSI-induced membrane fusion, focusing on the effects of lipid composition on fusion efficiency. Membrane fusion by the PSI involves an intermediate state whereby adjacent liposomes share their bilayers. We found that increasing the concentration of negatively charged phosphatidylserine (PS) phospholipids substantially accelerated PSI-mediated membrane fusion. NMR data demonstrated that PS did not affect the binding between the PSI and liposomes, but had seminal effects on the dynamics of PSI interaction with liposomes. In PS-free liposomes, the PSI underwent significant motion, which was suppressed on PS-contained liposomes. Molecular dynamics simulations showed that the PSI binds to PS-containing membranes with a dominant angle ranging from -31° to 30°, with respect to the bilayer, and is also present closer to the membrane surfaces. In contrast, PSI is mobile and exhibits multiple topological states on the surface of PS-free membranes. Taken together, our data suggested that PS lipids limit the motion of the anchored PSI, bringing it closer to the membrane surface and efficiently bridging different liposomes to accelerate fusion. As most phytopathogens have a higher content of negatively charged lipids as compared to host cells, these results indicate that the PSI selectively targets negatively charged lipids, which likely represents a way of distinguishing the pathogen from the host. ? 2022 American Society for Biochemistry and Molecular Biology Inc.. All rights reserved.