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Mycopathologia 2008-Jul

A 25-kDa serine peptidase with keratinolytic activity secreted by Coccidioides immitis.

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Bárbara Gabriela Brum Lopes
André Luis Souza Dos Santos
Cláudia de Carvalho Falci Bezerra
Bodo Wanke
Márcia Dos Santos Lazéra
Marília Martins Nishikawa
Ana Maria Mazotto
Vânia Monteiro Kussumi
Rosa Maria Tavares Haido
Alane Beatriz Vermelho

Keywords

Abstract

Coccidioides immitis is the causative agent of coccidioidomycosis, a systemic mycosis that attacks humans and a wide variety of animals. In the present study, we showed that the C. immitis mycelial form is able to release proteolytic enzyme into the extracellular environment. Under chemically defined growth conditions, mycelia secreted seven distinct polypeptides ranging from 15 to 65 kDa and an extracellular peptidase of 25 kDa. This enzyme had its activity fully inhibited by phenylmethylsulphonyl fluoride, a serine peptidase inhibitor. Conversely, metallo, cysteine, and aspartyl peptidase inhibitors did not alter the 25-kDa enzyme behavior. This extracellular serine peptidase was able to degrade keratin, a fibrous protein that composes human epidermis. Additionally, this peptidase cleaved different protein substrates, including gelatin, casein, hemoglobin, and albumin. Curiously, an 18-kDa serine peptidase activity was evidenced solely when casein was used as the co-polymerized protein substrate into the gel. The existence of different secreted peptidases could be advantageous for the adaptation of C. immitis to distinct environments during its complex life cycle.

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