Use of plant extracts on whitefly control in tomato grown in greenhouseLooking for alternative methods of control to silverleaf whitefly Bemisia tabaci (Gennadius) biotype B in tomato, attractiveness and oviposition preference tests were accomplished in greenhouse using fourteen aqueous extracts at 3% (weight/volume). The extracts were prepared with parts from Azadirachta indica, Trichilia pallida, Chenopodium ambrosioides, Piper nigrum, Melia azedarach, Ruta graveolens, Ricinus communis, Mentha pulegium, Tagetes erecta, Eucalyptus citriodora, Cymbopogon nardus and Coriandrum sativum. The most efficient extracts in greenhouse were also tested in laboratory to evaluate the possible systemic effect on whitefly nymphs. Tomato plants sprayed with extracts of leaves from M. pulegium, leaves and seeds from A. indica were less attractive to the adults of the insect. Plants sprayed with extracts of leaves from A. indica and leaves + branches from R. communis showed deterrent effects on the insect oviposition, reducing the number of eggs; in an opposite way, the extract of leaves from C. nardus stimulated the whitefly oviposition on the plants. The use of extracts in a systemic way did not affect the whitefly development period (egg-adult). The extracts of seeds and leaves from A. indica and leaves from M. pulegium increased the mortality of nymphs of B. tabaci biotype B.

Field assays were performed to evaluate the attractiveness and the non-preference of whitefly Bemisia tabaci (Genn.) biotype B for oviposition on squash genotypes (Cucurbita pepo) and to observe the susceptibility of genotypes (Novita, Sandy, Caserta Cac Melhorada, Novita Plus, Samira, Bianca, AF-2858 and Caserta TS) to silverleaf symptoms. The Sandy genotype was the least attractive to whitefly, while Novita Plus, AF-2858 and Samira were the most attractive. The Caserta Cac Melhorada genotype was the least preferred for oviposition. The Sandy and AF-2858 genotypes were the most productive, with the highest mean of fruits produced. The lowest silverleaf symptoms index was observed for the Sandy and Caserta Cac Melhorada genotypes.

Introduction: Emerging studies have proposed novel roles of HDL in cardiovascular and noncardiovascular diseases. The understanding of how HDL participates in a pathophysiological process involves animal models, as well as clinical studies. A key issue involving HDL studies is the accurate quantification of its proteome. HDL proteome is complex, and its composition may be modulated by the subject’s health state. The main goal of this work is to establish a pipeline for accurate quantification of HDL proteome in clinical and animal studies. Hypothesis: The knowledge of the composition of HDL proteome in clinical and animal studies is critical to understand its biological functions. Methods: We first performed a deep proteomic analysis to identify proteins belonging to HDL of mice and humans. We then established a targeted, data independent acquisition (DIA) strategy that works for mouse and humans. Next, by using different software platforms, we developed a quantification methodology specific for each species. Results: Although mice and humans share many of their HDL proteins, the protein sequence is unique for each species, and thus, HDL proteome quantification methods must be species specific. Using recent advances in mass spectrometry, we employed a single acquisition method that worked for both, mice and human samples. Differentiation occurred after acquisition, using spectral libraries specifically built for each species. Using different software platforms, we compared four strategies of quantification for HDL proteome, showing that CVs depend on the strategy employed. Thus, using quality control samples (n=8), we showed that for the same protein, CVs may vary up to 50 %. The quantification strategy was thus optimized in order to provide the best quantification with the least variance, reaching CVs lower than 15 % for 90 % of the proteins. Conclusions: Using the same mass spectrometry acquisition method, it is possible to quantify HDL proteome of mice and humans in a consistent and accurate way. These advances may integrate animal models and clinical studies of HDL proteome.