|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
2003-4-1
|
|
pubmed:abstractText |
Equinatoxin II (EqtII), a protein toxin from the sea anemone Actinia equina, readily creates pores in sphingomyelin-containing lipid membranes. The perturbation by EqtII of model lipid membranes composed of dimyristoylphosphatidycholine and sphingomyelin (10 mol %) was investigated using wideline phosphorus-31 and deuterium NMR. The preferential interaction between EqtII (0.1 and 0.4 mol %) and the individual bilayer lipids was studied by (31)P magic angle spinning NMR, and toxin-induced changes in bilayer morphology were examined by freeze-fracture electron microscopy. Both NMR and EM showed the formation of an additional lipid phase in sphingomyelin-containing mixed lipid multilamellar suspensions with 0.4 mol % EqtII. The new toxin-induced phase consisted of small unilamellar vesicles 20-40 nm in diameter. Deuterium NMR showed that the new lipid phase contains both dimyristoylphosphatidycholine and sphingomyelin. Solid-state (31)P NMR showed an increase in spin-lattice and a decrease in spin-spin relaxation times in mixed-lipid model membranes in the presence of EqtII, consistent with an increase in the intensity of low frequency motions. The (2)H and (31)P spectral intensity distributions confirmed a change in lipid mobility and showed the creation of an isotropic lipid phase, which was identified as the small vesicle structures visible by electron microscopy in the EqtII-lipid suspensions. The toxin appears to enhance slow motions in the membrane lipids and destabilize the membrane. This effect was greatly enhanced in sphingomyelin-containing mixed lipid membranes compared with pure phosphatidylcholine bilayers, suggesting a preferential interaction between the toxin and bilayer sphingomyelin.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-10429196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-10590307,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-10930518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-10985788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11023904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11076935,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11142519,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11222295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11371451,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11509361,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11525171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11689232,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-11827489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-1348018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-1420892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-1757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-1973096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-1981789,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-2187536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-2463153,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-2903587,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-335428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-3427188,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-356883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-38841,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-6106065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-656398,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-6871211,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7126566,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7317355,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7488111,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7512761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7679444,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7912550,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-7984032,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-8117706,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-8529661,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-8639486,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-8645323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-8744310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-8942660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-9002522,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-9266180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-9357951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-9804997,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12668447-9837740
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
0006-3495
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
84
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2382-92
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:12668447-Cnidarian Venoms,
pubmed-meshheading:12668447-Dimyristoylphosphatidylcholine,
pubmed-meshheading:12668447-Lipid Bilayers,
pubmed-meshheading:12668447-Magnetic Resonance Spectroscopy,
pubmed-meshheading:12668447-Membrane Fluidity,
pubmed-meshheading:12668447-Microscopy, Electron,
pubmed-meshheading:12668447-Molecular Conformation,
pubmed-meshheading:12668447-Permeability,
pubmed-meshheading:12668447-Porosity,
pubmed-meshheading:12668447-Sphingomyelins,
pubmed-meshheading:12668447-Structure-Activity Relationship
|
|
pubmed:year |
2003
|
|
pubmed:articleTitle |
Effects of the eukaryotic pore-forming cytolysin Equinatoxin II on lipid membranes and the role of sphingomyelin.
|
|
pubmed:affiliation |
Biomembrane Structure Unit, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
