Res1; Brenda Louyse Olimpia Souza Teixeira2; Lara R. Quadrado2; Aldo Tavares1; Anamelia Bocca1; Felipe Saldanha-araujo1; Octavio Franco2; Rinaldo W. Pereira1 University of Brasilia, Brasilia, Brazil; 2Catholic University of Brasilia, Brasilia, BrazilPF04.Correlation of exosomal miRNA- and anthropometric profile of an active life style Kitti Garai1; Adam Gyebrovszki2; Emese Katai3; Tamas Nagy3; Judit E. Pongracz1; Krisztian Kvell1; Marta WilhelmBackground: Extracellular vesicles (EV) can serve as carries of cellular facts. EVs derived from dendritic cells (DC) have already been shown to target other immune cells and modulate their function. EVs production by DC is induced by a diverse array of signals including cytokines, LPS, and antigens but the part of antimicrobial peptides, including the human cathelicidin LL37, within this method is largely unknown. In this context, we investigate whether or not LL-37 induces and alters DC-derived EVs profile.ISEV 2018 abstract bookMethods: Murine bone marrow-derived DCs have been stimulated with LPS (as a good control) and different concentrations of LL-37. EVs were obtained from cultured cell supernatants and purified by ultracentrifugation. Particle size distribution and concentration of EVs was measured by tunable resistive pulse sensing, and transmission electron microscopy was performed to characterize their morphology. Outcomes: Our preliminary results show that LL-37 increases the concentration of and decreases the average size of EVs when compared with LPS. EV morphology from our samples was in accordance H4 Receptor Agonist supplier together with the literature. Summary/Conclusion: The following ongoing step is the investigation regarding the part of LL37 induced EVs in the immunomodulation effectively described to be carried out by cathelicidin. Funding: This operate was funded by Funda o de Apoio Pesquisa do Distrito Federal, CNPq, CAPES and Universidade Cat ica de Brasilia.PF04.Immunoproteomic characterization of outer membrane vesicles from high-producing actinobacillus pleuropneumoniae Fabio Antenucci1; Zofia Magnowska2; Manfred Nimtz3; Camille Roesch4; Lothar J sch3; Anders Miki Bojesen1 University of Copenhagen, K enhavn S, Denmark; 2University of Copenhagen, Copenhagen, Denmark; 3Helmholtz Centre for Infection Investigation, Braunschweig, Germany; 4Izon Science Ltd, Lyon, FranceBackground: Outer membrane veiscles (OMVs) are created by the majority of Gram-negative bacteria. Thanks to the antigenic similarity between OMVs plus the bacterial outer membrane, OMVs have confirmed to be promising for the improvement of novel vaccines against bacterial pathogens. In this perform we describe the immunoproteomic characterization of OMVs from Actinobacillus pleuropneumoniae (App), a Gramnegative pathogen of good veterinary interest, within the context of vaccine improvement. Solutions: OMVs were isolated from App MIDG2331 serotype eight wild variety and an isogenic nlpI mutant employing a modified version of your hydrostatic filtration protocol described by Musante et al.. OMVs proteins were purified by Wessel-Fl e extraction and resolved by 2D Web page. Protein staining and 2D western Caspase 1 Inhibitor MedChemExpress blotting had been then applied to identify relevant protein spots, which had been excised and subjected to protein identification by MALDI peptide mapping. Benefits: Our evaluation led towards the identification of a number of virulence aspects in App OMVs, such as all three Apx toxins created by App MIDG2331 (Apx II, III and IV) and proteins involved in nutrient acquisition. Some of the proteins were also shown for the first ti.
