Protease Inhibitors in Plants: Genes for Improving Defenses Against Insects and Pathogens

JIPs and RIPs: the regulation of plant gene expression by jasmonates in response to environmental cues and pathogens.

“…By virtue of their activities, proteinase inhibitors have been proposed to protect plants against herbivory by decreasing the digestibility and nutritional quality of leaf proteins (Ryan, 1990).…”

Digestive enzymes during development of Ceratitis capitata (Diptera:Tephritidae) and effects of SBTI on its digestive serine proteinase targets

“…Plant proteinase inhibitors, a-amylase inhibitors, lectins and chitin binding proteins are usually expressed in response to herbivore insects, pathogens and wounding (Ryan, 1990;Botella et al, 1996;Koiwa et al, 1997;Sales et al, 2001) and may affect development by interfering in the proteolytic processes of a wide range of potentially damaging organisms, including bacteria, fungi, nematodes (Haq et al, 2004) and insects (Terra and Ferreira, 1994;Pompermayer, et al, 2001;Falco and Silva-Filho, 2003). The effects on insects can be observed when digestive enzymes are inhibited or when defense proteins bind to the gut structures of larvae and insects (XavierFilho, 1993).…”

Effect of trypsin inhibitor from Crotalaria pallida seeds on Callosobruchus maculatus (cowpea weevil) and Ceratitis capitata (fruit fly)

“…The use of proteinaceous inhibitors in insect control strategies has good potential, because insect digestive proteinases are promising targets in the control of various insects, including lepidopterans such as Manduca sexta [3], Heliothis zea [4], Spodoptera litura [5], and Lucilia cuprina [6], and also various coleopterans [7][8][9][10][11]. Despite several suggested physiological functions in plants [12][13][14], the inhibitors are known for their role in response to abiotic [15,16] biotic stresses, especially in plant defense processes against insect pest attack [9,[17][18][19][20]. These plant proteinaceous inhibitors are generally small, stable and abundant proteins [21] showing specificity for serine proteinase, cysteine proteinase, aspartic proteinase or metallo-proteinases [17].…”