期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS
卷 1861, 期 7, 页码 617-629出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbalip.2016.04.011
关键词
Membrane phospholipids; Phosphatidylcholine; Apolipophorin III; Fourier transform infrared spectroscopy; Fluorescence lifetime imaging microscopy
资金
- Ministry of Science and Higher Education (Poland) [N N303 822640]
- Foundation for Polish Science within the TEAM programme [TEAM/2011-7/2]
- European Regional Development Fund in the framework of the Development of Eastern Poland Operational Programme
- Ministry of Science and Higher Education, Warsaw, Poland
- European Union [POIG.02.01.00-12-064/08]
- National Science Center (Krakow, Poland) [UMO-2013/11/B/NZ6/00409]
Apolipophorin III (apoLp-III), an insect homologue of human apolipoprotein E (apoE), is a widely used model protein in studies on protein lipid interactions, and anti-Legionella activity of Galleria mellonella apoLp-III has been documented. Interestingly, exogenous choline-cultured Legionella dumoffii cells are considerably more susceptible to apoLp-III than non-supplemented bacteria. In order to explain these differences, we performed, for the first time, a detailed analysis of L. dumoffii lipids and a comparative lipidomic analysis of membranes of bacteria grown without and in the presence of exogenous choline. P-31 NMR analysis of L. dumoffii phospholipids (PLs) revealed a considerable increase in the phosphatidylcholine (PC) content in bacteria cultured on choline medium and a decrease in the phosphatidylethanolamine (PE) content in approximately the same range. The interactions of G. mellonella apoLp-III with lipid bilayer membranes prepared from PLs extracted from non and choline-supplemented L dumoffii cells were examined in detail by means of attenuated total reflection and linear dichroism-Fourier transform infrared spectroscopy. Furthermore, the kinetics of apoLp-III binding to liposomes formed from L. dumoffii PLs was analysed by fluorescence correlation spectroscopy and fluorescence lifetime imaging microscopy using fluorescently labelled G. mellonella apoLp-III. Our results indicated enhanced binding of apoLp-III to and deeper penetration into lipid membranes formed from PLs extracted from the choline-supplemented bacteria, i.e. characterized by an increased PC/PE ratio. This could explain, at least in part, the higher susceptibility of choline-cultured L. dumoffii to G. mellonella apoLp-III. (C) 2016 Elsevier B.V. All rights reserved.
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