A secreted serine protease of Paracoccidioides brasiliensis and its interactions with fungal proteins
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2010
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Background: Paracoccidioides brasiliensis is a thermodimorphic fungus, the causative agent of
paracoccidioidomycosis (PCM). Serine proteases are widely distributed and this class of peptidase has been related
to pathogenesis and nitrogen starvation in pathogenic fungi.
Results: A cDNA (Pbsp) encoding a secreted serine protease (PbSP), was isolated from a cDNA library constructed
with RNAs of fungal yeast cells recovered from liver of infected mice. Recombinant PbSP was produced in
Escherichia coli, and used to develop polyclonal antibodies that were able to detect a 66 kDa protein in the
P. brasiliensis proteome. In vitro deglycosylation assays with endoglycosidase H demonstrated that PbSP is a
N-glycosylated molecule. The Pbsp transcript and the protein were induced during nitrogen starvation. The Pbsp
transcript was also induced in yeast cells infecting murine macrophages. Interactions of PbSP with P. brasiliensis
proteins were evaluated by two-hybrid assay in the yeast Saccharomyces cerevisiae. PbSP interacts with a peptidyl
prolyl cis-trans isomerase, calnexin, HSP70 and a cell wall protein PWP2.
Conclusions: A secreted subtilisin induced during nitrogen starvation was characterized indicating the possible
role of this protein in the nitrogen acquisition. PbSP interactions with other P. brasiliensis proteins were reported.
Proteins interacting with PbSP are related to folding process, protein trafficking and cytoskeleton reorganization.
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PARENTE, Juliana A. et al. A secreted serine protease of Paracoccidioides brasiliensis and its interactions with fungal proteins. BMC Microbiology, London, v. 10, n. 292, 2010.