Source:http://linkedlifedata.com/resource/pubmed/id/12364551
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
10
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| pubmed:dateCreated |
2002-10-4
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| pubmed:abstractText |
We have analyzed the interaction of adamantyl Gb(3) (adaGb(3)), a semi-synthetic soluble analog of Gb(3), with HIV-1 surface envelope glycoprotein gp120. In this analog, which was orginally designed to inhibit verotoxin binding to its glycolipid receptor, Gb(3), the fatty acid chain is replaced with a rigid globular hydrocarbon frame (adamantane). Despite its solubility, adaGb(3) forms monolayers at an air-water interface. Compression isotherms of such monolayers demonstrated that the adamantane substitution resulted in a larger minimum molecular area and a more rigid, less compressible film than Gb(3). Insertion of gp120 into adaGb(3) monolayers was exponential whereas the gp120/Gb(3) interaction curve was sigmoidal with a lag phase of 40 min. Adding cholesterol into authentic Gb(3) monolayers abrogated the lag phase and increased the initial rate of interaction with gp120. This effect of cholesterol was not observed with phosphatidylcholine or sphingomyelin. In addition, verotoxin-bound adaGb(3) or Gb(3) plus cholesterol was recovered in fractions of comparable low density after ultracentrifugation through sucrose-density gradients in the presence of Triton X-100. The unique biological and physico-chemical properties of adaGb(3) suggest that this analog may be a potent soluble mimic of Gb(3), providing a novel concept for developing GSL-derived viral fusion inhibitors.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adamantane,
http://linkedlifedata.com/resource/pubmed/chemical/Cholesterol,
http://linkedlifedata.com/resource/pubmed/chemical/HIV Envelope Protein gp120,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfoglycosphingolipids,
http://linkedlifedata.com/resource/pubmed/chemical/Trihexosylceramides,
http://linkedlifedata.com/resource/pubmed/chemical/globotriaosylceramide
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| pubmed:status |
MEDLINE
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| pubmed:month |
Oct
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| pubmed:issn |
0022-2275
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
43
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1670-9
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:12364551-Adamantane,
pubmed-meshheading:12364551-Animals,
pubmed-meshheading:12364551-Cattle,
pubmed-meshheading:12364551-Centrifugation, Density Gradient,
pubmed-meshheading:12364551-Cholesterol,
pubmed-meshheading:12364551-Erythrocytes,
pubmed-meshheading:12364551-HIV Envelope Protein gp120,
pubmed-meshheading:12364551-Humans,
pubmed-meshheading:12364551-Lipids,
pubmed-meshheading:12364551-Models, Structural,
pubmed-meshheading:12364551-Pressure,
pubmed-meshheading:12364551-Protein Binding,
pubmed-meshheading:12364551-Protein Structure, Tertiary,
pubmed-meshheading:12364551-Serum Albumin, Bovine,
pubmed-meshheading:12364551-Solubility,
pubmed-meshheading:12364551-Substrate Specificity,
pubmed-meshheading:12364551-Sulfoglycosphingolipids,
pubmed-meshheading:12364551-Surface Tension,
pubmed-meshheading:12364551-Trihexosylceramides
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| pubmed:year |
2002
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| pubmed:articleTitle |
A novel soluble analog of the HIV-1 fusion cofactor, globotriaosylceramide (Gb(3)), eliminates the cholesterol requirement for high affinity gp120/Gb(3) interaction.
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| pubmed:affiliation |
Institut Méditerranéen de Recherche en Nutrition, UMR-INRA 1111, Faculté des Sciences St-Jérôme, 13397 Marseille Cedex 20, France.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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