title: Peptidases and peptidase inhibitors in gut of caterpillars and in the latex of their host plants.
abstract: Studies investigating the resistance-susceptibility of crop insects to proteins found in latex fluids have been reported. However, latex-bearing plants also host insects. In this study, the gut proteolytic system of Pseudosphinx tetrio, which feeds on Plumeria rubra leaves, was characterized and further challenged against the latex proteolytic system of its own host plant and those of other latex-bearing plants. The gut proteolytic system of Danaus plexippus (monarch) and the latex proteolytic system of its host plant (Calotropis procera) were also studied. The latex proteins underwent extensive hydrolysis when mixed with the corresponding gut homogenates of the hosted insects. The gut homogenates partially digested the latex proteins of foreign plants. The fifth instar of D. plexippus that were fed diets containing foreign latex developed as well as those individuals who were fed diets containing latex proteins from their host plant. In vitro assays detected serine and cysteine peptidase inhibitors in both the gut homogenates and the latex fluids. Curiously, the peptidase inhibitors of caterpillars did not inhibit the latex peptidases of their host plants. However, the peptidase inhibitors of laticifer origin inhibited the proteolysis of gut homogenates. In vivo analyses of the peritrophic membrane proteins of D. plexippus demonstrate resistance against latex peptidases. Only discrete changes were observed when the peritrophic membrane was directly treated with purified latex peptidases in vitro. This study concludes that peptidase inhibitors are involved in the defensive systems of both caterpillars and their host plants. Although latex peptidase inhibitors inhibit gut peptidases (in vitro), the ability of gut peptidases to digest latex proteins (in vivo) regardless of their origin seems to be important in governing the resistance-susceptibility of caterpillars.
authors.affiliation: Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, Fortaleza, CE, CEP 60451-970, Brazil, vramos@ufc.br.
authors.forename: Márcio V
authors.initials: MV
authors.lastname: Ramos
authors.forename: Danielle A
authors.initials: DA
authors.lastname: Pereira
authors.forename: Diego P
authors.initials: DP
authors.lastname: Souza
authors.forename: Maria-Lídia S
authors.initials: ML
authors.lastname: Silva
authors.forename: Luciana M R
authors.initials: LM
authors.lastname: Alencar
authors.forename: Jeanlex S
authors.initials: JS
authors.lastname: Sousa
authors.forename: Juliany-Fátima N
authors.initials: JF
authors.lastname: Queiroz
authors.forename: Cleverson D T
authors.initials: CD
authors.lastname: Freitas
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D029062:Apocynaceae / Q000378:metabolism* / Q000469:parasitology; D004064:Digestive System / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006790:Host-Parasite Interactions; D007840:Latex / Q000378:metabolism*; D007915:Lepidoptera / Q000378:metabolism* / Q000502:physiology; D013058:Mass Spectrometry; D018625:Microscopy, Atomic Force; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism*; D011480:Protease Inhibitors / Q000378:metabolism*; D059748:Proteolysis
chemical_list: D007840:Latex; D011480:Protease Inhibitors; D010447:Peptide Hydrolases