Cholesterol's interactions with serine phospholipids — A comparison of N-palmitoyl ceramide phosphoserine with dipalmitoyl phosphatidylserine

Sergelius, Christian; Yamaguchi, Seiko; Yamamoto, T.; Engberg, Oskar; Katsumura, Shigeo; Slotte, J. Peter

doi:10.1016/j.bbamem.2012.11.009

Cited by 8 publications

(7 citation statements)

References 55 publications

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“…However, the two-phase GUVs used in the current study are likely to have coexisting gel and liquid phases rather than L o and L d phases. With a gel-toliquid transition temperature over 50°C (55), one study showed that DPPS is dominant in a gel phase in liposomes consisting of POPC, DPPS, and cholesterol, and does not interact with cholesterol favorably (44). Although the system used in that study is different from ours, we also observed that the DiD(Ϫ) phase adopts irregular (not round) shapes that are typical of gel phases (Fig.…”

Section: Discussioncontrasting

confidence: 46%

“…To test whether PS with fully saturated acyl chains also fail to support Gag binding to GUVs, we examined POPCϩDPPSϩchol GUVs for binding of Gag-YFP upon RNase treatment. High-melting-temperature lipids such as DPPS (T m ϭ 54°C) tend to form a tightly packed phase known as the gel phase (42)(43)(44)(45), which can be visually separated from a coexisting liquid phase based on exclusion of a fluid-phase lipid dye. Indeed, when the fluid-phase probe DiD was included in POPCϩDPPSϩchol GUVs, DiD(ϩ) (liquid) and DiD(Ϫ) phases were readily distinguished (Fig.…”

Section: Efficient Binding Of Hiv-1 Gag-yfp To Guvs Requires Treatmenmentioning

confidence: 99%

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Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology Domain

Olety

Veatch

Ono

2015

J Virol

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HIV-1 Gag, which drives virion assembly, interacts with a plasma membrane (PM)-specific phosphoinositide, phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P 2 ]. While cellular acidic phospholipid-binding proteins/domains, such as the PI(4,5)P 2 -specific pleckstrin homology domain of phospholipase C␦1 (PH PLC␦1 ), mediate headgroup-specific interactions with corresponding phospholipids, the exact nature of the Gag-PI(4,5)P 2 interaction remains undetermined. In this study, we used giant unilamellar vesicles (GUVs) to examine how PI(4,5)P 2 with unsaturated or saturated acyl chains affect membrane binding of PH PLC␦ 1 and Gag. Both unsaturated dioleoyl-PI(4,5)P 2 [DO-PI(4,5)P 2 ] and saturated dipalmitoyl-PI(4,5)P 2 [DP-PI(4,5)P 2 ] successfully recruited PH PLC␦ 1 to membranes of single-phase GUVs. In contrast, DO-PI(4,5)P 2 but not DP-PI(4,5)P 2 recruited Gag to GUVs, indicating that PI(4,5)P 2 acyl chains contribute to stable membrane binding of Gag. GUVs containing PI(4,5)P 2 , cholesterol, and dipalmitoyl phosphatidylserine separated into two coexisting phases: one was a liquid phase, and the other appeared to be a phosphatidylserine-enriched gel phase. In these vesicles, the liquid phase recruited PH PLC␦ 1 regardless of PI(4,5)P 2 acyl chains. Likewise, Gag bound to the liquid phase when PI(4,5)P 2 had DO-acyl chains. DP-PI(4,5)P 2 -containing GUVs showed no detectable Gag binding to the liquid phase. Unexpectedly, however, DP-PI(4,5)P 2 still promoted recruitment of Gag, but not PH PLC␦ 1 , to the dipalmitoyl-phosphatidylserine-enriched gel phase of these GUVs. Altogether, these results revealed different roles for PI(4,5)P 2 acyl chains in membrane binding of two PI(4,5)P 2 -binding proteins, Gag and PH PLC␦ 1 . Notably, we observed that nonmyristylated Gag retains the preference for PI(4,5)P 2 containing an unsaturated acyl chain over DP-PI(4,5)P 2 , suggesting that Gag sensitivity to PI(4,5)P 2 acyl chain saturation is determined directly by the matrix-PI(4,5)P 2 interaction, rather than indirectly by a myristate-dependent mechanism. IMPORTANCEBinding of HIV-1 Gag to the plasma membrane is promoted by its interaction with a plasma membrane-localized phospholipid, PI(4,5)P 2 . Many cellular proteins are also recruited to the plasma membrane via PI(4,5)P 2 -interacting domains represented by PH PLC␦ 1 . However, differences and/or similarities between these host proteins and viral Gag protein in the nature of their PI(4,5)P 2 interactions, especially in the context of membrane binding, remain to be determined. Using a novel giant unilamellar vesicle-based system, we found that PI(4,5)P 2 with an unsaturated acyl chain recruited PH PLC␦ 1 and Gag similarly, whereas PI(4,5)P 2 with saturated acyl chains either recruited PH PLC␦ 1 but not Gag or sorted these proteins to different phases of vesicles. To our knowledge, this is the first study to show that PI(4,5)P 2 acyl chains differentially modulate membrane binding of PI(4,5)P 2 -binding proteins. Since Gag membrane binding is essential for progeny...

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Section: Discussioncontrasting

confidence: 46%

Section: Efficient Binding Of Hiv-1 Gag-yfp To Guvs Requires Treatmenmentioning

confidence: 99%

Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology Domain

Olety

Veatch

Ono

2015

J Virol

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“…We also found the SPC lipid family (Figure S1h), which was previously reported only by chemical synthesis . HR MS measurements showed that the major [M – H] − ions at m / z 721.5128 correspond to an elemental composition of C 37 H 74 O 9 N 2 P (calculated m / z : 721.5127), suggesting the presence of the SPC lipid (Table ).…”

Section: Resultssupporting

confidence: 73%

Lipidome of the Bacteroides Genus Containing New Peptidolipid and Sphingolipid Families Revealed by Multiple-Stage Mass Spectrometry

et al. 2023

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The anaerobic bacteria of the Bacteroides fragilis group including Bacteroides thetaiotaomicron, B. fragilis, Bacteroides vulgatus, and Bacteroides ovatus in genus Bacteroides are among the most commonly found human gut microbiota. They are generally commensal but are also opportunistic pathogens. Both the inner and outer membranes of the Bacteroides cell envelope contain abundant lipids with diversified structures, and dissection of the lipid composition of the inner and outer membrane fractions is important for understanding the biogenesis of this multilaminate wall structure. Here, we describe mass spectrometry-based approaches to delineate in detail the lipidome of the membrane and the outer membrane vesicle of the bacteria cells. We identified 15 lipid class/subclasses (>100 molecular species), including sphingolipid families [dihydroceramide (DHC), glycylseryl (GS) DHC, DHC-phosphoinositolphosphoryl-DHC (DHC-PIP-DHC), ethanolamine phosphorylceramide, inositol phosphorylceramide (IPC), serine phosphorylceramide, ceramide-1-phosphate, and glycosyl ceramide], phospholipids [phosphatidylethanolamine, phosphatidylinositol (PI), and phosphatidylserine], peptide lipids (GS-, S-, and G-lipids) and cholesterol sulfate, of which several have not been reported previously, or have similar structures to those found in Porphyromonas gingivalis, the periodontopathic bacterium in oral microbiota. The new DHC-PIPs-DHC lipid family is found only in B. vulgatus, which, however, lacks the PI lipid family. The galactosyl ceramide family is exclusively present in B. fragilis, which nevertheless lacks IPC and PI lipids. The lipidomes as revealed in this study demonstrate the lipid diversity among the various strains and the utility of multiple-stage mass spectrometry (MS n ) with high-resolution mass spectrometry in the structural elucidation of complex lipids.

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“…Cholesterol prefers to interact with saturated acyl chains, and the sphingosine backbone of SM is known to increase bilayer affinity for cholesterol (22). Even in ternary systems, the saturated 1,2-dipalmitoyl-sn-glycero-3-phosphoethanolamine and 1,2-dipalmitoyl-sn-glycero-3-phospho-L-serine or palmitoyl-ceramide-PE and palmitoyl-ceramide-PS were not able to form cholesterol-rich domains in an unsaturated PC bilayer (19,61). Cholesterol partitioning studies have examined unsaturated PE and PS bilayers and concluded that cholesterol affinity to different PLs was in the order PS > PC > PE (27).…”

Section: Discussionmentioning

confidence: 99%

Lipid Interactions and Organization in Complex Bilayer Membranes

Engberg

Yasuda

Hautala

et al. 2016

Biophysical Journal

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Bilayer lipids influence the lateral structure of the membranes, but the relationship between lipid properties and the lateral structure formed is not always understood. Model membrane studies on bilayers containing cholesterol and various phospholipids (PLs) suggest that high and low temperature melting PLs may segregate, especially in the presence of cholesterol. The effect of different PL headgroups on lateral structure of bilayers is also not clear. Here, we have examined the formation of lateral heterogeneity in increasingly complex (up to five-component) multilamellar bilayers. We have used time-resolved fluorescence spectroscopy with domain-selective fluorescent probes (PL-conjugated trans-parinaric acid), and (2)H NMR spectroscopy with site or perdeuterated PLs. We have measured changes in bilayer order using such domain-selective probes both as a function of temperature and composition. Our results from time-resolved fluorescence and (2)H NMR showed that in ternary bilayers, acyl chain order and thermostability in sphingomyelin-rich domains were not affected to any greater extent by the headgroup structure of the monounsaturated PLs (phosphatidylcholine, phosphatidylethanolamine, or phosphatidylserine) in the bilayer. In the complex five-component bilayers, we could not detect major differences between the different monounsaturated PLs regarding cholesterol-induced ordering. However, cholesterol clearly influenced deuterated N-palmitoyl sphingomyelin differently than the other deuterated PLs, suggesting that cholesterol favored N-palmitoyl sphingomyelin over the other PLs. Taken together, both the fluorescence spectroscopy and (2)H NMR data suggest that the complex five-component membranes displayed lateral heterogeneity, at least in the lower temperature regimen examined.

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Cholesterol's interactions with serine phospholipids — A comparison of N-palmitoyl ceramide phosphoserine with dipalmitoyl phosphatidylserine

Cited by 8 publications

References 55 publications

Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology Domain

Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology Domain

Lipidome of the Bacteroides Genus Containing New Peptidolipid and Sphingolipid Families Revealed by Multiple-Stage Mass Spectrometry

Lipid Interactions and Organization in Complex Bilayer Membranes

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