Feeding is crucial for the growth and survival of animals, including humans, but relatively little is known about how it is regulated. Here, we show that larval feeding in Ostrinia furnacalis is regulated by neuropeptide F (NPF, the homologous peptide of mammalian NPY) via the insulin signalling pathway in the midgut. Furthermore, the genes pi3k and mtor in the insulin pathway positively regulate α-amylase and lipase of the midgut by recruiting the transcription factors c-Myc and PPARγ for binding to the promotors of these two enzymes. Importantly, we find that the feeding behaviour and the digestive system of midgut in O. furnacalis larvae are closely related and interactive in that knocking down α-amylase or lipase induces a reduction in larval feeding, while food-deprived larvae lead to fewer expressions of α-amylase and lipase. Importantly, it is the gut NPF that regulates the α-amylase and lipase, while variations of α-amylase and lipase may feed back to the brain NPF. This current study reveals a molecular feedback mechanism between feeding behaviour and the digestive system that is regulated by the conserved NPF via insulin signalling systems in the midgut of O. furnacalis larvae.

Sitodiplosis mosellana, a periodic but devastating wheat pest that escapes temperature extremes in summer and winter by undergoing obligatory diapause. To determine the roles of small heat shock proteins (sHsps) in diapause of S. mosellana, we characterized two sHsp genes, SmHsp17.4 and SmHsp20.3, from this species. Both SmHsps contained the conserved α-crystallin domain and the carboxy-terminal I/VXI/V motif of the sHsp family. SmHsp17.4 had one intron while SmHsp20.3 had none. Quantitative PCR revealed that SmHsp17.4 expression decreased after diapause initiation, but substantially increased during transition to post-diapause quiescence. In contrast, SmHsp20.3 expression was not affected by entry of diapause, but was clearly up-regulated during summer and winter. Short-term more severe heat-stress (≥35 °C) of over-summering larvae or cold-stress (≤−5 °C) of over-wintering larvae could stimulate higher expression of both genes, and SmHsp17.4 was more responsive to cold stress while SmHsp20.3 was more sensitive to heat stress. Notably, transcription of SmHsp17.4, but not SmHsp20.3, in diapausing larvae was inducible by 20-hydroxyecdysone (20E). Recombinant SmHsp17.4 and SmHsp20.3 proteins also displayed significant chaperone functionality. These findings suggest that both SmHsps play key roles in stress tolerance during diapause; and 20E-regulated SmHsp17.4 was also likely involved in diapause termination.