Article
A 25-kDa serine peptidase with keratinolytic activity secreted by Coccidioides immitis
Registro en:
LOPES, Bárbara Gabriela Brum et al. A 25-kDa Serine Peptidase with Keratinolytic Activity Secreted by Coccidioides immitis. Mycopathologia, v.166, n. 1, p. 154-158, Jul. 2008.
0301-486X
10.1007/s11046-008-9116-1
1573-0832
Autor
Lopes, Bárbara Gabriela Brum
Santos, André Luis Souza dos
Bezerra, Cláudia de Carvalho Falci
Wanke, Bodo
Lazéra, Márcia dos Santos
Nishikawa, Marília Martins
Mazotto, Ana Maria
Kussumi, Vânia Monteiro
Haido, Rosa Maria Tavares
Vermelho, Alane Beatriz
Resumen
This study was supported by the Brazilian agencies: MCT/CNPq (Conselho Nacional de Desenvolvimento Cientifico e Tecnológico), CEPG/UFRJ (Conselho de Ensino para Graduados e Pesquisas), FAPERJ (Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro), FUJB (Fundação Universitária José Bonifácio), and CAPES (Coordenação de Aperfeiçoamento de Pessoal de Nível Superior). 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 lifecycle. 2030-12-31