ArticleACS infectious diseases2018
Bacterial Derived Carbohydrates Bind Cyr1 and Trigger Hyphal Growth in Candida albicans.
Article in ACS infectious diseases, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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
10 citing papers in PubMed, 21 citations in OpenAlex.
- Candida albicans Ssy1 is the extracellular sensor of gut microbiota-derived peptidoglycan fragments mediating invasive hyphal growth in the host.Nature communications · 2025Article
- Evaluation and Comparison ofBiochemistry · 2025Article
- Comprehensive Interactome Analysis for the Sole Adenylyl Cyclase Cyr1 of Candida albicans.Microbiology spectrum · 2022Article
- Purification and Characterization of a Stable, Membrane-Associated Peptidoglycan Responsive Adenylate Cyclase LRR Domain from Human CommensalBiochemistry · 2022Article
- A peptidoglycan storm caused by β-lactam antibiotic's action on host microbiota drives Candida albicans infection.Nature communications · 2021Article
- Pathogen-specific antimicrobials engineered de novo through membrane-protein biomimicry.Nature biomedical engineering · 2021Article
- Bacterial Peptidoglycan Fragments Differentially Regulate Innate Immune Signaling.ACS central science · 2021Article
- Synthesis of Bacterial-Derived Peptidoglycan Cross-Linked Fragments.The Journal of organic chemistry · 2020Article
- Revisiting peptidoglycan sensing: interactions with host immunity and beyond.Chemical communications (Cambridge, England) · 2020Review
- Protein-Protein Interactions inFrontiers in microbiology · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The dimorphic yeast Candida albicans is the most common pathogenic fungus found in humans. While this species is normally commensal, a morphological switch from budding yeast to filamentous hyphae allows the fungi to invade epithelial cells and cause infections. The phenotypic change is controlled by the adenylyl cyclase, Cyr1. Interestingly, this protein contains a leucine-rich repeat (LRR) domain, which is commonly found in innate immune receptors from plants and animals. A functional and pure LRR domain was obtained in high yields from E. coli expression. Utilizing a surface plasmon resonance assay, the LRR was found to bind diverse bacterial derived carbohydrates with high affinity. This domain is capable of binding fragments of peptidoglycan, a carbohydrate polymer component of the bacterial cell wall, as well as anthracyclines produced by Streptomyces, leading to hyphae formation. These findings add another dimension to the human microbiome, taking into account yeast-bacteria interactions that occur in the host.
Indexed as
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What OpenQuestion holds
Registered trials
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.