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A tryptophan amphiphilic tetramerization domain-containing acetylcholinesterase from the bovine lungworm, Dictyocaulus viviparus

Published online by Cambridge University Press:  24 May 2006

J. B. MATTHEWS ,
O. LAZARI ,
A. J. DAVIDSON ,
S. WARREN  and
M. E. SELKIRK
J. B. MATTHEWS
Affiliation:
Division of Parasitology, Moredun Research Institute, Pentlands Science Park, Edinburgh EH26 0PZ
O. LAZARI
Affiliation:
Veterinary Medicine Biology, Pfizer Animal Health, Sandwich, Kent CT13 9NJ
A. J. DAVIDSON
Affiliation:
Division of Parasitology, Moredun Research Institute, Pentlands Science Park, Edinburgh EH26 0PZ
S. WARREN
Affiliation:
Division of Parasitology, Moredun Research Institute, Pentlands Science Park, Edinburgh EH26 0PZ
M. E. SELKIRK
Affiliation:
Division of Cell and Molecular Biology, Imperial College London, London SW7 2AZ
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Abstract

Acetylcholine (ACh) is one of an array of neurotransmitters used by invertebrates and, analogous to vertebrate nervous systems, acetylcholinesterase (AChE) regulates synaptic levels of this transmitter. Similar to other invertebrates, nematodes possess several AChE genes. This is in contrast to vertebrates, which have a single AChE gene, transcripts of which are alternatively spliced to produce different types of the enzyme which vary at their C-termini. Parasitic nematodes have a repertoire of AChE genes which include those encoding neuromuscular AChEs and those genes which code for secreted AChEs. The latter proteins exist as soluble monomers released by the parasite during infection and these AChE are distinct from those enzymes which the nematodes use for synaptic transmission in their neuromuscular system. Thus far, Dictyocaulus viviparus is the only animal-parasitic nematode for which distinct genes that encode both neuromuscular and secreted AChEs have been defined. Here, we describe the isolation and characterization of a cDNA encoding a putative neuromuscular AChE from D. viviparus which contains a tryptophan amphiphilic tetramerization (WAT) domain at its C-terminus analogous to the common ‘tailed’ AChE form found in the neuromuscular systems of vertebrates and in the ACE-1 AChE from Caenorhabditis elegans. This enzyme differs from the previously isolated, D. viviparus neuromuscular AChE (Dv-ACE-2), which is a glycosylphosphatidylinositol-anchored variant analogous to vertebrate ‘hydrophobic’ AChE.

Keywords

Dictyocaulus viviparusnematodeacetylcholinesterasetryptophan amphiphilic tetramerization domain
Type
Research Article
Information
Parasitology , Volume 133 , Issue 3 , September 2006 , pp. 381 - 387
Copyright
2006 Cambridge University Press

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