caa a22 4500 606208631 CHVBK 20210128101023.0 cr unu---uuuuu 210128e20150101xx s 000 0 eng 10.1007/s00425-014-2174-3 doi (NATIONALLICENCE)springer-10.1007/s00425-014-2174-3 Peptidases and peptidase inhibitors in gut of caterpillars and in the latex of their host plants [Elektronische Daten] [Márcio Ramos, Danielle Pereira, Diego Souza, Maria-Lídia Silva, Luciana Alencar, Jeanlex Sousa, Juliany-Fátima Queiroz, Cleverson Freitas] 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. Springer-Verlag Berlin Heidelberg, 2014 Calotropis procera nationallicence Cryptostegia grandiflora nationallicence Danaus plexippus nationallicence Plumeria rubra nationallicence Pseudosphinx tetrio nationallicence CgLP : Latex proteins of Cryptostegia grandiflora nationallicence CpCP : Purified peptidases of C. proceralatex nationallicence CpLP : Latex proteins of Calotropis procera nationallicence DTT : Dithiothreitol nationallicence HT : Heat treated nationallicence LP : Latex protein nationallicence PM : Peritrophic membrane nationallicence PrLP : Latex proteins of Plumeria rubra nationallicence Ramos Márcio Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut Pereira Danielle Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut Souza Diego Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut Silva Maria-Lídia aut Alencar Luciana Departamento de Física, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE, Brazil aut Sousa Jeanlex Departamento de Física, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE, Brazil aut Queiroz Juliany-Fátima Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut Freitas Cleverson Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut Planta Springer Berlin Heidelberg 241/1(2015-01-01), 167-178 0032-0935 241:1<167 2015 241 425 https://doi.org/10.1007/s00425-014-2174-3 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00425-014-2174-3 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Ramos Márcio Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut NATIONALLICENCE 700 1- Pereira Danielle Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut NATIONALLICENCE 700 1- Souza Diego Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut NATIONALLICENCE 700 1- Silva Maria-Lídia aut NATIONALLICENCE 700 1- Alencar Luciana Departamento de Física, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE, Brazil aut NATIONALLICENCE 700 1- Sousa Jeanlex Departamento de Física, Universidade Federal do Ceará, Campus do Pici, Fortaleza, CE, Brazil aut NATIONALLICENCE 700 1- Queiroz Juliany-Fátima Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut NATIONALLICENCE 700 1- Freitas Cleverson Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Campus do Pici, Cx. Postal 6033, CEP 60451-970, Fortaleza, CE, Brazil aut NATIONALLICENCE 773 0- Planta Springer Berlin Heidelberg 241/1(2015-01-01), 167-178 0032-0935 241:1<167 2015 241 425