ArticlePLoS pathogens2014
Structural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coli.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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.
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Who cites it
28 citing papers in PubMed, 49 citations in OpenAlex.
- Biophysical and functional characterization of the Escherichia coli Dr fimbrial envelope reveals its importance for pathogenesis and lithogenesis.PLoS pathogens · 2026Article
- Deciphering the Implications ofPathogens (Basel, Switzerland) · 2026Review
- EnteroaggregativeEcoSal Plus · 2025Review
- Structural basis of aggregative adherence fimbriae II interactions with sialic acid, mucin, and human intestinal cells.Infection and immunity · 2025Article
- The AcrAB efflux pump contributes to the virulence of EnteroaggregativeFrontiers in cellular and infection microbiology · 2025Article
- Chitosan-Coated Silver Nanoparticles Inhibit Adherence and Biofilm Formation of UropathogenicACS infectious diseases · 2024Article
- Aggregative adherence fimbriae form compact structures as seen by SAXS.Scientific reports · 2023Article
- Shiga-Toxin-Producing Strains ofMicroorganisms · 2023Article
- Diversity in Genetic Regulation of Bacterial Fimbriae Assembled by the Chaperone Usher Pathway.International journal of molecular sciences · 2022Review
- Antibiofilm agents with therapeutic potential against enteroaggregative Escherichia coli.PLoS neglected tropical diseases · 2022Article
- The Superior Adherence Phenotype of E. coli O104:H4 is Directly Mediated by the Aggregative Adherence Fimbriae Type I.Virulence · 2021Article
- Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021Article
- Structure Determination of Microtubules and Pili: Past, Present, and Future Directions.Frontiers in molecular biosciences · 2021Review
- Enteroaggregative E. coli Adherence to Human Heparan Sulfate Proteoglycans Drives Segment and Host Specific Responses to Infection.PLoS pathogens · 2020Article
- Identification and characterisation of enteroaggregative Escherichia coli subtypes associated with human disease.Scientific reports · 2020Article
- Classical chaperone-usher (CU) adhesive fimbriome: uropathogenic Escherichia coli (UPEC) and urinary tract infections (UTIs).Folia microbiologica · 2020Review
- Adhesion of EnteroaggregativeBio-protocol · 2018Article
- Article
- Methylation, crystallization and SAD phasing of the Csu pilus CsuC-CsuE chaperone-adhesin subunit pre-assembly complex from Acinetobacter baumannii.Acta crystallographica. Section F, Structural biology communications · 2017Article
- EnteroaggregativemBio · 2017Article
Corrections and comments
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Authors and funding
16 authors at 5 institutions in 4 countries.
Funding
Abstract
Enteroaggregative Escherichia coli (EAEC) is a leading cause of acute and persistent diarrhea worldwide. A recently emerged Shiga-toxin-producing strain of EAEC resulted in significant mortality and morbidity due to progressive development of hemolytic-uremic syndrome. The attachment of EAEC to the human intestinal mucosa is mediated by aggregative adherence fimbria (AAF). Using X-ray crystallography and NMR structures, we present new atomic resolution insight into the structure of AAF variant I from the strain that caused the deadly outbreak in Germany in 2011, and AAF variant II from archetype strain 042, and propose a mechanism for AAF-mediated adhesion and biofilm formation. Our work shows that major subunits of AAF assemble into linear polymers by donor strand complementation where a single minor subunit is inserted at the tip of the polymer by accepting the donor strand from the terminal major subunit. Whereas the minor subunits of AAF have a distinct conserved structure, AAF major subunits display large structural differences, affecting the overall pilus architecture. These structures suggest a mechanism for AAF-mediated adhesion and biofilm formation. Binding experiments using wild type and mutant subunits (NMR and SPR) and bacteria (ELISA) revealed that despite the structural differences AAF recognize a common receptor, fibronectin, by employing clusters of basic residues at the junction between subunits in the pilus. We show that AAF-fibronectin attachment is based primarily on electrostatic interactions, a mechanism not reported previously for bacterial adhesion to biotic surfaces.
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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.