Hydration and Localization of Diacylglycerol in the Insect Lipoprotein Lipophorin. A 13C-NMR Study

Jl, Soulages; Rivera, Madison E.; Fa, Walker; Ma, Wells

doi:10.1021/bi00177a015

Cited by 20 publications

(13 citation statements)

References 20 publications

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“…A signal at d 179.8 in the 13 C NMR spectrum indicated the presence of acidic carbonyl function. Based on these data and those reported by Kawahara et al (2000) and Soulages et al (1994), we concluded that the isolated antifouling compound was 2-hydroxymyristic acid (HAB) (Fig. 1).…”

Section: Identification Of Antifouling Compoundssupporting

confidence: 70%

Isolation of antifouling compounds from the marine bacterium, Shewanella oneidensis SCH0402

Bhattarai

Ganti

Paudel

et al. 2006

World J Microbiol Biotechnol

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Two compounds, 2-hydroxymyristic acid (HMA) and cis-9-oleic acid (COA), were isolated from a chloroform extract of the marine bacterium, Shewanella oneidensis SCH0402. In a spectrophotometerbased chemotaxis assay, HMA completely eliminated the optical density (OD) of Alteromonas marina SCH0401 and Bacillus atrophaeus SCH0408, motile, fouling bacteria, at 100 and 1000 lg ml -1 , respectively. COA similarly decreased the OD of A. marina and B. atrophaeus by 100% at 1000 lg ml -1 . The commercially available, highly toxic anti-fouling compound, tributyltin oxide (TBTO) never reduced the OD of the target bacteria by 100% even at higher concentration. Instead, all the test bacterial cells were killed at higher than 1000 lg ml -1 of concentration. Both HMA and COA inhibited germination of Ulva pertusa spores completely at 10 and 100 lg ml -1 , respectively, while TBTO inhibited germination at 0.01 lg ml -1 . However, in field assays, both HMA and COA showed antifouling activities as potent as TBTO against a wide range of fouling organisms, including micro-and macro-algae, barnacles, and mussels. The average fouling coverage on the surface of the control panel was 93 ± 6% after 1.5 years but no fouling was observed on the surface of the test panel onto which each compound was applied separately. Thus, bacterial repellent compounds can be used as substitutes for potent toxic anti-fouling compounds, resulting in higher standards of environmental safety without loss of anti-fouling performance.

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Section: Identification Of Antifouling Compoundssupporting

confidence: 70%

Isolation of antifouling compounds from the marine bacterium, Shewanella oneidensis SCH0402

Bhattarai

Ganti

Paudel

et al. 2006

World J Microbiol Biotechnol

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“…Previous in vitro studies showed that, in some model systems, apoLp-III binds to PC or other phospholipids (26,(32)(33)(34). However, apoLp-III does not bind to lipoprotein particles whose surface appears to be covered almost exclusively by phospholipid (4,35,36). The presence of DG on the lipoprotein surface seems to be necessary to trigger the binding of apoLp-III.…”

Section: Discussionmentioning

confidence: 98%

Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: a surface plasmon resonance spectroscopy study.

Soulages

Salamon

Wells

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The binding of the exchangeable apolipoprotein apolipophorin III (apoLp-III) to an egg phosphatidylcholine bilayer as a function of the concentration of diacylglycerol (DG) in the bilayer was studied by surface plasmon resonance spectroscopy. At a DG concentration of 2 mol % in the bilayer, the binding of apoLp-III reached saturation. Under saturating conditions, apoLp-III forms a closely packed monolayer -55 A thick, in which each molecule of protein occupies -500 A2 at the membrane surface. These dimensions are consistent with the molecular size of the apoLp-III molecule determined by x-ray crystallography, if apoLp-III binds to the bilayer with the long axis of the apoLp-III normal to the membrane surface. In the absence of protein, the overall structure of the lipid bilayer was not significantly changed up to 2.5 mol % DG. However, at 4 and 6 mol % DG, the presence of nonbilayer structures was observed. The addition of apoLp-III to a membrane containing 6 mol % DG promoted the formation of large lipid-protein complexes. These data support a two-step sequential binding mechanism for binding of apoLp-III to a lipid surface. The first step is a recognition process, consisting of the adsorption of apoLp-III to a nascent hydrophobic defect in the phospholipid bilayer caused by the presence of DG. This recognition process might depend on the presence of a hydrophobic sensor located at one of the ends of the long axis of the apoLp-III molecule but would be consolidated through Hbond and electrostatic interactions. Once primary binding is achieved, subsequent enlargement of the hydrophobic defect in the lipid surface would trigger the unfolding of the apolipoprotein and binding via the amphipathic a-helices. This two-step sequential binding mechanism could be a general mechanism for all exchangeable apolipoproteins. A possible physiological role of the ability of apoLp-III to bind to lipid structures in two orientations is also proposed.Lipophorin is the main lipoprotein found in the hemolymph of insects; it transports phospholipid, diacylglycerol (DG), and hydrocarbons among insect tissues. The lipophorin particle contains between 35% and 65% (weight %) lipid and two nonexchangeable apolipoprotein molecules-one apolipophorin I molecule of -250 kDa and one apolipophorin II molecule of "80 kDa (1-5). In those lipophorin particles containing >35% lipid, which is mainly due to an increase in the DG content, a third molecule, the exchangeable apolipoprotein apolipophorin III (apoLp-III; 18 kDa), is also found. The number of molecules of apoLp-III bound to the lipophorin is related to the DG content and varies between 0 and at least 16 molecules. The interaction of apoLp-III with lipid is of interest for several reasons. (i) apoLp-11I plays an essential role in the transport of large amounts of DG, which is the major source of energy for flight in many insects (1-5).(ii) apoLp-III is the only full-length exchangeable apolipopro-The publication costs of this article were defrayed in part by page charge payment....

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“…Insect Lps may function as reusable shuttles for lipid transport (Blacklock and Ryan, 1994;Soulages et al, 1994;Arrese et al, 2001;van der Horst et al, 2002). For example, Lp complexes transfer diacylglycerols to flight muscles and the protein can be recycled back to the hemolymph.…”

Section: Introductionmentioning

confidence: 99%

Anopheles gambiae lipophorin: Characterization and role in lipid transport to developing oocyte

Atella

Silva-Neto

Golodne

et al. 2006

Insect Biochemistry and Molecular Biology

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Hydration and Localization of Diacylglycerol in the Insect Lipoprotein Lipophorin. A 13C-NMR Study

Cited by 20 publications

References 20 publications

Isolation of antifouling compounds from the marine bacterium, Shewanella oneidensis SCH0402

Isolation of antifouling compounds from the marine bacterium, Shewanella oneidensis SCH0402

Low concentrations of diacylglycerol promote the binding of apolipophorin III to a phospholipid bilayer: a surface plasmon resonance spectroscopy study.

Anopheles gambiae lipophorin: Characterization and role in lipid transport to developing oocyte

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