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ShAR2β, a divergent nicotinic acetylcholine receptor subunit from the blood fluke Schistosoma

Published online by Cambridge University Press:  11 January 2007

G. N. BENTLEY
Affiliation:
The School of Biology, University of Leeds, West Yorkshire, Leeds, LS2 9JT, UK
A. K. JONES*
Affiliation:
MRC Functional Genetics Unit, Department of Physiology, Anatomy and Genetics, Le Gros Clark Building, University of Oxford, South Parks Road, Oxford OX1 3QX, UK
A. AGNEW
Affiliation:
The School of Biology, University of Leeds, West Yorkshire, Leeds, LS2 9JT, UK
*
*Corresponding author: MRC Functional Genetics Unit, Department of Physiology, Anatomy and Genetics, Le Gros Clark Building, University of Oxford, South Parks Road, Oxford OX1 3QX, UK. Tel: +44 1865 272196. Fax: +44 1865 282651. E-mail: andrew.jones@anat.ox.ac.uk

Summary

Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels that mediate the fast actions of the neurotransmitter, acetylcholine. Invertebrate nAChRs are of interest as they are targets of widely-selling insecticides and drugs that control nematode parasites. Here, we report the cloning of ShAR2β, a candidate nAChR subunit from the blood fluke, Schistosoma haematobium, which is the third trematode nAChR subunit to be characterized. While ShAR2β possesses key structural features common to all nAChRs, its amino acid sequence shares considerably low identity with those of insect, nematode and vertebrate nAChR subunits. In particular, the second transmembrane domain of ShAR2β, which lines the ion channel, bears unusual amino acid residues which will likely give rise to a receptor with distinct functional properties. Phylogenetic analysis shows that ShAR2β is a divergent nAChR subunit that may define a clade of trematode-specific subunits. We discuss our findings in the context of potentially exploiting this receptor as a target for controlling schistosome parasites.

Type
Research Article
Copyright
Copyright © Cambridge University Press 2007

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