ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural basis for evasion of IgA immunity by Staphylococcus aureus revealed in the complex of SSL7 with Fc of human IgA1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
54 citing papers in PubMed.
- The protease code of the bacterial gut microbiota: ecological regulation, barrier disruption, and rewiring host defense and signaling.Gut microbes · 2026Review
- The Crystal Structure of Human IgD-Fc Reveals Unexpected Differences With Other Antibody Isotypes.Proteins · 2025Article
- Scabies.Nature reviews. Disease primers · 2024Review
- SIgA structures bound to Streptococcus pyogenes M4 and human CD89 provide insights into host-pathogen interactions.Nature communications · 2023Article
- Secretory IgA impacts the microbiota density in the human nose.Microbiome · 2023Article
- Exploring Immunome and Microbiome Interplay in Reproductive Health: Current Knowledge, Challenges, and Novel Diagnostic Tools.Seminars in reproductive medicine · 2023Review
- Isolation and functional analysis of phage-displayed antibody fragments targeting the staphylococcal superantigen-like proteins.MicrobiologyOpen · 2023Article
- Multiple Domains of Staphylococcal Superantigen-like Protein 11 (SSL11) Contribute to Neutrophil Inhibition.Biochemistry · 2022Article
- Sialylation as an Important Regulator of Antibody Function.Frontiers in immunology · 2022Review
- 3D Structures of IgA, IgM, and Components.International journal of molecular sciences · 2021Review
- Label-Free Method Development for Hydroxyproline PTM Mapping in Human Plasma Proteome.The protein journal · 2021Article
- Tissues: the unexplored frontier of antibody mediated immunity.Current opinion in virology · 2021Review
- A VFrontiers in plant science · 2021Article
- Article
- Secret(ory) revealed: the long-awaited structures of secretory IgA.Cell research · 2020Article
- Structural insights into secretory immunoglobulin A and its interaction with a pneumococcal adhesin.Cell research · 2020Article
- IgA and FcαRI: Versatile Players in Homeostasis, Infection, and Autoimmunity.ImmunoTargets and therapy · 2020Review
- IgA: Structure, Function, and Developability.Antibodies (Basel, Switzerland) · 2019Review
- Molecular determinants of the mechanism and substrate specificity ofThe Journal of biological chemistry · 2019Article
- Staphylococcal Superantigen-like protein 11 mediates neutrophil adhesion and motility arrest, a unique bacterial toxin action.Scientific reports · 2019Article
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
Infection by Staphylococcus aureus can result in severe conditions such as septicemia, toxic shock, pneumonia, and endocarditis with antibiotic resistance and persistent nasal carriage in normal individuals being key drivers of the medical impact of this virulent pathogen. In both virulent infection and nasal colonization, S. aureus encounters the host immune system and produces a wide array of factors that frustrate host immunity. One in particular, the prototypical staphylococcal superantigen-like protein SSL7, potently binds IgA and C5, thereby inhibiting immune responses dependent on these major immune mediators. We report here the three-dimensional structure of the complex of SSL7 with Fc of human IgA1 at 3.2 A resolution. Two SSL7 molecules interact with the Fc (one per heavy chain) primarily at the junction between the Calpha2 and Calpha3 domains. The binding site on each IgA chain is extensive, with SSL7 shielding most of the lateral surface of the Calpha3 domain. However, the SSL7 molecules are positioned such that they should allow binding to secretory IgA. The key IgA residues interacting with SSL7 are also bound by the leukocyte IgA receptor, FcalphaRI (CD89), thereby explaining how SSL7 potently inhibits IgA-dependent cellular effector functions mediated by FcalphaRI, such as phagocytosis, degranulation, and respiratory burst. Thus, the ability of S. aureus to subvert IgA-mediated immunity is likely to facilitate survival in mucosal environments such as the nasal passage and may contribute to systemic infections.
Indexed as
Identifiers
What OpenQuestion holds
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.