Identification of a cDNA encoding DH, PBAN and other FXPRL neuropeptides from the tobacco hornworm, Manduca sexta, and expression associated with pupal diapause

Peptides
Wei Hua Xu, David L Denlinger

Abstract

We have cloned the diapause hormone (DH)-pheromone biosynthesis activating neuropeptide (PBAN) cDNA from the suboesophageal ganglion (SG) of Manduca sexta pupae using rapid amplification of cDNA ends. The Mas-DH-PBAN cDNA encodes a preprohormone of 194 amino acids that contains five peptides (PBAN, DH-like, and alpha-, beta-, gamma-SGNP), all of which share a common FXPRL sequence at the C-terminus. Yet, the sequences are rather distinct from those reported from other species: Mas-alpha-SGNP has a unique C-terminal FXPEL (the arginine or lysine at FXPR(or K)L is replaced by glutamic acid), Mas-gamma-SGNP is one amino acid shorter than its counterpart in other species, and Mas-PBAN contains two extra residues not seen in other species. Mas-DH-like peptide has the highest homology (83%) to Bombyx mori DH. Northern blot analysis shows a single mRNA corresponding in size to the Mas-DH-PBAN cDNA detected in brain-SG samples of pupae and adults, suggesting that these peptides are derived from a precursor through posttranslational processing. Using the more sensitive method of RT-PCR, DH-PBAN mRNA is also detectable in thoracic ganglia, although the expression is much lower than in the SG. Developmental profiles of DH-PBAN transcripts...Continue Reading

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Citations

Mar 1, 2011·FEBS Letters·Luca SchiesariRodolfo Costa
Nov 3, 2010·Journal of Insect Physiology·Man-Yeon ChoiSteven M Valles
Sep 2, 2010·General and Comparative Endocrinology·Meritxell Pérez-HedoMatilde Eizaguirre
Sep 9, 2008·General and Comparative Endocrinology·N Audsley, R J Weaver
May 23, 2008·General and Comparative Endocrinology·Ada Rafaeli
Jun 1, 2010·Archives of Insect Biochemistry and Physiology·Man-Yeon ChoiSteven M Valles
Dec 8, 2005·Journal of Insect Physiology·Vladimír Kostál
Jan 5, 2021·Frontiers in Physiology·Yaling ZhangXinming Yin

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