Volume 39, Issue 16 pp. 2882-2884

Communication

Gp120 Binds Cooperatively to Several Biologically Relevant Glycosphingolipids: Quantitative Measurements at Equilibrium by Total Internal Reflection Fluorescence Microscopy

John C. Conboy Dr.,

John C. Conboy Dr.

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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Katherine D. McReynolds Dr.,

Katherine D. McReynolds Dr.

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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Jacquelyn Gervay-Hague Prof. Dr.,

Jacquelyn Gervay-Hague Prof. Dr.

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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S. Scott Saavedra Prof. Dr.,

S. Scott Saavedra Prof. Dr.

[email protected]

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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John C. Conboy Dr.,

John C. Conboy Dr.

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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Katherine D. McReynolds Dr.,

Katherine D. McReynolds Dr.

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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Jacquelyn Gervay-Hague Prof. Dr.,

Jacquelyn Gervay-Hague Prof. Dr.

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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S. Scott Saavedra Prof. Dr.,

S. Scott Saavedra Prof. Dr.

[email protected]

Department of Chemistry University of Arizona Tucson, AZ 85721-0041 (USA) Fax: (+1) 520-621-8407

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First published: 11 August 2000

https://doi.org/10.1002/1521-3773(20000818)39:16<2882::AID-ANIE2882>3.0.CO;2-M

Citations: 16

This research was supported by the NIH (AI40359-02), the NSF (CHE-9726132 and CHE-9623583), Eli Lilly (JGH), and the Alfred P. Sloan Foundation (J.G.H.). K.D.M. gratefully acknowledges receipt of the University of Arizona Dean's Fellowship and the Department of Chemistry Carl S. Marvel Fellowship. We thank Ying-Mei Gu for performing the streptavidin adsorption measurements.

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Abstract

The binding of the HIV-1 surface glycoprotein gp120 to several glycosphingolipids, 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 equilibrium 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.

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Volume39, Issue16

August 18, 2000

Pages 2882-2884

Gp120 Binds Cooperatively to Several Biologically Relevant Glycosphingolipids: Quantitative Measurements at Equilibrium by Total Internal Reflection Fluorescence Microscopy

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Gp120 Binds Cooperatively to Several Biologically Relevant Glycosphingolipids: Quantitative Measurements at Equilibrium by Total Internal Reflection Fluorescence Microscopy

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