Cloning and transcriptional expression of a leucokinin‐like peptide receptor from the Southern cattle tick, Boophilus microplus (Acari: Ixodidae)

Abstract

Leucokinins are invertebrate neuropeptides that exhibit myotropic and diuretic activity. Only one leucokinin-like peptide receptor is known, the lymnokinin receptor from the mollusc Lymnaea stagnalis. A cDNA encoding a leucokinin-like peptide receptor was cloned from the Southern cattle tick, Boophilus microplus, a pest of cattle world-wide. This is the first neuropeptide receptor known from the Acari and the second known in the subfamily of leucokinin-like peptide G-protein-coupled receptors. The deduced amino acid sequence exhibits 40% identity to the lymnokinin receptor. The receptor transcript is present in all tick life stages as determined by semiquantitative reverse transcription polymerase chain reaction. We also propose that the sequence AAF50775.1 from the Drosophila melanogaster genome (CG10626) encodes the first identified insect leucokinin receptor.

Systematic G-protein-coupled Receptor Analysis inDrosophila melanogaster Identifies a Leucokinin Receptor with Novel Roles

“…Similar results have been reported elsewhere (19,37,38). The two non-insect leucokinin-like receptors (from L. stagnalis (15) and B. microplus (18)) were included in the dendrogram and were found to sit within a tightly defined clade, containing characterized examples of Drosophila tachykinin receptors (40 -42), together with novel putative genes. As leucokinins are considered to be distantly similar to tachykinins, this was clearly the group containing the strongest candidates for a leucokinin receptor.…”

“…No leucokinin receptors have been identified in insects, although a receptor for a distantly related peptide, that shares a FxSWxamide motif with Drosokinin, has been cloned from the pond snail Lymnaea stagnalis, and was found to be a member of the GPCR superfamily (15). A further leucokinin-like receptor has been cloned in the cattle tick Boophilus microplus, and this also displays the seven-transmembrane domain structure characteristic of GPCRs (18). Although a Drosophila gene has been identified as being similar to the lymnokinin receptor in silico (18,19), no functional evidence for its identification as a leucokinin receptor is available nor is the similarity between Drosophila and Lymnaea leucokinins compelling (Table I).…”

“…A further leucokinin-like receptor has been cloned in the cattle tick Boophilus microplus, and this also displays the seven-transmembrane domain structure characteristic of GPCRs (18). Although a Drosophila gene has been identified as being similar to the lymnokinin receptor in silico (18,19), no functional evidence for its identification as a leucokinin receptor is available nor is the similarity between Drosophila and Lymnaea leucokinins compelling (Table I). Accordingly, in this paper, we used a genome-wide scan to identify the clade of GPCRs that were most similar to receptors for tachykinins, including the lymnokinin receptor, and to assay them all systematically for activity.…”

Integrative physiology, functional genomics and the phenotype gap: a guide for comparative physiologists

“…Indeed, although the first leucokinins were characterized in an insect (Holman et al, 1984), the first gene for a leucokinin receptor, and its cognate peptide, were identified in the pond snail Lymnaea stagnalis in a single, thoroughly impressive paper (Cox et al, 1997). Similarly, leucokinin signalling is known to occur in the Acari (mites and ticks) (Holmes et al, 2000). In insects, leucokinins are uniformly myogenic and diuretic (Coast et al, 2002).…”

Two novel neuropeptides in innervation of the salivary glands of the black‐legged tick, Ixodes scapularis: Myoinhibitory peptide and SIFamide

“…Periviscerokinin was the first conserved neuropeptide identified in ticks by using matrix-assisted laser desorption/ionization-time of flight (MALDI-TOF) analysis of single neurons (Neupert et al, 2005). Molecular cloning and functional analysis of the Gprotein-coupled receptor for a kinin-like peptide in the southern cattle tick, Boophilus microplus, further suggested that ticks produce multiple neuropeptides and receptors similar to those identified in other arthropods (Holmes et al, 2000(Holmes et al, , 2003Taneja-Bageshwar et al, 2006). We recently described the complex neuroendocrine network present in the central and peripheral nervous systems of the hard tick, Rhipicephalus appendiculatus, by using 15 different antibodies that recognize various neuropeptides (Šimo et al, 2009).…”