Abstract
Proteases of Candida dubliniensis have been scarcely studied, these enzymes may play an important role in nitrogen metabolism, post-translational processing, nutritional stress, dimorphism, virulence, etc. In this work, we report the presence of five different intracellular proteases and one extracellular proteolytic activity. The intracellular proteases are: aminopeptidase ycdAPE, carboxypeptidase ycdCP, dipeptidyl aminopeptidase ycdDAP, proteinases ycdPrA and ycdPrB, and extracellular protease Sap activity, measured under several nutritional conditions. C. dubliniensis produced the highest level of intracellular proteolytic enzymes, i.e., ycdAPE, ycdCP, ycdDAP, ycdPrA and ycdPrB in media with peptone during stationary growth phase. Chelating agents affected mainly APE activity; whereas ycdCp, ycdDAP, and ycdPrB were affected by serine protease inhibitors; ycdPrA was affected by pepstatin, an aspartyl protease inhibitor. We found Sap activity in C. dubliniensis in YCB-SBA medium, this activity was inhibited by pepstatin inhibitor. Southern analysis revealed the presence of at least four genes encoding Sap in the C. dublinienisis genome (using as probes SAP1, SAP2, SAP3, and SAP4-6 genes from C. albicans).
Highlights
Proteolysis, a vital process for cell life, plays an important role in different physiological functions, such as protein digestion, hormone maturation, immune response, inflammation, fertilization, germination, as well as in other morphological processes
We report the presence of five different intracellular proteases and one extracellular proteolytic activity in C. dubliniensis
This paper presents, as far as we know, the first activity, this activity seems to be a metalloprotease, report on intracellular proteases of C. dubliniensis and according to the results obtained in the inhibition suggests four encoding secreted aspartic proteinase multi-gene (SAP) genes on the genome of assays
Summary
Proteolysis, a vital process for cell life, plays an important role in different physiological functions, such as protein digestion, hormone maturation, immune response, inflammation, fertilization, germination, as well as in other morphological processes. Candida dubliniensis was first described as a novel species in 1995 This organism is very close to the human yeast pathogen, Candida albicans. There are several proteases associated with yeast proteasomes that participate in stress-dependent and ubiquitin-mediated proteolysis They are involved in the degradation of short-lived and regulator proteins that generate small peptides from proteins, these latter are degraded into amino acids by tri-, di-, carboxi-, and amino-peptidases [6,7]. Extracellular proteolytic activity plays a central role in Candida albicans pathogenicity and is produced by a family of 10 secreted aspartyl proteinases (Sap proteins) [3]. Numerous studies have correlated extracellular proteolytic activity in vitro with the virulence of Candida species and have shown that the most virulent species, such as C. albicans, C. tropicalis, and C. parapsilosis, produce more proteinases in vitro than the less virulent species [3]. We report the presence of five different intracellular proteases and one extracellular proteolytic activity in C. dubliniensis
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