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

Abstract

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.

Molecular cloning, mRNA expression and biological activity of the pheromone biosynthesis activating neuropeptide (PBAN) from the European corn borer, Ostrinia nubilalis

“…Sequencing of the entire coding sequence and exon–intron boundaries of the Ostnu ‐ PBAN gene revealed that it is at least 5 kb long and consists of six exons and five introns with a conserved distribution of intron positions within codons (0, 2, 1, 2, 1). The Ostnu‐PBAN gene has extensive structural homology to the B. mori (Xu et al ., ), Helicoverpa armigera (Zhang et al ., ), Clostera anastomosis (Jing et al ., ) and M. vitrata (Chang & Ramasamy ) DH ‐ PBAN genes, which have previously been identified in the genomes of lepidopteran species belonging to various families. Short‐ and medium‐length 3′ UTR forms were also observed in the amplification products obtained from adzuki bean borer ( Os.…”

Pheromone‐binding proteins based phylogenetics and phylogeography of Maruca spp. from Asia, Africa, Oceania, and South America

“…The total DNA was extracted from individual larva of Maruca using (Chang & Srinivasan, 2014) using Primer3 (Untergasser et al, 2007), and their quality was checked in PCR Primer Stats (http://www.bioin forma tics.org/sms2/ Alternative primer 5′-GTTGCAGGAGCTGAAAATGG-3′ 5′-GCTGTCCTTCGGGTAACATC-3′ Internal primer 5′-CTC ATC TGC ATG TCC ACC A -3′ 5′-CTT GGT GGA CAT CCA GAT GAG-3′ PBP2 Main primer 5′-AATGGCCTAAAGGGCCACAA-3′ 5′-AGGTTTCATGTCACAATCTTCATC-3′ 1.1-3.0…”

Identification and expression of a new member of the pyrokinin/pban gene family in the sand fly Phlebotomus papatasi

“…This has resulted in confusion over which conserved domains are present among non-lepidopteran species, and how to apply the a, b, PBAN and c NP labels. While we have adopted the format of Jurenka and Nusawardani (2011), other examples of PBAN-like peptide classifications exist in the literature (Choi et al, 2010;2013;Chang and Ramasamy, 2014). Thus, a class-wide pk/pban translation analysis is needed to identify which conserved peptide domains are present, regardless of functional processing, thereby making it possible to reliably identify NP products.…”