Echinococcus granulosus antigen B hydrophobic ligand binding properties

Gustavo Chemale, John Barrett, A. Zaha, Henrique B. Ferreira, Peter M. Brophy

Research output: Contribution to journalArticlepeer-review

50 Citations (SciVal)

Abstract

Antigen B (AgB), an immunodominant component of the cestode parasite Echinococcus granulosus, presents homology to and shares apparent structural similarities with helix-rich hydrophobic ligand binding proteins (HLBPs) from other cestodes. In order to investigate the fatty acid binding properties of AgB, two of its subunit components (rAgB8/1 and rAgB8/2) were expressed in Escherichia coli and purified, and the native antigen was purified from the hydatid cyst fluid by affinity chromatography using a monoclonal antibody raised against rAgB8/1. The interaction of the purified native and recombinant proteins with the fluorescent ligands DAUDA, ANS, DACA and 16-AP was investigated. The palmitic acid derived fluorescent ligand, 16-AP, showed the greatest enhancement in fluorescence when bound to native AgB or to its recombinant subunits, and the dissociation constants for 16-AP binding were determined. Surprisingly, in contrast to HLBPs from other cestodes, interactions with other fatty acids, including palmitic acid, caused an increase in fluorescence instead of competing with 16-AP. Our results suggest that AgB might have evolved different functions in the binding of hydrophobic compounds, dependent on cestode environment.
Original languageEnglish
Pages (from-to)189-194
Number of pages6
JournalBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
DOIs
Publication statusPublished - 14 Mar 2005

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