ArticleProceedings of the National Academy of Sciences of the United States of America2000
Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.
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Who cites it
203 citing papers in PubMed, 516 citations in OpenAlex.
- Physiological IgM class catalytic antibodies selective for transthyretin amyloid.The Journal of biological chemistry · 2014Trial
- Constitutive production of catalytic antibodies to a Staphylococcus aureus virulence factor and effect of infection.The Journal of biological chemistry · 2012Trial
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- Molecular basis and therapeutic potential of sortase A inhibitors as new antibiotics against MDR pathogens.Open biology · 2026Review
- Modulating pressure in the Orbitrap improves sensitivity and mass resolution in charge detection mass spectrometry.Nature communications · 2026Article
- An Optimized and Systematically Integrated Expression, Extraction, and Purification Strategy Enabling Efficient Production of TCR-Like Antibodies in Escherichia coli.Current microbiology · 2026Article
- Structural insights into antibody responses against influenza A virus in its natural reservoir.bioRxiv : the preprint server for biology · 2026Article
- A viral glycoprotein targets IgGEMBO molecular medicine · 2026Article
- Examining the role of IgA in a persistent model of Staphylococcus aureus colonization.PLoS pathogens · 2026Article
- Full-Length Context Disrupts Folding of IgG-Binding Domains of Protein A.bioRxiv : the preprint server for biology · 2025Article
- Immunomodulatory Biomaterials for Bone and Soft Tissue Chronic Inflammation Diseases.Small science · 2025Review
- Article
- A review of targeted drug delivery with antibody-drug complexes.The Journal of pharmacology and experimental therapeutics · 2025Review
- Peptide Tags for Site-Selective Nonenzymatic Covalent Modification of Proteins.Journal of peptide science : an official publication of the European Peptide Society · 2025Review
- A synergistic generative-ranking framework for tailored design of therapeutic single-domain antibodies.Cell discovery · 2025Article
- Whole-genome sequencing and biofilm gene characterization in multidrug-Resistant Staphylococcus aureus clinical strains.Journal, genetic engineering & biotechnology · 2025Article
- Conserved heavy/light contacts and germline preferences revealed by a large-scale analysis of natively paired human antibody sequences and structural data.Communications biology · 2025Article
- A Novel Interaction of Staphylococcal Protein A With Human Fibronectin and Its Implications in Host Cell Adhesion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025Article
- A comprehensive antigen-antibody complex database unlocking insights into interaction interface.eLife · 2025Article
- A SpA+LukAB vaccine targeting Staphylococcus aureus evasion factors restricts infection in two minipig infection models.NPJ vaccines · 2025Article
143 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
Abstract
Staphylococcus aureus produces a virulence factor, protein A (SpA), that contains five homologous Ig-binding domains. The interactions of SpA with the Fab region of membrane-anchored Igs can stimulate a large fraction of B cells, contributing to lymphocyte clonal selection. To understand the molecular basis for this activity, we have solved the crystal structure of the complex between domain D of SpA and the Fab fragment of a human IgM antibody to 2.7-A resolution. In the complex, helices II and III of domain D interact with the variable region of the Fab heavy chain (V(H)) through framework residues, without the involvement of the hypervariable regions implicated in antigen recognition. The contact residues are highly conserved in human V(H)3 antibodies but not in other families. The contact residues from domain D also are conserved among all SpA Ig-binding domains, suggesting that each could bind in a similar manner. Features of this interaction parallel those reported for staphylococcal enterotoxins that are superantigens for many T cells. The structural homology between Ig V(H) regions and the T-cell receptor V(beta) regions facilitates their comparison, and both types of interactions involve lymphocyte receptor surface remote from the antigen binding site. However, T-cell superantigens reportedly interact through hydrogen bonds with T-cell receptor V(beta) backbone atoms in a primary sequence-independent manner, whereas SpA relies on a sequence-restricted conformational binding with residue side chains, suggesting that this common bacterial pathogen has adopted distinct molecular recognition strategies for affecting large sets of B and T lymphocytes.
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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.