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FMRFamide-like peptides in root knot nematodes and their potential role in nematode physiology

Published online by Cambridge University Press:  21 October 2009

M.J.G. Johnston*
Affiliation:
Parasitology, School of Biological Sciences, Medical Biology Centre, Queen's University Belfast, 97 Lisburn Road, BelfastBT9 7BL, Northern Ireland Applied Plant Science, Newforge Lane, Agri-Food and Biosciences Institute, BelfastBT9 5PX, Northern Ireland
P. McVeigh
Affiliation:
Parasitology, School of Biological Sciences, Medical Biology Centre, Queen's University Belfast, 97 Lisburn Road, BelfastBT9 7BL, Northern Ireland
S. McMaster
Affiliation:
Parasitology, School of Biological Sciences, Medical Biology Centre, Queen's University Belfast, 97 Lisburn Road, BelfastBT9 7BL, Northern Ireland Applied Plant Science, Newforge Lane, Agri-Food and Biosciences Institute, BelfastBT9 5PX, Northern Ireland
C.C. Fleming
Affiliation:
Applied Plant Science, Newforge Lane, Agri-Food and Biosciences Institute, BelfastBT9 5PX, Northern Ireland
A.G. Maule
Affiliation:
Parasitology, School of Biological Sciences, Medical Biology Centre, Queen's University Belfast, 97 Lisburn Road, BelfastBT9 7BL, Northern Ireland

Abstract

FMRFamide-like peptides (FLPs) are a diverse group of neuropeptides that are expressed abundantly in nematodes. They exert potent physiological effects on locomotory, feeding and reproductive musculature and also act as neuromodulators. However, little is known about the specific expression patterns and functions of individual peptides. The current study employed rapid amplification of cDNA ends-polymerase chain reaction (RACE-PCR) to characterize flp genes from infective juveniles of the root knot nematodes, Meloidogyne incognita and Meloidogyne minor. The peptides identified from these transcripts are sequelogs of FLPs from the free-living nematode, Caenorhabditis elegans; the genes have therefore been designated as Mi-flp-1, Mi-flp-7, Mi-flp-12, Mm-flp-12 and Mi-flp-14. Mi-flp-1 encodes five FLPs with the common C-terminal moiety, NFLRFamide. Mi-flp-7 encodes two copies of APLDRSALVRFamide and APLDRAAMVRFamide and one copy of APFDRSSMVRFamide. Mi-flp-12 and Mm-flp-12 encode the novel peptide KNNKFEFIRFamide (a longer version of RNKFEFIRFamide found in C. elegans). Mi-flp-14 encodes a single copy of KHEYLRFamide (commonly known as AF2 and regarded as the most abundant nematode FLP), and a single copy of the novel peptide KHEFVRFamide. These FLPs share a high degree of conservation between Meloidogyne species and nematodes from other clades, including those of humans and animals, perhaps suggesting a common neurophysiological role which may be exploited by novel drugs. FLP immunoreactivity was observed for the first time in Meloidogyne, in the circumpharyngeal nerve ring, pharyngeal nerves and ventral nerve cord. Additionally, in situ hybridization revealed Mi-flp-12 expression in an RIR-like neuron and Mi-flp-14 expression in SMB-like neurons, respectively. These localizations imply physiological roles for FLP-12 and FLP-14 peptides, including locomotion and sensory perception.

Type
Research Papers
Copyright
Copyright © Cambridge University Press 2010

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Footnotes

Nucleotide sequence data reported in this paper are available in the GenBank™, EMBL and DDBJ databases under the accession numbers AY729023, AY856132, AY804187, AY907829 and DQ228710.

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