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PMID:16487302

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Citation

dos Santos, AL, de Carvalho, IM, da Silva, BA, Portela, MB, Alviano, CS and de Araújo Soares, RM (2006) Secretion of serine peptidase by a clinical strain of Candida albicans: influence of growth conditions and cleavage of human serum proteins and extracellular matrix components. FEMS Immunol. Med. Microbiol. 46:209-20

Abstract

Candida albicans expresses a vast number of hydrolytic enzymes, playing roles in several phases of yeast-host interactions. Here, we identified two novel extracellular peptidase classes in C. albicans. Using gelatin-sodium dodecyl sulfate polyacrylamide gel electrophoresis two gelatinolytic activities were detected at physiological pH: a 60-kDa metallopeptidase, completely blocked by 1,10-phenanthroline, and a 50-kDa serine peptidase inhibited by phenylmethylsulfonyl fluoride. In an effort to establish a probable functional implication for these novel peptidase classes, we demonstrated that the 50-kDa secretory serine peptidase was active over a broad pH range (5.0-7.2) and was capable to hydrolyze some soluble human serum proteins and extracellular matrix components. Conversely, when this isolate was grown in yeast carbon base supplemented with bovine serum albumin, a secretory aspartyl peptidase activity was measured, instead of metallo- and serine peptidases, suggesting that distinct medium composition induces different expression of released peptidases in C. albicans. Additionally, we showed by quantitative proteolytic measurement, flow cytometry and immunoblotting assays that the brain heart infusion medium might repress the Sap1-3 production. Collectively, our results showed for the first time the capability of an extracellular proteolytic enzyme other than aspartic-type peptidases to cleave a broad spectrum of relevant host proteinaceous substrates by the human pathogen C. albicans.

Links

PubMed Online version:10.1111/j.1574-695X.2005.00023.x

Keywords

Adult; Blood Proteins/metabolism; Candida albicans/enzymology; Candida albicans/growth & development; Candida albicans/pathogenicity; Candidiasis/microbiology; Culture Media; Extracellular Matrix/metabolism; Female; Fungal Proteins/metabolism; Humans; Metalloproteases/metabolism; Serine Endopeptidases/secretion; Urinary Tract Infections/microbiology

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

9HIV1:Q9Q288

GO:0004190: aspartic-type endopeptidase activity

ECO:0000314:

F

Figure 1

complete
CACAO 10776

Notes

See also

References

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