ArticleThe Biochemical journal2015
The solution structures of native and patient monomeric human IgA1 reveal asymmetric extended structures: implications for function and IgAN disease.
Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Atomistic scattering modeling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy.The Journal of biological chemistry · 2026Article
- N-Glycosylation of Antibodies: Biological Effects During Infections and Therapeutic Applications.Antibodies (Basel, Switzerland) · 2025Review
- Humoral immune responses primed by the alteration of gut microbiota were associated with galactose-deficient IgA1 production in IgA nephropathy.Frontiers in immunology · 2024Article
- A solution structure analysis reveals a bent collagen triple helix in the complement activation recognition molecule mannan-binding lectin.The Journal of biological chemistry · 2023Article
- Serological Measurement of Poly-IgA Immune Complex Levels in IgA Nephropathy and IgA Vasculitis.Bio-protocol · 2022Article
- 3D Structures of IgA, IgM, and Components.International journal of molecular sciences · 2021Review
- Propensity of IgA to self-aggregate via tailpiece cysteine-471 and treatment of IgA nephropathy using cysteamine.JCI insight · 2021Article
- Solution structures of human myeloma IgG3 antibody reveal extended Fab and Fc regions relative to the other IgG subclasses.The Journal of biological chemistry · 2021Article
- Functional human IgA targets a conserved site on malaria sporozoites.Science translational medicine · 2021Article
- Renal deposition and clearance of recombinant poly-IgA complexes in a model of IgA nephropathy.The Journal of pathology · 2021Article
- Solution structure of deglycosylated human IgG1 shows the role of CBiophysical journal · 2021Article
- The solution structure of the complement deregulator FHR5 reveals a compact dimer and provides new insights into CFHR5 nephropathy.The Journal of biological chemistry · 2020Article
- IgA: Structure, Function, and Developability.Antibodies (Basel, Switzerland) · 2019Review
- Atomistic Modeling of Scattering Curves for Human IgG1/4 Reveals New Structure-Function Insights.Biophysical journal · 2019Article
- Distinct Fcα receptorThe Journal of biological chemistry · 2019Article
- Two distinct conformations of factor H regulate discrete complement-binding functions in the fluid phase and at cell surfaces.The Journal of biological chemistry · 2018Article
- Identification of serum glycoprotein ligands for the immunomodulatory receptor blood dendritic cell antigen 2.Glycobiology · 2018Article
- Non-linearity of the collagen triple helix in solution and implications for collagen function.The Biochemical journal · 2017Article
- Investigating Structure and Dynamics of Proteins in Amorphous Phases Using Neutron Scattering.Computational and structural biotechnology journal · 2017Review
- Characterization of Monoclonal Antibody-Protein Antigen Complexes Using Small-Angle Scattering and Molecular Modeling.Antibodies (Basel, Switzerland) · 2017Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Native IgA1, for which no crystal structure is known, contains an O-galactosylated 23-residue hinge region that joins its Fab and Fc regions. IgA nephropathy (IgAN) is a leading cause of chronic kidney disease in developed countries. Because IgA1 in IgAN often has a poorly O-galactosylated hinge region, the solution structures of monomeric IgA1 from a healthy subject and three IgAN patients with four different O-galactosylation levels were studied. Analytical ultracentrifugation showed that all four IgA1 samples were monomeric with similar sedimentation coefficients, s(0)20,w. X-ray scattering showed that the radius of gyration (Rg) slightly increased with IgA1 concentration, indicating self-association, although their distance distribution curves, P(r), were unchanged with concentration. Neutron scattering indicated similar Rg values and P(r) curves, although IgA1 showed a propensity to aggregate in heavy water buffer. A new atomistic modelling procedure based on comparisons with 177000 conformationally-randomized IgA1 structures with the individual experimental scattering curves revealed similar extended Y-shaped solution structures for all four differentially-glycosylated IgA1 molecules. The final models indicated that the N-glycans at Asn(263) were folded back against the Fc surface, the C-terminal tailpiece conformations were undefined and hinge O-galactosylation had little effect on the solution structure. The solution structures for full-length IgA1 showed extended hinges and the Fab and Fc regions were positioned asymmetrically to provide ample space for the functionally-important binding of two FcαR receptors to its Fc region. Whereas no link between O-galactosylation and the IgA1 solution structure was detected, an increase in IgA1 aggregation with reduced O-galactosylation may relate to IgAN.
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