Extracellular proteinases of Candida species pathogenic yeasts

Rapala‐Kozik, M.; Bochenska, O.; Zajac, D.; Karkowska‐Kuleta, J.; Gogol, M.; Zawrotniak, M.; Kozik, A.

doi:10.1111/omi.12206

Cited by 94Antifungal resistance and susceptibilityFungal and yeast genetics researchFungal Infections and Studies

Extracellular proteinases of Candida species pathogenic yeasts

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Rapala‐Kozik, M., Bochenska, O., Zajac, D., Karkowska‐Kuleta, J., Gogol, M., Zawrotniak, M., Kozik, A.·2018·Molecular Oral Microbiology

DOI 10.1111/omi.12206

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Abstract

The increased incidence of severe disseminated infections caused by the opportunistic yeast-like fungi Candida spp. highlights the urgent need for research into the major virulence factors of these pathogens-extracellular aspartic proteinases of the candidapepsin and yapsin families. Classically, these enzymes were considered to be generally destructive factors that damage host tissues and provide nutrients for pathogen propagation. However, in recent decades, novel and more specific functions have been suggested for extracellular candidal proteinases. These include contributions to cell wall maintenance and remodeling, the formation of polymicrobial biofilms, adhesion to external protective barriers of the host, the deregulation of host proteolytic cascades (such as the complement system, blood coagulation and the kallikrein-kinin system), a dysregulated host proteinase-inhibitor balance, the inactivation of host antimicrobial peptides, evasion of immune responses and the induction of inflammatory mediator release from host cells. Only a few of these activities recognized in Candida albicans candidapepsins have been also confirmed in other Candida species, and characterization of Candida glabrata yapsins remains limited.

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C. glabrata cell wall is associated with serine protease Cwp1 (ORF: CBS138), a gelatinolytic enzyme.
“C. glabrata is exceptional from this rule because the cell wall is associated with serine protease, Cwp1 (ORF: CBS138)—a gelatinolytic enzyme [24].”
From Candida glabrata: pathogenicity and resistance mechanisms for adaptation and survival (2021) · cites this paper as [24]
The primary factor aiding persistence of C. glabrata is its less aggressive nature to stimulate a strong reaction of the host immune system.
“The primary factor aiding the persistence of C. glabrata is its less aggressive nature to stimulate the strong reaction of the host immune system [24].”
From Candida glabrata: pathogenicity and resistance mechanisms for adaptation and survival (2021) · cites this paper as [24]

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Authors: Rapala‐Kozik, M., Bochenska, O., Zajac, D., Karkowska‐Kuleta, J., Gogol, M., Zawrotniak, M., & Kozik, A.
Affiliations: Department of Comparative Biochemistry and Bioanalytics Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University Krakow Poland
Department of Analytical Biochemistry Faculty of Biochemistry, Biophysics and Biotechnology Jagiellonian University Krakow Poland
Jagiellonian University (PL)
Corresponding author: Kozik, A.
ORCID: Karkowska‐Kuleta, J.
Zawrotniak, M.
Kozik, A.
Venue: Molecular Oral Microbiology
Publisher: Wiley
Published: 2018-01-19
Volume: 33
Issue: 2
Pages: 113-124
ISSN: 2041-1006 (ISSN-L)
2041-1014
DOI: 10.1111/omi.12206
OpenAlex: W2769719637
Cited by: 94
References: 125
Citations by year: 2026: 3 · 2025: 11 · 2024: 33 · 2023: 8 · 2022: 9 · 2021: 11 · 2020: 8 · 2019: 7 · 2018: 4
FWCI: 0.80
Type: journal article
Language: en
Open access: green
ruj.uj.edu.pl
Licence: cc-by-nc-nd
onlinelibrary.wiley.com/termsAndConditions#vor (vor)
Locations: Molecular Oral Microbiology (publishedVersion)
PubMed (publishedVersion)
Jagiellonian University Repository (Jagiellonian University) (submittedVersion, cc-by-nc-nd)
Topics: Health Sciences › Medicine › Infectious Diseases › Antifungal resistance and susceptibility
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Health Sciences › Medicine › Epidemiology › Fungal Infections and Studies
Keywords: Candida, extracellular protease, aspartic protease, virulence factors, Candida albicans, Candida glabrata, cell wall remodeling, biofilm formation, complement system, coagulation, kallikrein-kinin system, antimicrobial peptides, immune evasion, inflammatory mediators, opportunistic fungal infection
MeSH terms: Candida parapsilosis, Antibodies, Blood Coagulation, Candida, Candida albicans, Cell Wall, Humans, Pepsin A, Peptide Hydrolases, Protease Inhibitors, Aspartic Acid Endopeptidases, Sequence Homology, Amino Acid, Biofilms, Antimicrobial Cationic Peptides, Virulence Factors, Candida tropicalis, Candida glabrata, Host-Pathogen Interactions, Immune Evasion, Proteolysis

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Extracellular proteinases of Candida species pathogenic yeasts

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