| Title: | "Molecular and pharmacological characterization of the Chelicerata pyrokinin receptor from the southern cattle tick, Rhipicephalus (Boophilus) microplus" |
| Author(s): | Yang Y; Nachman RJ; Pietrantonio PV; |
| Address: | "Department of Entomology, Texas A&M University, College Station, TX 77843-2475, USA. Insect Control and Cotton Disease Research Unit, Southern Plains Agricultural Research Center, U.S. Department of Agriculture, College Station, TX 77845, USA. Department of Entomology, Texas A&M University, College Station, TX 77843-2475, USA. Electronic address: p-pietrantonio@tamu.edu" |
| DOI: | 10.1016/j.ibmb.2015.02.010 |
| ISSN/ISBN: | 1879-0240 (Electronic) 0965-1748 (Linking) |
| Abstract: | "We identified the first pyrokinin receptor (Rhimi-PKR) in Chelicerata and analyzed structure-activity relationships of cognate ligand neuropeptides and their analogs. Based on comparative and phylogenetic analyses, this receptor, which we cloned from larvae of the cattle tick Rhipicephalus microplus (Acari: Ixodidae), is the ortholog of the insect pyrokinin (PK)/pheromone biosynthesis activating neuropeptide (PBAN)/diapause hormone (DH) neuropeptide family receptor. Rhimi-PKR functional analyses using calcium bioluminescence were performed with a developed stable recombinant CHO-K1 cell line. Rhimi-PKR was activated by four endogenous PKs from the Lyme disease vector, the tick Ixodes scapularis (EC50s range: 85.4 nM-546 nM), and weakly by another tick PRX-amide peptide, periviscerokinin (PVK) (EC50 = 24.5 muM). PK analogs with substitutions of leucine, isoleucine or valine at the C-terminus for three tick PK peptides, Ixosc-PK1, Ixosc-PK2, and Ixosc-PK3, retained their potency on Rhimi-PKR. Therefore, Rhimi-PKR is less selective and substantially more tolerant than insect PK receptors of C-terminal substitutions of leucine to isoleucine or valine, a key structural feature that serves to distinguish insect PK from PVK/CAP2b receptors. In females, ovary and synganglion had the highest Rhimi-PKR relative transcript abundance followed by the rectal sac, salivary glands, Malpighian tubules, and midgut. This is the first pharmacological analysis of a PK/PBAN/DH-like receptor from the Chelicerata, which will now permit the discovery of the endocrinological roles of this neuropeptide family in vectors of vertebrate pathogens" |
| Keywords: | Amino Acid Sequence Animals Arthropod Proteins/chemistry/genetics/*metabolism Base Sequence Female Gene Expression Molecular Sequence Data Rhipicephalus/chemistry/genetics/*metabolism Acari Arthropod PRX-amide peptidomimetics Gpcr Neuromedin U Pyrokinin (; |
| Notes: | "MedlineYang, Yunlong Nachman, Ronald J Pietrantonio, Patricia V eng Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. England 2015/03/10 Insect Biochem Mol Biol. 2015 May; 60:13-23. doi: 10.1016/j.ibmb.2015.02.010. Epub 2015 Mar 4" |
