{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,20]],"date-time":"2026-06-20T08:45:59Z","timestamp":1781945159517,"version":"3.54.5"},"reference-count":23,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2004,1,16]],"date-time":"2004-01-16T00:00:00Z","timestamp":1074211200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Yeast"],"published-print":{"date-parts":[[2004,1,30]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Within the context of studies on genes from <jats:italic>Paracoccidioides brasiliensis<\/jats:italic> (<jats:italic>Pb<\/jats:italic>) potentially associated with fungus\u2013host 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 <jats:italic>Pb<\/jats:italic> cDNA library and was designated <jats:italic>PbcatP<\/jats:italic>. 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 <jats:italic>Pb<\/jats:italic>CATP revealed canonical motifs of monofunctional typical small subunit catalases and the peroxisome\u2010PTS\u20101\u2010targeting signal. The deduced and the native <jats:italic>Pb<\/jats:italic>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 <jats:italic>Pb<\/jats:italic>CATP and cloning and characterization of the cDNA are essential steps for investigating the role of catalase as a defence of <jats:italic>P. brasiliensis<\/jats:italic> against oxygen\u2010dependent killing mechanisms. These results suggest that this protein exerts an influence in the virulence of <jats:italic>P. brasiliensis<\/jats:italic>. Copyright \u00a9 2004 John Wiley &amp; Sons, Ltd.<\/jats:p>","DOI":"10.1002\/yea.1077","type":"journal-article","created":{"date-parts":[[2004,1,27]],"date-time":"2004-01-27T08:00:54Z","timestamp":1075190454000},"page":"173-182","source":"Crossref","is-referenced-by-count":34,"title":["Monofunctional catalase P of <i>Paracoccidioides brasiliensis<\/i>: identification, characterization, molecular cloning and expression analysis"],"prefix":"10.1002","volume":"21","author":[{"given":"Sabrina F. I.","family":"Moreira","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexandre M.","family":"Bail\u00e3o","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M\u00f4nica S.","family":"Barbosa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rosalia S. 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