Evidence map›Paper›PMID 40890180›Full record

ArticleScientific reports2025

Functional roles of purified yapsins from Candida glabrata (Nakaseomyces glabratus) in immune modulation and cross-species biofilm formation.

Dorota Satala, Grzegorz Satala, Kamila Kulig, Justyna Karkowska-Kuleta, Andrzej Kozik, Maria Rapala-Kozik

Abstract read
In one paragraph

Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

5 citing papers in PubMed.

  1. Article
  2. Journal of medical microbiology · 2026
    Review
  3. Article
  4. Article
  5. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Dorota SatalaDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków, 30-387, Poland. dorota.satala@uj.edu.pl.
Grzegorz SatalaDepartment of Medicinal Chemistry, Maj Institute of Pharmacology, Polish Academy of Sciences, Smetna 12, Kraków, Poland.
Kamila KuligDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków, 30-387, Poland.
Justyna Karkowska-KuletaDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków, 30-387, Poland.
Andrzej KozikDepartment of Analytical Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków, 30-387, Poland.
Maria Rapala-KozikDepartment of Comparative Biochemistry and Bioanalytics, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, Kraków, 30-387, Poland.

Funding

Narodowe Centrum Nauki 2020/39/D/NZ6/00854
6 · The paper itself

Abstract

Candida glabrata (currently classified as Nakaseomyces glabratus) is an opportunistic yeast-like fungus that causes infections in humans, with limited treatment options due to resistance to antifungal drugs. In contrast to C. albicans, which produces secreted aspartic proteases (Saps) involved in pathogenicity, C. glabrata expresses a distinct group of cell surface-associated aspartic proteases known as yapsins (Yps). While YPS gene deletion mutants have proposed roles in cellular homeostasis, their precise contribution to fungal virulence and host interactions remains unclear. Herein, we present the first detailed biochemical and functional characterization of two native Yps proteins, Yps3 and Yps9, purified from C. glabrata cultures. Both proteases displayed robust activity in a mildly acidic to neutral pH range (5.5-7.0), resistance to the classical aspartic protease inhibitor pepstatin A, and selectively degraded key host antimicrobial peptides, including LL-37 cathelicidin, histatin 5 (Hst5), and kininogen-derived peptide NAT26, by hydrolyzing lysine residues. Additionally, Yps9 promoted C. albicans biofilm dispersal. In a Galleria mellonella infection model, a pre-treatment with each protease enhanced larval survival and increased phenol oxidase activity, implying a role of yapsins in immune priming. Collectively, these findings reveal multifunctional roles for Yps3 and Yps9 in fungal virulence, biofilm modulation, and host immune interactions.

Indexed as

Aspartic Acid ProteasesBiofilmsCandida glabrataFungal ProteinsAnimalsCandida albicansCandidiasisMothsVirulenceAspartic Acid ProteasesFungal ProteinsCandida glabrataGalleria mellonellaHost defense peptidesImmune modulationYapsin aspartic proteases

Identifiers

PMID40890180
PMCPMC12402140

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.