2013
DOI: 10.1111/1574-6968.12097
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Identification of human plasma proteins associated with the cell wall of the pathogenic fungusParacoccidioides brasiliensis

Abstract: Paracoccidioides brasiliensis and P. lutzii are thermodimorphic species that cause paracoccidioidomycosis. The cell wall is the outermost fungal organelle to form an interface with the host. A number of host effector compounds, including immunologically active molecules, circulate in the plasma. In the present work we extracted cell wall-associated proteins from the yeast pathogenic phase of P. brasiliensis, isolate Pb3, grown in the presence of human plasma, and analyzed bound plasma proteins by liquid chroma… Show more

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Cited by 9 publications
(7 citation statements)
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“…[16][17][18] P. brasiliensis is also known to produce a variety of proteinases. 19,20 The aspartyl proteinases, also known as acid proteases, constitute one of the 4 superfamilies of proteolytic enzymes. They are generally similar to pepsin and show specificity for preferential cleavage at peptide bonds between hydrophobic amino acid residues.…”
Section: Introductionmentioning
confidence: 99%
“…[16][17][18] P. brasiliensis is also known to produce a variety of proteinases. 19,20 The aspartyl proteinases, also known as acid proteases, constitute one of the 4 superfamilies of proteolytic enzymes. They are generally similar to pepsin and show specificity for preferential cleavage at peptide bonds between hydrophobic amino acid residues.…”
Section: Introductionmentioning
confidence: 99%
“…Cell wall purification was performed as previously described for Paracoccidioides brasiliensis (Longo et al. ). Briefly, yeast cell pellets were washed three times in phosphate‐buffered saline solution and mechanically broken in a cell disruptor (B. Braun Biotech International GmBH, Melsungen, Germany) in the presence of glass beads (425–600 μm; Sigma‐Aldrich).…”
Section: Methodsmentioning
confidence: 99%
“…Longo et al identified the ceruloplasmin bound to the cell wall of P . brasiliensis [ 38 ]. Ceruloplasmin is responsible for transporting 70% of the total copper in human serum and exhibits a copper-dependent oxidase activity, which possibly oxidizes Fe 2+ to Fe 3+ , thereby participating in iron transport.…”
Section: Discussionmentioning
confidence: 99%