Candida parapsilosis expresses and secretes two aspartic proteinases
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Updated: Nov 8, 2026

Quantifying the Antifungal Activity of Peptides Against Candida albicans
Published on: January 13, 2023
1Laboratory of Protein Crystallography, Oklahoma Medical Research Foundation, Oklahoma City 73104.
Abstract:
We have isolated and characterized a second aspartic proteinase secreted by the CHUV E-18 strain of Candida parapsilosis. This proteinase is produced at a level corresponding to approximately 25% of the production of the main proteinase described earlier [1]. This minor proteinase has similar molecular weight and pH optimum but differs in the isoelectric point and in the specificity when compared with the major secreted form. The determination of the amino terminal amino acid sequence identified this minor form of Candida parapsilosis aspartic proteinase as a protein which corresponds to the sequence deduced from genomic DNA originally reported as a pseudogene [1]. We conclude that strain CHUV E-18 of Candida parapsilosis expresses and secretes two different aspartic proteinases.
Insights
Candida parapsilosis secretes two distinct aspartic proteinases. A newly identified minor proteinase, previously thought to be a pseudogene, is actively expressed and secreted by the CHUV E-18 strain.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Candida parapsilosis is a fungal pathogen known to secrete aspartic proteinases.
- Previous research identified a primary aspartic proteinase from the CHUV E-18 strain.
- A potential secondary aspartic proteinase gene was previously identified but considered a pseudogene.
Purpose of the Study:
- To isolate and characterize a second aspartic proteinase from Candida parapsilosis CHUV E-18.
- To compare the properties of this minor proteinase with the previously identified major proteinase.
- To determine the identity and expression status of the minor aspartic proteinase.
Main Methods:
- Isolation and characterization of secreted proteinases.
- Biochemical analysis including molecular weight and pH optimum determination.
- Isoelectric focusing and substrate specificity assays.
- Amino-terminal amino acid sequencing.
Main Results:
- A second aspartic proteinase was isolated and characterized from C. parapsilosis CHUV E-18.
- This minor proteinase constitutes approximately 25% of the total secreted proteinase production.
- It shares a similar molecular weight and pH optimum with the major proteinase but differs in isoelectric point and substrate specificity.
- Amino-terminal sequencing confirmed this proteinase corresponds to the sequence previously annotated as a pseudogene.
Conclusions:
- The CHUV E-18 strain of Candida parapsilosis expresses and secretes two distinct aspartic proteinases.
- The previously identified pseudogene is actively transcribed and translated into a functional, secreted proteinase.
- This finding expands our understanding of the proteinase repertoire in Candida parapsilosis.
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