ArticlemAbs2018
Structural investigation of human S. aureus-targeting antibodies that bind wall teichoic acid.
Article in mAbs, 2018. 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.
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
28 citing papers in PubMed, 36 citations in OpenAlex.
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- ImmunoPET with Zirconium-89 specifically detects postoperative biofilm-associated implant infections: a preclinical study.EJNMMI research · 2026Article
- Staphylococcus aureus: Antimicrobial resistance, quorum sensing, and antibiofilm approaches.European journal of microbiology & immunology · 2025Review
- Isotype conversion of Staphylococcal-specific IgG into IgM broadens the reactivity to other bacterial pathogens.Cell reports. Medicine · 2025Article
- Antibody dependent complement activation is critical for boosting opsonophagocytosis of Staphylococcus epidermidis in an extremely preterm human whole blood model.Scientific reports · 2025Article
- Single-cell Sequencing of Circulating Human Plasmablasts during Staphylococcus aureus Bacteremia.Journal of immunology (Baltimore, Md. : 1950) · 2024Article
- Human IgG Fc-engineering for enhanced plasma half-life, mucosal distribution and killing of cancer cells and bacteria.Nature communications · 2024Article
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- Anti-Hcp1 Monoclonal Antibody Is Protective againstPathogens (Basel, Switzerland) · 2023Article
- CD5L is a canonical component of circulatory IgM.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Human anti-C1q autoantibodies bind specifically to solid-phase C1q and enhance phagocytosis but not complement activation.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Outsmarting Pathogens with Antibody Engineering.Annual review of chemical and biomolecular engineering · 2023Review
- Anti-glycan monoclonal antibodies: Basic research and clinical applications.Current opinion in chemical biology · 2023Review
- Evaluating the Targeting of aInternational journal of molecular sciences · 2023Article
- Flow cytometry-based rapid detection ofRSC advances · 2022Article
- Catching Threads in Bacterial Cell Walls.ACS central science · 2022Article
- Antibody Recognition of DifferentACS central science · 2022Article
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- A homogeneous high-DAR antibody-drug conjugate platform combining THIOMAB antibodies and XTEN polypeptides.Chemical science · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infections caused by methicillin-resistant Staphylococcus aureus (MRSA) are a growing health threat worldwide. Efforts to identify novel antibodies that target S. aureus cell surface antigens are a promising direction in the development of antibiotics that can halt MRSA infection. We biochemically and structurally characterized three patient-derived MRSA-targeting antibodies that bind to wall teichoic acid (WTA), which is a polyanionic surface glycopolymer. In S. aureus, WTA exists in both α- and β-forms, based on the stereochemistry of attachment of a N-acetylglucosamine residue to the repeating phosphoribitol sugar unit. We identified a panel of antibodies cloned from human patients that specifically recognize the α or β form of WTA, and can bind with high affinity to pathogenic wild-type strains of S. aureus bacteria. To investigate how the β-WTA specific antibodies interact with their target epitope, we determined the X-ray crystal structures of the three β-WTA specific antibodies, 4462, 4497, and 6078 (Protein Data Bank IDs 6DWI, 6DWA, and 6DW2, respectively), bound to a synthetic WTA epitope. These structures reveal that all three of these antibodies, while utilizing distinct antibody complementarity-determining region sequences and conformations to interact with β-WTA, fulfill two recognition principles: binding to the β-GlcNAc pyranose core and triangulation of WTA phosphate residues with polar contacts. These studies reveal the molecular basis for targeting a unique S. aureus cell surface epitope and highlight the power of human patient-based antibody discovery techniques for finding novel pathogen-targeting therapeutics.
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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.