ArticleBMC microbiology2021
Candida albicans and Candida glabrata triosephosphate isomerase - a moonlighting protein that can be exposed on the candidal cell surface and bind to human extracellular matrix proteins.
Article in BMC microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Candida-associated immune and metabolic rewiring in chronic obstructive pulmonary disease.BMC pulmonary medicine · 2026Article
- Isobavachalcone effectively inhibits the growth ofAntimicrobial agents and chemotherapy · 2026Article
- Cell Surface Shaving-Based Proteomic Profiling of the Surfaceome in Pathogenic Microorganisms.International journal of molecular sciences · 2026Review
- Divergence in surface protein exposure between reference and clinical-derivedActa biochimica Polonica · 2026Article
- Growth conditions shape the proteome and diversity ofCell surface (Amsterdam, Netherlands) · 2025Article
- Functional roles of purified yapsins from Candida glabrata (Nakaseomyces glabratus) in immune modulation and cross-species biofilm formation.Scientific reports · 2025Article
- Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface ofInternational journal of molecular sciences · 2024Article
- Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023Review
- Review
- Proteinous Components of Neutrophil Extracellular Traps Are Arrested by the Cell Wall Proteins ofCells · 2021Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTriosephosphate isomerase (Tpi1) is a glycolytic enzyme that has recently been reported also to be an atypical proteinaceous component of the Candida yeast cell wall. Similar to other known candidal "moonlighting proteins", surface-exposed Tpi1 is likely to contribute to fungal adhesion during the colonization and infection of a human host. The aim of our present study was to directly prove the presence of Tpi1 on C. albicans and C. glabrata cells under various growth conditions and characterize the interactions of native Tpi1, isolated and purified from the candidal cell wall, with human extracellular matrix proteins.
resultsSurface plasmon resonance measurements were used to determine the dissociation constants for the complexes of Tpi1 with host proteins and these values were found to fall within a relatively narrow range of 10
conclusionsThe current study provided structural insights into the interactions of human extracellular matrix proteins with Tpi1 that can occur at the cell surface of Candida yeasts and contribute to the host infection by these fungal pathogens.
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