title: flp-32 Ligand/receptor silencing phenocopy faster plant pathogenic nematodes.
abstract: Restrictions on nematicide usage underscore the need for novel control strategies for plant pathogenic nematodes such as Globodera pallida (potato cyst nematode) that impose a significant economic burden on plant cultivation activities. The nematode neuropeptide signalling system is an attractive resource for novel control targets as it plays a critical role in sensory and motor functions. The FMRFamide-like peptides (FLPs) form the largest and most diverse family of neuropeptides in invertebrates, and are structurally conserved across nematode species, highlighting the utility of the FLPergic system as a broad-spectrum control target. flp-32 is expressed widely across nematode species. This study investigates the role of flp-32 in G. pallida and shows that: (i) Gp-flp-32 encodes the peptide AMRNALVRFamide; (ii) Gp-flp-32 is expressed in the brain and ventral nerve cord of G. pallida; (iii) migration rate increases in Gp-flp-32-silenced worms; (iv) the ability of G. pallida to infect potato plant root systems is enhanced in Gp-flp-32-silenced worms; (v) a novel putative Gp-flp-32 receptor (Gp-flp-32R) is expressed in G. pallida; and, (vi) Gp-flp-32R-silenced worms also display an increase in migration rate. This work demonstrates that Gp-flp-32 plays an intrinsic role in the modulation of locomotory behaviour in G. pallida and putatively interacts with at least one novel G-protein coupled receptor (Gp-flp-32R). This is the first functional characterisation of a parasitic nematode FLP-GPCR.
authors.affiliation: Molecular Biosciences-Parasitology, Institute for Global Food Security, School of Biological Sciences, Queen's University Belfast, Belfast, United Kingdom.
authors.forename: Louise E
authors.initials: LE
authors.lastname: Atkinson
authors.forename: Michael
authors.initials: M
authors.lastname: Stevenson
authors.forename: Ciaran J
authors.initials: CJ
authors.lastname: McCoy
authors.forename: Nikki J
authors.initials: NJ
authors.lastname: Marks
authors.forename: Colin
authors.initials: C
authors.lastname: Fleming
authors.forename: Mostafa
authors.initials: M
authors.lastname: Zamanian
authors.forename: Tim A
authors.initials: TA
authors.lastname: Day
authors.forename: Michael J
authors.initials: MJ
authors.lastname: Kimber
authors.forename: Aaron G
authors.initials: AG
authors.lastname: Maule
authors.forename: Angela
authors.initials: A
authors.lastname: Mousley
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002490:Central Nervous System / Q000033:anatomy & histology / Q000378:metabolism; D019835:FMRFamide / Q000235:genetics* / Q000378:metabolism; D020868:Gene Silencing; D015801:Helminth Proteins / Q000235:genetics* / Q000378:metabolism; D054884:Host-Pathogen Interactions / Q000235:genetics; D008024:Ligands; D049990:Membrane Transport Modulators / Q000378:metabolism; D008969:Molecular Sequence Data; D009068:Movement; D010935:Plant Diseases / Q000469:parasitology; D034741:RNA, Small Interfering / Q000235:genetics; D043562:Receptors, G-Protein-Coupled / Q000235:genetics* / Q000378:metabolism; D015398:Signal Transduction; D011198:Solanum tuberosum / Q000378:metabolism / Q000469:parasitology*; D014431:Tylenchoidea / Q000502:physiology*
chemical_list: D015801:Helminth Proteins; D008024:Ligands; D049990:Membrane Transport Modulators; D034741:RNA, Small Interfering; D043562:Receptors, G-Protein-Coupled; D019835:FMRFamide