ArticleNano letters2019
Fluidic Force Microscopy Demonstrates That Homophilic Adhesion by Candida albicans Als Proteins Is Mediated by Amyloid Bonds between Cells.
Article in Nano letters, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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Who cites it
22 citing papers in PubMed, 49 citations in OpenAlex.
- Article
- Amyloid fibrils of the Als5p-derived peptide NHVirulence · 2025Article
- Review
- Functional redundancy in Candida auris cell surface adhesins crucial for cell-cell interaction and aggregation.Nature communications · 2024Article
- Characterization of a unique attachment organelle: Single-cell force spectroscopy ofNanoscale · 2024Article
- Functional Redundancy inResearch square · 2024Article
- Functional Redundancy inbioRxiv : the preprint server for biology · 2024Article
- Article
- Blocking Serum Amyloid-P Component from Binding to Macrophages and Augmenting Fungal Functional Amyloid Increases Macrophage Phagocytosis ofPathogens (Basel, Switzerland) · 2022Article
- Extending applications of AFM to fluidic AFM in single living cell studies.Journal of cellular physiology · 2022Review
- Cell-Cell Mating Interactions: Overview and Potential of Single-Cell Force Spectroscopy.International journal of molecular sciences · 2022Review
- Structure and Conservation of Amyloid Spines From theFrontiers in molecular biosciences · 2022Article
- FLO11, a Developmental Gene Conferring Impressive Adaptive Plasticity to the YeastPathogens (Basel, Switzerland) · 2021Review
- Multi-Omics Reveals the Inhibition ofMicroorganisms · 2021Article
- The Flo Adhesin Family.Pathogens (Basel, Switzerland) · 2021Review
- Article
- A New Function for Amyloid-Like Interactions: Cross-Beta Aggregates of Adhesins form Cell-to-Cell Bonds.Pathogens (Basel, Switzerland) · 2021Review
- The impact of the Fungus-Host-Microbiota interplay upon Candida albicans infections: current knowledge and new perspectives.FEMS microbiology reviews · 2021Review
- Single-cell fluidic force microscopy reveals stress-dependent molecular interactions in yeast mating.Communications biology · 2021Article
- How Microbes Use Force To Control Adhesion.Journal of bacteriology · 2020Review
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
Abstract
The fungal pathogen Candida albicans frequently forms drug-resistant biofilms in hospital settings and in chronic disease patients. Cell adhesion and biofilm formation involve a family of cell surface Als (agglutinin-like sequence) proteins. It is now well documented that amyloid-like clusters of laterally arranged Als proteins activate cell-cell adhesion under mechanical stress, but whether amyloid-like bonds form between aggregating cells is not known. To address this issue, we measure the forces driving Als5-mediated intercellular adhesion using an innovative fluidic force microscopy platform. Strong cell-cell adhesion is dependent on expression of amyloid-forming Als5 at high cell surface density and is inhibited by a short antiamyloid peptide. Furthermore, there is greatly attenuated binding between cells expressing amyloid-forming Als5 and cells with a nonamyloid form of Als5. Thus, homophilic bonding between Als5 proteins on adhering cells is the major mode of fungal aggregation, rather than protein-ligand interactions. These results point to a model whereby amyloid-like β-sheet interactions play a dual role in cell-cell adhesion, that is, in formation of adhesin nanoclusters ( cis-interactions) and in homophilic bonding between amyloid sequences on opposing cells ( trans-interactions). Because potential amyloid-forming sequences are found in many microbial adhesins, we speculate that this novel mechanism of amyloid-based homophilic adhesion might be widespread and could represent an interesting target for treating biofilm-associated infections.
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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.