We have already described the regulation by phosphorylation

We have already described the regulation by phosphorylation

of PbICL, the other enzyme unique to the glyoxylate cycle [32]. The secretion of PbMLS [9] suggests that it interacts with fungus proteins themselves and host surface proteins. Extracellular vesicles from Paracoccidioides spp present proteins with many functions [33]. Of 11 PbMLS-interacting proteins, 5 were also found in the extracellular vesicle. Extracellular proteins are known to play important roles, such as the uptake of nutrients, cell-cell communication and AICAR purchase detoxification of the environment [34]. More specifically, proteins secreted by pathogenic microorganisms appear to play important roles in virulence BAY 80-6946 research buy [35]. Corroborating our results, many proteins identified in this study, such as 2-methylcitrate synthase, malate dehydrogenase, nucleoside diphosphate kinase, pyruvate kinase, hsp70-like protein and Cobalamin-independent Selleckchem AZD6094 methionine synthase, had previously been described as secreted proteins in Paracoccidioides Pb01 secretome from mycelium and yeast cells [36]. The adhesion of pathogens to host cells is considered to be an essential step in the establishment of infection [37]. Several clinically important fungi, such as Candida albicans, Aspergillus fumigatus, Histoplasma capsulatum and Cryptococcus neoformans, are known to bind

to proteins of the extracellular matrix (ECM) [38]. The adhesins of fungi are important in the migration, invasion, differentiation and proliferation of microbes. Paracoccidioides yeast cells also have the ability to adhere and invade host cells [39, 40]. Some adhesins, such as PbDfg5p [41], triosephosphate isomerase (PbTPI) [42], glyceraldehyde-3-phosphate dehydrogenase (PbGAPDH) [39], and enolase (PbEno) [43], and PbMLS [9] have been described in Paracoccidioides Pb01. Here, the interaction between PbMLS and enolase and triosephosphate isomerase was confirmed by Far-Western blot assay. The interaction of PbMLS

with those proteins suggests that the joint action of those adhesins could Levetiracetam promote adhesion to and invasion of host cells, acting as potent virulence factors. PbMLS appears to act in the interaction between Paracoccidioides Pb01 and macrophage because it interacts with several macrophage-specific proteins, of which 5 proteins are related to cytoskeleton, which suggests the involvement of that structure in the fungus adhesion process. The PbMLS binding to actin was confirmed by Far-Western blot. The cytoskeletons of the macrophages control the movement of the cell membrane, which reflects the movement of the cell as a whole and are also involved in processes such as phagocytosis [44]. Our previous work used Far-Western blotting and flow cytometry to show that PbMLS binds to A549 cells.

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