Paracoccidioides brasiliensis, a thermally dimorphic
fungus, is the causative agent of
paracoccidioidomycosis, a systemic mycosis that is widespread in
Latin America. This
fungus is a facultative intracellular pathogen able to survive and replicate inside non-activated
macrophages. Therefore, the
survival of P. brasiliensis inside the host depends on the
ability to adapt to
oxidative stress induced by immune
cells, especially
alveolar macrophages. For several years,
reactive oxygen species (ROS) were only associated with
pathological processes. Currently, a plethora of
roles for ROS in
cell signaling have emerged. We have previously reported that low ROS concentrations cause
cell proliferation in the
human pathogenic
fungus P. brasiliensis. In the present
report, we investigated the influence of
phosphorylation events in that process. Using a
mass spectrometry-based approach, we mapped 440
phosphorylation sites in 230 P. brasiliensis
proteins and showed that
phosphorylation at different sites determines fungal responses to
oxidative stress, which are regulated by
phosphatases and
kinases activities. Furthermore, we present additional evidence for a functional two-component
signal transduction system in P. brasiliensis. These findings
will help us to understand the
phosphorylation events involved in the
oxidative stress response.