Hostname: page-component-cd9895bd7-q99xh Total loading time: 0 Render date: 2024-12-23T13:36:08.007Z Has data issue: false hasContentIssue false

Immunocytochemical localization of a putative inhibitory amino acid receptor subunit in the parasitic nematodes Haemonchus contortus and Ascaris suum

Published online by Cambridge University Press:  01 July 1998

T. M. SKINNER
Affiliation:
Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK Present address: Roslin Institute, Roslin, Edinburgh EH25 9PS, UK.
Z. A. BASCAL
Affiliation:
Department of Physiology and Pharmacology, Bassett Crescent East, University of Southampton, Southampton SO9 3TU, UK
L. HOLDEN-DYE
Affiliation:
Department of Physiology and Pharmacology, Bassett Crescent East, University of Southampton, Southampton SO9 3TU, UK
G. G. LUNT
Affiliation:
Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK
A. J. WOLSTENHOLME
Affiliation:
Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, UK

Abstract

A rabbit antiserum was raised against a synthetic peptide corresponding to a region near the N-terminus of the Haemonchus contortus inhibitory amino acid receptor subunit, HG1. The antiserum recognized a recombinant form of the N-terminal domain of the subunit on Western blots and reacted with the ventral nerve cord of H. contortus in immunofluorescence experiments. Immunofluorescence was also detected in specific head neurons of H. contortus: these were tentatively identified as ring motor- and inter-neurons, plus a possible sensory neuron equivalent to the AQR cell of Caenorhabditis elegans. In the roundworm Ascaris suum, immunoreactivity was limited to the muscle arms, the post-synaptic component of the neuromuscular junction. The possible ligand of receptors containing the HG1 subunit is discussed in the light of this expression pattern.

Type
Research Article
Copyright
1998 Cambridge University Press

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)