Identification of a unique pheromonotropic neuropeptide including double FXPRL motifs from a geometrid species, Ascotis selenaria cretacea, which produces an epoxyalkenyl sex pheromone

Kawai, Takeshi; Ohnishi, Atsushi; Suzuki, Masataka; Fujii, Takeshi; Matsuoka, Kanae; Kato, Ikuo; Matsumoto, Shogo; Ando, Tetsu

doi:10.1016/j.ibmb.2006.12.002

Cited by 11 publications

(8 citation statements)

References 31 publications

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“…In the present study, the DH-PBAN transcripts were exclusively located in the head and thorax of adult male and female M. vitrata , but no expression was detected in the abdomen of adults (Figure 5). Our results do not conflict with published results that the DH-PBAN gene is also feebly expressed in thoracic ganglia of H. zea [72], H. virescens [50], Samia cynthia ricini [73], M. sexta [74], Plutella xylostella [75], Ascotis selenaria cretacea [76], Antheraea pernyi [77], and Solenopsis invicta [78]. Association between DH-PBAN expression and abdominal tissue distribution has been reported only in the FXPRLamide-like immunoreactivity assays in abdominal ganglions [73], [77]–[79].…”

Section: Discussionsupporting

confidence: 55%

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Chang

Srinivasan

2014

PLoS ONE

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Neuropeptides play essential roles in a variety of physiological responses that contribute to the development and reproduction of insects. Both the diapause hormone (DH) and pheromone biosynthesis activating neuropeptide (PBAN) belong to the PBAN/pyrokinin neuropeptide family, which has a conserved pentapeptide motif FXPRL at the C-terminus. We identified the full-length cDNA encoding DH-PBAN in Maruca vitrata, a major lepidopteran pest of leguminous crops. The open reading frame of Marvi-DH-PBAN is 591 bp in length, encoding 197 amino acids, from which five putative neuropeptides [DH, PBAN, α-subesophageal ganglion neuropeptide (SGNP), β-SGNP and γ-SGNP] are derived. Marvi-DH-PBAN was highly similar (83%) to DH-PBAN of Omphisa fuscidentalis (Lepidoptera: Crambidae), but possesses a unique C-terminal FNPRL motif, where asparagine has replaced a serine residue present in other lepidopteran PBAN peptides. The genomic DNA sequence of Marvi-DH-PBAN is 6,231 bp in size and is composed of six exons. Phylogenetic analysis has revealed that the Marvi-DH-PBAN protein sequence is closest to its homolog in Crambidae, but distant from Diptera, Coleoptera and Hymenoptera DH-PBAN, which agrees with the current taxonomy. DH-PBAN transcripts were present in the head and thoracic complex, but absent in the abdomen of M. vitrata. Real-time quantitative PCR assays have demonstrated a relatively higher expression of Marvi-DH-PBAN mRNA in the latter half of the pupal stages and in adults. These findings represent a significant step forward in our understanding of the DH-PBAN gene architecture and phylogeny, and raise the possibility of using Marvi-DH-PBAN to manage M. vitrata populations through molecular techniques.

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Section: Discussionsupporting

confidence: 55%

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Chang

Srinivasan

2014

PLoS ONE

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“…Chromatographic behavior of the natural pheromonotropic peptide revealed a unique structure, including b-SGNP (Assc-PBAN III). 17) By RT-PCR screening, specific high expression of Assc-PBAN mRNA was detected in the brain-SG complexes of the female and male adults and, interestingly, weak expression was observed in thoracic ganglions.…”

Section: Identification Of Assc-pbanmentioning

confidence: 97%

“…The cDNA encodes 181 amino acids, including a PBAN homologue and four other putative peptides: a diapause hormone homologue, a-SG neuropeptide (SGNP), b-SGNP, and g-SGNP, all of which shared an FXPR(K)L motif on their C-termini. 17) Although PBANs with 30-35 amino acids have been characterized, the Assc-PBAN homologue (Assc-PBAN I) consisted of 28 amino acids and showed lower homology (Ͻ46%) than the others, as shown in Fig. 2.…”

Section: Identification Of Assc-pbanmentioning

confidence: 99%

“…2) with the predicted sequences by using solid-phase methodology with Fmoc-strategy using an automated peptide synthesizer and observed the highest activity of Assc-PBAN III among the three candidates. 17) Furthermore, to identify the sequence of the Assc-PBAN actually produced, the brain-SG extract was fractionated by HPLC referring to the synthetic peptides, and pheromonotropic activity of each fraction was measured. Chromatographic behavior of the natural pheromonotropic peptide revealed a unique structure, including b-SGNP (Assc-PBAN III).…”

Section: Identification Of Assc-pbanmentioning

confidence: 99%

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Epoxyalkenyl sex pheromones produced by female moths in highly evolved groups: biosynthesis and its endocrine regulation

2008

Self Cite

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“…Using DNA cloning tools more PBAN encoding genes have been identified from the moths, B. mori (Kawano et al ., 1992; Sato et al ., 1993), H. zea (Davis et al ., 1992; Ma et al ., 1994), Mamestra brassicae (Jacquin‐Joly et al ., 1998), Helicoverpa assulta (Choi et al ., 1998), Helicoverpa armigera (Choi, 1999; Zhang et al ., 2004), Agrotis ipsilon (Duportets et al ., 1999), Bombyx mandarina (Xu et al ., 1999), Spodoptera littoralis (Iglesias et al ., 2002), Heliothis virescens (Xu & Denlinger, 2003), Manduca sexta (Xu & Denlinger, 2004), Adoxophyes sp. (Choi et al ., 2004), Samia cynthia ricini (Wei et al ., 2004), Plutella xylostella (Lee & Boo, 2005), Ascotis selenaria cretacea (Kawai et al ., 2007), Clostera anastomosis (Jing et al ., 2007), Spodoptera exigua (Xu et al ., 2007), Orgyia thyellina (Uehara et al ., 2007) and Antheraea pernyi (Wei et al ., 2008). From the identification of PBAN cDNAs, PBAN, diapause hormone (DH) and three additional FXPR/KL neuropeptides (NPs: α, β, γ) were deduced from the same gene and are well conserved in moths.…”

Section: Introductionmentioning

confidence: 99%

Identification of a new member of the PBAN family of neuropeptides from the fire ant, Solenopsis invicta

Choi¹,

Meer²

2009

Insect Molecular Biology

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Neuropeptide hormones produced by neurosecretory cells in the central or peripheral nervous systems regulate various physiological and behavioral events during insect development and reproduction. PBAN/ Pyrokinin is a major neuropeptide family, characterized by a 5-amino-acid C-terminal sequence, FXPRLamide. This family of peptides has been implicated in regulating various physiological functions including, pheromone biosynthesis, muscle contraction, diapause induction or termination, melanization, and puparium formation in different insect species. In the present study, we report a new member of the PBAN family from the red imported fire ant, Solenopsis invicta , Soi-PBAN, composed of 26-AA (GSGEDLSYGDAYEVDEDDHPLFVPRL). Three additional peptides were deduced from Soi-PBAN cDNA: 15-AA (TSQDIASGMWFGPRL), 8-AA (QPQFTPRL) and 9-AA (LPWIPSPRL), that correspond to diapause hormone (DH), β β β β -neuropeptide (NP), and γ γ γ γ -NP, which are found in many lepidopteran moths. Five peptides, DH, α α α α , β β β β , γ γ γ γ NPs, and PBAN are encoded from PBAN genes of lepidopteran moths, but in the fire ant the α α α α -NP is missing. Each of the four synthetic peptides from the fire ant Soi-PBAN cDNA showed significant pheromonotropic activity in a moth model, indicating that these peptides are cross-reactive. Soi-β β β β -NP induced the highest amount of pheromone production of the four peptides evaluated. The Soi-DH homologue had the lowest pheromonotropic activity, but was still significantly greater than control values. When the deduced amino acid sequences (entire ORF domains) from Soi-PBAN cDNA were compared with other known sequences, the fire ant was most similar to the honey bee, but phylogenetically distant from moth and beetle species. Soi-PBAN (26-AA) unlike the other three peptides shows a low degree of sequence identity with honeybee PBAN (33-AA). Based on the amino acid sequences encoded from insect PBAN genes identified to date, neuropeptide diversity is correlated with the taxonomic or phylogenetic classification of Insecta. From the present study we report the first neuropeptide identified and characterized from the central nervous system of Formicidae.

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Identification of a unique pheromonotropic neuropeptide including double FXPRL motifs from a geometrid species, Ascotis selenaria cretacea, which produces an epoxyalkenyl sex pheromone

Cited by 11 publications

References 31 publications

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Identification and Expression Analysis of Diapause Hormone and Pheromone Biosynthesis Activating Neuropeptide (DH-PBAN) in the Legume Pod Borer, Maruca vitrata Fabricius

Epoxyalkenyl sex pheromones produced by female moths in highly evolved groups: biosynthesis and its endocrine regulation

Identification of a new member of the PBAN family of neuropeptides from the fire ant, Solenopsis invicta

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