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Burkholderia Oklahomensis Agglutinin Is a Canonical Two-Domain OAA-family Lectin: Structures, Carbohydrate Binding and anti-HIV Activity

Burkholderia Oklahomensis Agglutinin Is a Canonical Two-Domain OAA-family Lectin: Structures, Carbohydrate Binding and anti-HIV Activity

Matthew J Whitley, William Furey, Sireesha Kollipara, Angela M Gronenborn

FEBS J. 2013 May;280(9):2056-67.

PMID: 23480609

Abstract:

Burkholderia oklahomensis EO147 agglutinin (BOA) is a 29 kDa member of the Oscillatoria agardhii agglutinin (OAA) family of lectins. Members of the OAA family recognize high-mannose glycans, and, by binding to the HIV envelope glycoprotein 120 (gp120), block the virus from binding to and entering the host cell, thereby inhibiting infection. OAA-family lectins comprise either one or two homologous domains, with a single domain possessing two glycan binding sites. We solved the structure of BOA in the ligand-free form as well as in complex with four molecules of 3α,6α-mannopentaose, the core unit of the N-linked high-mannose structures found on gp120 in vivo. This is the first structure of a double-domain OAA-family lectin in which all four binding sites are occupied by ligand. The structural details of the BOA-glycan interactions presented here, together with determination of affinity constants and HIV inactivation data, shed further light onto the structure-function relationship in this important class of anti-HIV proteins.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP112828690	3α,6α-Mannopentaose		112828-69-0	Price

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