Proteomic analysis of lysine succinylation of the human pathogen Histoplasma capsulatum

摘要: Abstract Histoplasma capsulatum , the causative agent of histoplasmosis (also called “Darling's disease”), can affect both immunocompetent and immunocompromised hosts. Post-translational protein modification by lysine succinylation (Ksuc) is a frequent occurrence in eukaryote prokaryote. Recently, roles its regulatory enzymes regulating metabolic pathway bacteria, mammalian fungus were highlighted. Here, we report first global profiling succinylation, with 463 sites 202 proteins from H. NAM1 identified, coupling immune-affinity enrichment using an anti-succinyllysine antibody mass spectrometry. The bioinformatics results including GO functional analysis showed that these succinylated are mainly involved central metabolism synthesis, consistent previous reports. 13 on histones H2A, H2B, H3 H4 firstly reported. data good resource for further characterization . Biological significance lung disease histoplasmosis. ability yeasts to infect proliferate within macrophages as intracellular pathogen be contributed several virulence factors regulation. Lysine was recently shown play critical role regulation Candida albicans characterized this work, may also relevant New This represents important address function succinylation.