ArticleJournal of bacteriology1997
The glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase of Candida albicans is a surface antigen.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers, 1 of them a synthesis that pooled it.
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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.
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.
Who cites it
49 citing papers in PubMed, 1 synthesis or guideline pooled it, 163 citations in OpenAlex.
- Use of recombinant proteins for the diagnosis and prevention ofFrontiers in veterinary science · 2024Pooled it
- Omics and Multiomics-Based Diagnostics for Invasive Candidiasis: Toward Precision Medicine.Molecular & cellular proteomics : MCP · 2025Review
- Endocytic tethers modulate unconventional GAPDH secretion.Cell surface (Amsterdam, Netherlands) · 2025Article
- Identification of the Most Immunoreactive Antigens ofJournal of proteome research · 2024Article
- Glyceraldehyde 3-Phosphate Dehydrogenase on the Surface ofInternational journal of molecular sciences · 2024Article
- Review
- Mass Spectrometry-Based Proteomic and Immunoproteomic Analyses of theJournal of fungi (Basel, Switzerland) · 2021Article
- Review
- Article
- Evaluation of anti-biofilm activity of acidic amino acids and synergy with ciprofloxacin on Staphylococcus aureus biofilms.Scientific reports · 2020Article
- Study on the Function of the Inositol Polyphosphate Kinases Kcs1 and Vip1 ofFrontiers in microbiology · 2020Article
- Potential Antifungal Targets Based on Glucose Metabolism Pathways ofFrontiers in microbiology · 2020Review
- Why Do Intravascular Schistosomes Coat Themselves in Glycolytic Enzymes?BioEssays : news and reviews in molecular, cellular and developmental biology · 2019Article
- Comparison ofHeliyon · 2019Article
- A dedicated glyceraldehyde-3-phosphate dehydrogenase is involved in the biosynthesis of volatile sesquiterpenes in Trichoderma virens-evidence for the role of a fungal GAPDH in secondary metabolism.Current genetics · 2019Article
- Identification of Cross Reactive Antigens of C. botulinum Types A, B, E & F by Immunoproteomic Approach.Current microbiology · 2018Article
- Comparative Secretome Analysis Reveals Perturbation of Host Secretion Pathways by a Hypovirus.Scientific reports · 2016Article
- Exploiting death: apoptotic immunity in microbial pathogenesis.Cell death and differentiation · 2016Review
- Extracellular Vesicle-Associated Transitory Cell Wall Components and Their Impact on the Interaction of Fungi with Host Cells.Frontiers in microbiology · 2016Review
- Candida albicans cell shaving uncovers new proteins involved in cell wall integrity, yeast to hypha transition, stress response and host-pathogen interaction.Journal of proteomics · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A lambda gt11 cDNA library from Candida albicans ATCC 26555 was screened by using pooled sera from two patients with systemic candidiasis and five neutropenic patients with high levels of anti-C. albicans immunoglobulin M antibodies. Seven clones were isolated from 60,000 recombinant phages. The most reactive one contained a 0.9-kb cDNA encoding a polypeptide immunoreactive only with sera from patients with systemic candidiasis. The whole gene was isolated from a genomic library by using the cDNA as a probe. The nucleotide sequence of the coding region showed homology (78 to 79%) to the Saccharomyces cerevisiae TDH1 to TDH3 genes coding for glyceraldehyde-3-phosphate dehydrogenase (GAPDH), and their amino acid sequences showed 76% identity; thus, this gene has been named C. albicans TDH1. A rabbit polyclonal antiserum against the purified cytosolic C. albicans GAPDH (polyclonal antibody [PAb] anti-CA-GAPDH) was used to identify the GAPDH in the beta-mercaptoethanol extracts containing cell wall moieties. Indirect immunofluorescence demonstrated the presence of GAPDH at the C. albicans cell surface, particularly on the blastoconidia. Semiquantitative flow cytometry analysis showed the sensitivity of this GAPDH form to trypsin and its resistance to be removed with 2 M NaCl or 2% sodium dodecyl sulfate. The decrease in fluorescence in the presence of soluble GAPDH indicates the specificity of the labelling. In addition, a dose-dependent GAPDH enzymatic activity was detected in intact blastoconidia and germ tube cells. This activity was reduced by pretreatment of the cells with trypsin, formaldehyde, and PAb anti-CA-GAPDH. These observations indicate that an immunogenic, enzymatically active cell wall-associated form of the glycolytic enzyme GAPDH is found at the cell surface of C. albicans cells.
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Registered trials
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