ArticleThe Journal of biological chemistry2026
Atomistic scattering modeling of the solution structure of human dimeric IgA1 reveals a structural and mechanistic basis for IgA nephropathy.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
IgA nephropathy (IgAN) is characterized by mesangial deposition of J-chain containing dimeric IgA1 (dIgA1). Given that deposited IgA1 is mostly dIgA1, solution structure determinations of dIgA1 in phenotyped patients may be relevant to the pathogenesis of IgAN. Thus, dIgA1 from three IgAN patients and a healthy control was isolated. Biochemically, the dIgA1 structures were correlated with serum IgA-IgG immune complex levels, activated human mesangial cells interleukin-6 production, and the pattern of IgA1 N- and O-glycosylation. The degree of dIgA1 hinge O-glycosylation varied between the four subjects, being lower in IgAN subjects with an active renal biopsy Oxford score and clinically progressive IgAN. Their solution structures were investigated using analytical ultracentrifugation and small angle X-ray and neutron scattering. The increased O-glycosylation of the dIgA1 hinge was associated with larger X-ray radii of gyration R
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