title: Peptidase profiles from non-albicans Candida spp. isolated from the blood of a patient with chronic myeloid leukemia and another with sickle cell disease.
abstract: Candida lipolytica and Candida rugosa were isolated from blood samples from a patient with chronic myeloid leukemia (31 years old) and a patient with sickle cell disease (1-year-old), respectively. Isolates were grown for 48 h at 37 degrees C in either Sabouraud or tryptone soy broth (TSB). Peptidases were tested for using substrate sodium dodecyl sulfate-polyacrylamide gels with gelatin, casein, bovine serum albumin (BSA) or hemoglobin. Enzymography analyses were made on the following substrates: human albumin, IgG and human fibrinogen, which had been incubated with the concentrated supernatants. For C. lipolytica, a approximately 60-kDa gelatin-degrading serine proteolytic activity was found in the TSB supernantant as well as a metallopeptidase activity capable of hydrolysing human albumin, IgG and human fibrinogen. With C. rugosa, albumin, IgG and human fibrinogen substrates were degraded by an aspartyl-like peptidase activity. Supernatants from C. rugosa also showed three serine proteolytic activities towards gelatin (approximately 50 kDa, TSB), casein ( approximately 94 kDa, TSB) and BSA ( approximately 120-kDa, Sabouraud), in addition to a metallopeptidase capable of degrading casein ( approximately 110 kDa, Sabouraud). Little is known about peptidases of C. rugosa and C. lipolytica and this preliminary data may prove useful for future work on host-parasite relationship and antifungal agents.
authors.affiliation: Departamento de Microbiologia Geral, Instituto de Microbiologia Prof. Paulo de Góes (IMPPG), Bloco I, Centro de Ciências da Saúde (CCS), Universidade Federal do Rio de Janeiro (UFRJ), Cidade Universitária, Ilha do Fundão, Rio de Janeiro, Brazil.
authors.forename: Ana Cristina Nogueira
authors.initials: AC
authors.lastname: De Melo
authors.forename: Marcos
authors.initials: M
authors.lastname: Dornelas-Ribeiro
authors.forename: Edilma Paraguai
authors.initials: EP
authors.lastname: De Souza
authors.forename: Andrew
authors.initials: A
authors.lastname: Macrae
authors.forename: Sérgio Eduardo Longo
authors.initials: SE
authors.lastname: Fracalanzza
authors.forename: Alane B
authors.initials: AB
authors.lastname: Vermelho
mesh_terms: D000328:Adult; D000755:Anemia, Sickle Cell / Q000150:complications*; D001798:Blood Proteins / Q000378:metabolism; D002175:Candida / Q000187:drug effects / Q000201:enzymology*; D002176:Candida albicans / Q000201:enzymology; D002177:Candidiasis / Q000150:complications* / Q000382:microbiology*; D003470:Culture Media; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D007223:Infant; D015464:Leukemia, Myelogenous, Chronic, BCR-ABL Positive / Q000150:complications*; D008297:Male; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000378:metabolism*
chemical_list: D001798:Blood Proteins; D003470:Culture Media; D005656:Fungal Proteins; D011480:Protease Inhibitors; D012697:Serine Endopeptidases