Ovicidal lectins from Moringa oleifera and Myracrodruon urundeuva cause alterations in chorionic surface and penetrate the embryos of Aedes aegypti eggs.

BACKGROUND: Lectins from Moringa oleifera seeds (WSMoL), Myracrodruon urundeuva bark (MuBL), and heartwood (MuHL) are larvicidal agents against Aedes aegypti; in addition, WSMoL is an ovicidal agent against this mosquito. In this work, we evaluated the ovicidal activity of MuBL and MuHL by determining the concentrations that reduce the hatching rates by 50% in 72 h (EC50 ). The effects of WSMoL, MuBL, and MuHL on the ultrastructure of the eggs' surface were assessed by scanning electron microscopy (SEM). In addition, the ability of these lectins to penetrate the eggs was investigated by using conjugates of the lectins with fluorescein isothiocyanate (FITC). RESULTS: MuBL and MuHL were ovicidal agents with EC50 of 0.26 and 0.80 mg/mL (260 and 800 ppm), respectively. SEM images of eggs treated with WSMoL for 24 h revealed discontinuity of the exochorionic network and the absence of the exochorionic cells and their tubercles. After 48 and 72 h of incubation, strong deformation and degeneration of egg surfaces were observed. In MuBL and MuHL-treated eggs, the presence of lumps on the surface of the eggs, disappearance of the exochorionic network and the decrease and deformation of tubercles were observed. Lastly, fluorescence microscopy revealed that the three lectins were able to enter the eggs and reach the digestive tract of the embryos. CONCLUSION: WSMoL, MuBL, and MuHL are ovicidal agents on A. aegypti that have differing efficiencies in terms of how they cause alterations in the chorionic surface and in terms of their ability to penetrate the eggs. © 2019 Society of Chemical Industry.

Binding targets of termiticidal lectins from the bark and leaf of Myracrodruon urundeuva in the gut of Nasutitermes corniger workers.

BACKGROUND: Lectins, carbohydrate-binding proteins, from the bark (MuBL) and leaf (MuLL) of Myracrodruon urundeuva are termiticidal agents against Nasutitermes corniger workers and have been shown to induce oxidative stress and cell death in the midgut of these insects. In this study, we investigated the binding targets of MuBL and MuLL in the gut of N. corniger workers by determining the effects of these lectins on the activity of digestive enzymes. In addition, we used mass spectrometry to identify peptides from gut proteins that adsorbed to MuBL-Sepharose and MuLL-Sepharose columns. RESULTS: Exoglucanase activity was neutralized in the presence of MuBL and stimulated by MuLL. α-l-Arabinofuranosidase activity was not affected by MuBL but was inhibited by MuLL. Both lectins stimulated α-amylase activity and inhibited protease and trypsin-like activities. Peptides with homology to apolipophorin, trypsin-like enzyme, and ABC transporter substrate-binding protein were detected from proteins that adsorbed to MuBL-Sepharose, while peptides from proteins that bound to MuLL-Sepharose shared homology with apolipophorin. CONCLUSION: This study revealed that digestive enzymes and transport proteins found in worker guts can be recognized by MuBL and MuLL. Thus, the mechanism of their termiticidal activity may involve changes in the digestion and absorption of nutrients. © 2018 Society of Chemical Industry.