Patrícia M. G. Paiva
Departamento de Bioquímica, Centro de Biociências, Universidade Federal de Pernambuco, Recife, Brazil
Emmanuel V. Pontual
Departamento de Morfologia e Fisiologia Animal, Universidade Federal Rural de Pernambuco, Recife, Brazil
Thiago H. Napoleão
Departamento de Bioquímica, Centro de Biociências, Universidade Federal de Pernambuco, Recife, Brazil
Luana C. B. B. Coelho
Departamento de Bioquímica, Centro de Biociências, Universidade Federal de Pernambuco, Recife, Brazil
Series: Insects and Other Terrestrial Arthropods: Biology, Chemistry and Behavior, Microbiology Research Advances
BISAC: SCI008000
Lectins are hemagglutinating proteins that promote cellular responses due to their interaction with glycosylated molecules. Trypsin inhibitors have been described as endogenous regulators of proteolytic enzymes and as storage proteins. Plant lectins and trypsin inhibitors with insecticidal activity may become an alternative to synthetic insecticides that adversely affect the environment and have promoted the emergence of resistant organisms. These proteins exert deleterious effects on larval survival, weight, feeding ability, and development of insects as well as morphology of larvae, pupae and adults.
The digestive processes in larval gut are highly active and their integrity is an essential aspect in insect development. Plant lectins and trypsin inhibitors can modulate the activity of digestive enzymes in larval gut. This book reports larvicidal lectins and trypsin inhibitors isolated from different plant tissues (e.g. bark, heartwood, leaves, flowers and seeds) with potential applications in the control of numerous insect species, including Achaea janata, Aedes aegypti, Anthonomus grandis, Callosobruchus maculatus, Corcyra cephalonica, Ephestia kuehniella, Helicoverpa armigera, Lacanobia oleracea, Ostrinia nubilalis, Spodoptera littoralis, Spodoptera litura and Zabrotes subfasciatus. The changes in morphology of larvae treated with lectins or trypsin inhibitors, as well as the effect of these proteins on larval á-amylase, â-glucosidase, protease and aminopeptidase activities, are also discussed. (Imprint: Nova)
