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昆虫毒液肽作为有效的大肠杆菌 ATP 合酶抑制剂。

Insect venom peptides as potent inhibitors of Escherichia coli ATP synthase.

机构信息

Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO 63501, USA.

Department of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO 63501, USA.

出版信息

Int J Biol Macromol. 2020 May 1;150:23-30. doi: 10.1016/j.ijbiomac.2020.02.046. Epub 2020 Feb 6.

DOI:10.1016/j.ijbiomac.2020.02.046
PMID:32035966
Abstract

Insect venom peptides (IVPs) eumenitin, lasiocepsin, lycosin1, mastoparanB, panurgine1, and protonectin possess antibacterial properties, and the ubiquitous enzyme ATP synthase has a peptide-binding site. In the present study, we studied the effect of IVPs on binding and inhibition of three Escherichia coli strains (wild type, mutant, and null) and isolated E. coli ATP synthase. IVPs and their C-terminal amide (-NH) analogs caused variable inhibition of membrane-bound FF ATP synthase. While wild type E. coli growth was substantially hampered, null E. coli growth was near normal in the presence of IVPs and their C-terminal-NH analogs. The presence of C-terminal-NH groups on IVPs resulted in increased inhibition of ATP synthase and reduced growth of E. coli strains. Insignificant inhibition of the βDELSEED-motif mutant enzyme with the βAAAAAAA-motif confirmed that IVPs interact with the βDELSEED-motif, also known as the peptide-binding site. The higher level of growth loss in E. coli strains by eumenitin, lasiocepsin, lycosin1, mastoparanB, panurgine1, and protonectin and their C-terminal-NH analogs suggested the likelihood of additional cellular or molecular targets. IVPs caused inhibition of E. coli strains, which demonstrates an association between antimicrobial traits of IVPs and bacterial ATP synthase.

摘要

昆虫毒液肽 (IVP) eumenitin、lasiocepsin、lycosin1、mastoparanB、panurgine1 和 protonectin 具有抗菌特性,而普遍存在的酶 ATP 合酶具有肽结合位点。在本研究中,我们研究了 IVP 对三种大肠杆菌菌株(野生型、突变型和缺失型)结合和抑制的影响,并分离了大肠杆菌 ATP 合酶。IVP 及其 C 末端酰胺 (-NH) 类似物对膜结合 FF ATP 合酶的抑制作用不同。虽然野生型大肠杆菌的生长受到严重阻碍,但在 IVP 及其 C 末端-NH 类似物存在的情况下,缺失型大肠杆菌的生长几乎正常。IVP 上 C 末端-NH 基团的存在导致 ATP 合酶的抑制增加和大肠杆菌菌株的生长减少。具有 βAAAAAAA 基序的 βDELSEED 基序突变酶的抑制作用不明显,证实 IVP 与 βDELSEED 基序(也称为肽结合位点)相互作用。eumenitin、lasiocepsin、lycosin1、mastoparanB、panurgine1 和 protonectin 及其 C 末端-NH 类似物在大肠杆菌菌株中引起更高水平的生长损失,这表明可能存在其他细胞或分子靶标。IVP 引起大肠杆菌菌株的抑制作用,这表明 IVP 的抗菌特性与细菌 ATP 合酶之间存在关联。

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