|JIANG, HONGBO - Kansas State University|
|DOBESH, SHARON - Kansas State University|
|DONGHUN, KIM - Kansas State University|
|KRZYSZTOF, KACZMAREK - Technical University Of Lodz|
|JANUSZ, ZABROCKI - Technical University Of Lodz|
|PARK, YOONSEONG - Kansas State University|
Submitted to: Scientific Reports
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/18/2016
Publication Date: 2/28/2016
Citation: Jiang, H., Dobesh, S., Donghun, K., Evans, J.D., Nachman, R.J., Krzysztof, K., Janusz, Z., Park, Y. 2016. Ligand selectivity in tachykinin and natalisin neuropeptidergic systems of the honey bee parasitic mite Varroa destructor. Scientific Reports. 6:19547. doi: 10.1038/srep19547.
Interpretive Summary: Varroa mites remain the most important biological threat for honey bees. Controlling these parasites will require novel methods due to acaricide resistance and sensitivity of bees to current control methods. This collaborative study describes a novel approach toward blocking mite proteins that are key for mite development. The results, which show promise, can lead to new avenues of mite research and control, and ultimately help provide beekeepers with new solutions for this key parasite.
Technical Abstract: The varroa mite, Varroa destructor, is a devastating ectoparasite of the honey bees Apis mellifera and A. cerana. Control of these mites in beehives is a challenge in part due to the lack of toxic agents that are specific to mites and not to the host honey bee. In searching for a specific toxic target of varroa mites, we investigated two closely related neuropeptidergic systems, tachykinin-related peptide (TRP) and natalisin (NTL), and their respective receptors. Honey bees lack both NTL and the NTL receptor in their genome sequences, providing the rationale for investigating these receptors to understand their specificities to various ligands. We characterized the receptors for NTL and TRP of V. destructor (VdNTL-R and VdTRP-R, respectively) and for TRP of A. mellifera (AmTRP-R) in a heterologous reporter assay system to determine the activities of various ligands including TRP/NTL peptides and peptidomimetics. Although we found that AmTRP-R is highly promiscuous, activated by various ligands including two VdNTL peptides when a total of 36 ligands were tested, we serendipitously found that peptides carrying the C-terminal motif -FWxxRamide are highly specific to VdTRP-R. This motif can serve as a seed sequence for designing a VdTRP-R-specific agonist.