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Monofunctional catalase P of Paracoccidioides brasiliensis : identification, characterization, molecular cloning and expression analysis
Author(s) -
Moreira Sabrina F. I.,
Bailão Alexandre M.,
Barbosa Mônica S.,
Jesuino Rosalia S. A.,
Felipe M. Sueli Soares,
Pereira Maristela,
Soares Célia Maria de Almeida
Publication year - 2004
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.1077
Subject(s) - paracoccidioides brasiliensis , biology , complementary dna , catalase , cdna library , microbiology and biotechnology , biochemistry , amino acid , peptide sequence , gene , enzyme
Within the context of studies on genes from Paracoccidioides brasiliensis ( Pb ) potentially associated with fungus–host interaction, we isolated a 61 kDa protein, pI 6.2, that was reactive with sera of patients with paracoccidioidomycosis. This protein was identified as a peroxisomal catalase. A complete cDNA encoding this catalase was isolated from a Pb cDNA library and was designated PbcatP . The cDNA contained a 1509 bp ORF containing 502 amino acids, whose molecular mass was 57 kDa, with a pI of 6.5. The translated protein Pb CATP revealed canonical motifs of monofunctional typical small subunit catalases and the peroxisome‐PTS‐1‐targeting signal. The deduced and the native Pb CATP demonstrated amino acid sequence homology to known monofunctional catalases and was most closely related to catalases from other fungi. The protein and mRNA were diminished in the mycelial saprobic phase compared to the yeast phase of infection. Protein synthesis and mRNA levels increased during the transition from mycelium to yeast. In addition, the catalase protein was induced when cells were exposed to hydrogen peroxide. The identification and characterization of the Pb CATP and cloning and characterization of the cDNA are essential steps for investigating the role of catalase as a defence of P. brasiliensis against oxygen‐dependent killing mechanisms. These results suggest that this protein exerts an influence in the virulence of P. brasiliensis . Copyright © 2004 John Wiley & Sons, Ltd.