ArticlePLoS pathogens2015
Inhibition and Reversal of Microbial Attachment by an Antibody with Parasteric Activity against the FimH Adhesin of Uropathogenic E. coli.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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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
34 citing papers in PubMed, 56 citations in OpenAlex.
- Improving the immunogenicity ofFrontiers in immunology · 2026Article
- Antibodies disrupt bacterial adhesion by ligand mimicry and allosteric interference.Nature communications · 2025Article
- De Novo Design of Miniprotein Inhibitors of Bacterial Adhesins.Research square · 2025Article
- Article
- Structure-based design of an immunogenic, conformationally stabilized FimH antigen for a urinary tract infection vaccine.PLoS pathogens · 2025Article
- Immunoinformatics-driven design and computational analysis of a multiepitope vaccine targeting uropathogenicIn silico pharmacology · 2025Article
- Beyond Antibiotics: What the Future Holds.Antibiotics (Basel, Switzerland) · 2024Review
- Effect of Gravity on Bacterial Adhesion to Heterogeneous Surfaces.Pathogens (Basel, Switzerland) · 2023Article
- The Diversity ofMicroorganisms · 2023Review
- Microbial Genomics: Innovative Targets and Mechanisms.Antibiotics (Basel, Switzerland) · 2023Review
- Recombinant FimH Adhesin Demonstrates How the Allosteric Catch Bond Mechanism Can Support Fast and Strong Bacterial Attachment in the Absence of Shear.Journal of molecular biology · 2022Article
- Neutralizing Antibodies Against Allosteric Proteins: Insights From a Bacterial Adhesin.Journal of molecular biology · 2022Review
- Targeting the BspC-vimentin interaction to develop anti-virulence therapies during Group B streptococcal meningitis.PLoS pathogens · 2022Article
- Strategies to Tackle Antimicrobial Resistance: The Example ofInternational journal of molecular sciences · 2021Review
- Toggle switch residues control allosteric transitions in bacterial adhesins by participating in a concerted repacking of the protein core.PLoS pathogens · 2021Article
- Conformational stability of the bacterial adhesin, FimH, with an inactivating mutation.Proteins · 2021Article
- FimH as a scaffold for regulated molecular recognition.Journal of biological engineering · 2021Article
- Possible drugs for the treatment of bacterial infections in the future: anti-virulence drugs.The Journal of antibiotics · 2021Review
- Microbial Genomics as a Catalyst for Targeted Antivirulence Therapeutics.Frontiers in medicine · 2021Article
- The interaction between flagellin and the glycosphingolipid Gb3 on host cells contributes toVirulence · 2020Article
Corrections and comments
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Authors and funding
14 authors at 3 institutions in 1 country.
Funding
Abstract
Attachment proteins from the surface of eukaryotic cells, bacteria and viruses are critical receptors in cell adhesion or signaling and are primary targets for the development of vaccines and therapeutic antibodies. It is proposed that the ligand-binding pocket in receptor proteins can shift between inactive and active conformations with weak and strong ligand-binding capability, respectively. Here, using monoclonal antibodies against a vaccine target protein - fimbrial adhesin FimH of uropathogenic Escherichia coli, we demonstrate that unusually strong receptor inhibition can be achieved by antibody that binds within the binding pocket and displaces the ligand in a non-competitive way. The non-competitive antibody binds to a loop that interacts with the ligand in the active conformation of the pocket but is shifted away from ligand in the inactive conformation. We refer to this as a parasteric inhibition, where the inhibitor binds adjacent to the ligand in the binding pocket. We showed that the receptor-blocking mechanism of parasteric antibody differs from that of orthosteric inhibition, where the inhibitor replaces the ligand or allosteric inhibition where the inhibitor binds at a site distant from the ligand, and is very potent in blocking bacterial adhesion, dissolving surface-adherent biofilms and protecting mice from urinary bladder infection.
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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.