Gp120 binds cooperatively to several biologically relevant glycosphingolipids

Quantitative measurements at equilibrium by total internal reflection fluorescence microscopy

John C. Conboy, Katherine D. McReynolds, Jacquelyn Gervay-Hague, S. Scott Saavedra

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The binding of The HIV-1 surface glycoprotein gp120 to several glycosphingolipides, reconstituted into planar lipid bilayers (see scheme; small circle= 2-oleoyl-1-palmitoylphosphatidylcholine (POPC), arrow = glycosylceramide recognition element; left: low and right: high protein concentrations), has been quantitatively measured under quilibrium conditions. Complex binding behavior was observed, which suggests that the induced aggregation of gp120 molecules at a ligand-bearing membrane surface may be an important step in the mechanism of HIV-1 infection of a host cell.

Original languageEnglish (US)
Pages (from-to)2882-2884
Number of pages3
JournalAngewandte Chemie - International Edition
Volume39
Issue number16
DOIs
StatePublished - Aug 18 2000
Externally publishedYes

Fingerprint

Bearings (structural)
Glycosphingolipids
Lipid bilayers
Fluorescence microscopy
Membrane Glycoproteins
Agglomeration
Ligands
Membranes
Glycoproteins
Molecules
Proteins
1-oleoyl-2-palmitoylphosphatidylcholine

Keywords

  • Fluorescence spectroscopy
  • Glycolipids
  • Structure-activity relationships

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Gp120 binds cooperatively to several biologically relevant glycosphingolipids : Quantitative measurements at equilibrium by total internal reflection fluorescence microscopy. / Conboy, John C.; McReynolds, Katherine D.; Gervay-Hague, Jacquelyn; Saavedra, S. Scott.

In: Angewandte Chemie - International Edition, Vol. 39, No. 16, 18.08.2000, p. 2882-2884.

Research output: Contribution to journalArticle

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