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Serine proteases are widely distributed and this class of peptidase has been related to pathogenesis and nitrogen starvation in pathogenic fungi.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Results<\/jats:title>\n            <jats:p>A cDNA (<jats:italic>Pb<\/jats:italic> sp) encoding a secreted serine protease (<jats:italic>Pb<\/jats:italic> SP), was isolated from a cDNA library constructed with RNAs of fungal yeast cells recovered from liver of infected mice. Recombinant <jats:italic>Pb<\/jats:italic> SP was produced in <jats:italic>Escherichia coli<\/jats:italic>, and used to develop polyclonal antibodies that were able to detect a 66 kDa protein in the <jats:italic>P. brasiliensis<\/jats:italic> proteome. <jats:italic>In vitro<\/jats:italic> deglycosylation assays with endoglycosidase H demonstrated that <jats:italic>Pb<\/jats:italic> SP is a <jats:italic>N<\/jats:italic>-glycosylated molecule. The <jats:italic>Pb<\/jats:italic> sp transcript and the protein were induced during nitrogen starvation. The <jats:italic>Pb<\/jats:italic> sp transcript was also induced in yeast cells infecting murine macrophages. Interactions of <jats:italic>Pb<\/jats:italic> SP with <jats:italic>P. brasiliensis<\/jats:italic> proteins were evaluated by two-hybrid assay in the yeast <jats:italic>Saccharomyces cerevisiae<\/jats:italic>. <jats:italic>Pb<\/jats:italic> SP interacts with a peptidyl prolyl cis-trans isomerase, calnexin, HSP70 and a cell wall protein PWP2.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>Conclusions<\/jats:title>\n            <jats:p>A secreted subtilisin induced during nitrogen starvation was characterized indicating the possible role of this protein in the nitrogen acquisition. <jats:italic>Pb<\/jats:italic> SP interactions with other <jats:italic>P. brasiliensis<\/jats:italic> proteins were reported. Proteins interacting with <jats:italic>Pb<\/jats:italic> SP are related to folding process, protein trafficking and cytoskeleton reorganization.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1186\/1471-2180-10-292","type":"journal-article","created":{"date-parts":[[2010,11,16]],"date-time":"2010-11-16T19:15:41Z","timestamp":1289934941000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["A secreted serine protease of Paracoccidioides brasiliensis and its interactions with fungal proteins"],"prefix":"10.1186","volume":"10","author":[{"given":"Juliana A","family":"Parente","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"S\u00edlvia M","family":"Salem-Izacc","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Jaime M","family":"Santana","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Maristela","family":"Pereira","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Clayton L","family":"Borges","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Alexandre M","family":"Bail\u00e3o","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"C\u00e9lia MA","family":"Soares","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"297","published-online":{"date-parts":[[2010,11,16]]},"reference":[{"key":"1248_CR1","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1042\/bj2900205","volume":"290","author":"ND Rawlings","year":"1993","unstructured":"Rawlings ND, Barrett AJ: Evolutionary families of peptidases. 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