Effect of the viral proteins on the fluidity of the membrane lipids in Sindbis virus

Sefton, Bartholomew M.; Gaffney, Betty J.

doi:10.1016/0022-2836(74)90378-7

Cited by 92 publications

(33 citation statements)

References 34 publications

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“…PE is known to have a higher gel-fluid phase transition temperature than phosphatidylcholines (PCs) and is likely to convert to s o . For example, the typical monounsaturated PE species, POPE (5) and SOPE (6) Lipid membranes of influenza viruses were previously studied using fluorescent 13,14 and spin labels 10,11 . The early spin label study of influenza virus 12 aimed only at determination of whether the influenza envelope contains a lipid bilayer, but the study detected less 'fluidity' in the influenza membrane than in the erythrocyte membrane.…”

Section: Discussionmentioning

confidence: 99%

“…The influenza virus has played a pivotal role in the development of the raft hypothesis, starting with early studies that inferred ordered domains using spin probes [10][11][12] and fluorescence 13,14 and that suggested that an ordered lipid domain is selected in toto as the envelope during budding from the plasma membrane 15 . These lipids are either selected at the time of budding or pre-selected as the 'pre-envelope' suggested by clusters of the viral envelope protein hemagglutinin seen in immunoelectron microscopy 16 .…”

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confidence: 99%

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Progressive ordering with decreasing temperature of the phospholipids of influenza virus

Polozov¹,

Bezrukov²,

Gawrisch³

et al. 2008

Nat Chem Biol

208

159

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Using linewidth and spinning sideband intensities of lipid hydrocarbon chain resonances in proton magic angle spinning NMR spectra, we detected the temperature-dependent phase state of naturally occurring lipids of intact influenza virus without exogenous probes. Increasingly, below 41 1C ordered and disordered lipid domains coexisted for the viral envelope and extracts thereof. At 22 1C much lipid was in a gel phase, the fraction of which reversibly increased with cholesterol depletion. Diffusion measurements and fluorescence microscopy independently confirmed the existence of gel-phase domains. Thus the existence of ordered regions of lipids in biological membranes is now demonstrated. Above the physiological temperatures of influenza infection, the physical properties of viral envelope lipids, regardless of protein content, were indistinguishable from those of the disordered fraction. Viral fusion appears to be uncorrelated to ordered lipid content. Lipid ordering may contribute to viral stability at lower temperatures, which has recently been found to be critical for airborne transmission.Membranes of most enveloped viruses form by budding out from the plasma membranes of their host cells a highly select subset of plasma membrane components. In general, the selected membrane proteins are coded by the viral genome, whereas lipids are recruited from host membranes; however, the lipid composition of the viral envelope differs from that of the host membrane 1,2 and from other budding viruses 3 . The envelope of influenza contains higher amounts of both cholesterol 1 and glycosphingolipids 4 -lipids known to partition into the liquid ordered (l o ) phase. The l o phase is characterized by extended hydrocarbon chains having a reduced gauche-trans isomerization compared with those of the liquid disordered (l d ) phase, but having a similar rotational and translational mobility 5 . Liquid ordered phases are thought to be at the core of lipid rafts 6 , which are defined as transient membrane microdomains that are enriched in sphingolipids and cholesterol (1) 7 -a hypothesis that has generated much debate 8,9 .The influenza virus has played a pivotal role in the development of the raft hypothesis, starting with early studies that inferred ordered domains using spin probes 10-12 and fluorescence 13,14 and that suggested that an ordered lipid domain is selected in toto as the envelope during budding from the plasma membrane 15 . These lipids are either selected at the time of budding or pre-selected as the 'pre-envelope' suggested by clusters of the viral envelope protein hemagglutinin seen in immunoelectron microscopy 16 .Although detection of virus-sized domains of lipids (B100-nm diameter) is below the limit of resolution of fluorescent microscopy, large micrometer-sized membrane domains are reliably detected [17][18][19] . Recently, proton magic angle spinning NMR ( 1 H MAS NMR) has been used to determine the phase diagram of the same lipid compositions used to study large membrane domains in lipid bilayers and othe...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Progressive ordering with decreasing temperature of the phospholipids of influenza virus

Polozov¹,

Bezrukov²,

Gawrisch³

et al. 2008

Nat Chem Biol

208

159

View full text Add to dashboard Cite

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“…The factors that have been demonstrated to affect the order parameter of the fatty acid spin labels in membranes include lipid composition (4,5), the presence of some membrane proteins (6)(7)(8), anesthetics (26,27), and interaction of membranes and membrane receptors with certain drugs and small molecules (10,11 (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

“…However, the flexibility of lipid chains is not always determined by chemical composition alone, but may also be affected by the presence of proteins in the intact membrane. As an example, the motions of the lipids in Sindbis virus are dominated by the presence of the viral proteins (8). Thus, the question of whether differences in glycoprotein mobility may be correlated with measurable differences in lipid motion can best be answered by measurements of lipid motion in the intact cell membranes.…”

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confidence: 99%

“…(a) The motions of membrane lipids may contribute to an "apparent microviscosity" for motions of those proteins that are free to rotate or diffuse in fluid lipid regions. In this case, the motions of the lipids may be influenced by fatty acid composition (4) and ratios of cholesterol to phospholipid (5) or by the presence of the membrane proteins themselves (6)(7)(8). (b) Lateral phase separations in membranes may include protein as well as lipid components (9).…”

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Fatty acid chain flexibility in the membranes of normal and transformed fibroblasts.

Gaffney¹

1975

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

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Electron Spin Resonance of Biomolecules

Gaffney

2006

Encyclopedia of Molecular Cell Biology and Molecular Medicine

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Basic ESR Concepts and Spectra 3 2 ESR and the Roles of Naturally Occurring Paramagnetic Biomolecules 5 2.1 Free-radical Enzyme Intermediates 5 2.2 Paramagnetic Metal Ions in Biology 6 2.3 Protein Complexes with Nitric Oxide (NO) 8 2.4 Factors Directing Electron Flow in Energetic Membranes 9 2.4.1 ESR Studies of Photosynthesis 9 2.4.2 ESR Studies of Respiratory Enzymes 10 3 ESR Probes of Biological Structure and Function 10 3.1 Spin Labeling 10 3.1.1 Dynamics of Proteins, DNA, and Membranes 10 3.1.2 Site-directed Spin Labeling (SDSL) 11 3.2 Spin Trapping 13 3.3 ESR Imaging 14 3.3.1 ESR Imaging of Oxygen in Tissues 14 3.3.2 ESR Imaging of NO 15 3.4 Long-range Distance (6-60 Å) Measurements by ESR 15 Bibliography 15 Books and Reviews 15 Primary Literature 16

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Effect of the viral proteins on the fluidity of the membrane lipids in Sindbis virus

Cited by 92 publications

References 34 publications

Progressive ordering with decreasing temperature of the phospholipids of influenza virus

Progressive ordering with decreasing temperature of the phospholipids of influenza virus

Fatty acid chain flexibility in the membranes of normal and transformed fibroblasts.

Electron Spin Resonance of Biomolecules

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