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Accessibility of the high-mannose glycans of glycoprotein gp120 from human immunodeficiency virus type 1 probed by in vitro interaction with mannose-binding lectins.
Astoul CH; Peumans WJ; Van Damme EJ; Roug; Institut de Pharmacologie et
October 30, 2000
Biochem Biophys Res Commun. 2000 Aug 2;274(2):455-60. Unique Identifier

The direct interaction of mannose-specific plant lectins with gp120 of HIV-1 was studied by surface plasmon resonance. Inhibition experiments indicated that exposed high mannose type glycans play a key role in the interaction. Most of the lectins specifically accommodate outer alpha1,2-, alpha1,3-, or alpha1,6-linked di- or trimannosides, and especially legume lectins, also interact with the trimannoside core of the complex type glycans. The unexpected affinity of some lectins towards gp120 presumably results from conformational differences in their binding sites. These results demonstrate that mannose-specific plant lectins are powerful tools to study the accessibility and elucidate the function of the gp120 glycans in the recognition and infection of the host cells by HIV-1. Copyright 2000 Academic Press.

JOURNAL ARTICLE Binding Sites Biosensing Techniques Dose-Response Relationship, Drug HIV Envelope Protein gp120/*CHEMISTRY HIV-1/*CHEMISTRY Lectins/*CHEMISTRY/PHARMACOLOGY Mannose/*CHEMISTRY Models, Molecular Polysaccharides/*CHEMISTRY Protein Binding/DRUG EFFECTS/PHYSIOLOGY Substrate Specificity Support, Non-U.S. Gov't Surface Plasmon Resonance

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