Pheromone biosynthesis activating neuropeptide (PBAN) produced in the subesophageal ganglion is known to stimulate pheromone production in the pheromone gland. A cDNA isolated from female adult heads of Maruca vitrata encodes 197 amino acids including PBAN, designated as Mvi-PBAN, and four other neuropeptides (NPs): diapause hormone (DH) homologue, α-NP, β-NP and γ-NP. All of the peptides are amidated in their C-termini and shared a conserved motif, FXPR(or K)L-NH2 structure. Mvi-PBAN consists of 35 amino acids as previously reported (Chang and Ramasamy, 2014). RT-PCR analysis revealed that Mvi-PBAN cDNA was expressed in all examined body parts. Nucleotide sequence analysis of RT-PCR products indicated the Mvi-PBAN sequence was identical in all examined body parts of both sexes. These results suggest that Mvi-PBAN expression is maintained in examined stages or tissues.