ArticleEBioMedicine2016
Lessons from the Crystal Structure of the S. aureus Surface Protein Clumping Factor A in Complex With Tefibazumab, an Inhibiting Monoclonal Antibody.
Article in EBioMedicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 47 citations in OpenAlex.
- Monoclonal Antibodies Targeting Bacterial Infections: A Broad Review of the Field.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026Review
- Dual-mode ClfA-targeting DARPin biologics protect against diverse methicillin-resistantbioRxiv : the preprint server for biology · 2026Article
- Article
- Structure of ClfA002 in Complex With Neutralizing Antibody AZD7745 Provides Insight into Its Broad Neutralization Mechanism in Staphylococcus aureus Infection.The Journal of infectious diseases · 2025Article
- Click display: a rapid and efficient in vitro protein display method for directed evolution.Nucleic acids research · 2023Article
- The Two-Track Investigation of Fibronectin Binding Protein A ofInternational journal of molecular sciences · 2023Article
- Functional diversity of staphylococcal surface proteins at the host-microbe interface.Frontiers in microbiology · 2023Review
- Adhesive Virulence Factors ofACS bio & med chem Au · 2022Article
- Review
- Allantodapsone is a Pan-Inhibitor of Staphylococcus aureus Adhesion to Fibrinogen, Loricrin, and Cytokeratin 10.Microbiology spectrum · 2022Article
- Fibronectin binding protein B binds to loricrin and promotes corneocyte adhesion by Staphylococcus aureus.Nature communications · 2022Article
- Engineered human antibodies for the opsonization and killing ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Human monoclonal antibodies againsteLife · 2022Article
- Staphylococcus aureus vWF-binding protein triggers a strong interaction between clumping factor A and host vWF.Communications biology · 2021Article
- Staphylococcus lugdunensis: a Skin Commensal with Invasive Pathogenic Potential.Clinical microbiology reviews · 2021Review
- The Multivalent Role of Fibronectin-Binding Proteins A and B (FnBPA and FnBPB) ofFrontiers in microbiology · 2020Review
- Binding Strength of Gram-Positive Bacterial Adhesins.Frontiers in microbiology · 2020Review
- Surface Proteins ofMicrobiology spectrum · 2019Review
- Sortases, Surface Proteins, and Their Roles inMicrobiology spectrum · 2019Article
- Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The Staphylococcus aureus fibrinogen binding MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules), ClfA (clumping factor A) is an important virulence factor in staphylococcal infections and a component of several vaccines currently under clinical evaluation. The mouse monoclonal antibody aurexis (also called 12-9), and the humanized version tefibazumab are therapeutic monoclonal antibodies targeting ClfA that in combination with conventional antibiotics were effective in animal models but showed less impressive efficacy in a limited Phase II clinical trial. We here report the crystal structure and a biochemical characterization of the ClfA/tefibazumab (Fab) complex. The epitope for tefibazumab is located to the "top" of the N3 subdomain of ClfA and partially overlaps with a previously unidentified second binding site for fibrinogen. A high-affinity binding of ClfA to fibrinogen involves both an interaction at the N3 site and the previously identified docking of the C-terminal segment of the fibrinogen γ-chain in the N2N3 trench. Although tefibazumab binds ClfA with high affinity we observe a modest IC
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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.