Detection of Autoantibodies to Complement Components by Surface Plasmon Resonance-Based Technology

Noé, Rémi; Chauvet, Sophie; Togarsimalemath, Shambhuprasad Kotresh; Marinozzi, Maria Chiara; Radanova, Maria; Vasilev, Vasil; Frémeaux‐Bacchi, Véronique; Dragon-Durey, Marie-Agnès; Roumenina, Lubka T.

doi:10.1007/978-1-4939-8949-2_24

Cited by 4 publications

(2 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Nowadays the presence of anti-C3 activation fragments Ab can be detected routinely by ELISA (31–34, 40). More in depth characterization of the binding is done by surface plasmon resonance (SPR), allowing evaluation of the antigen-antibody interaction in real time as well as running functional tests for the formation, and regulation of the C3 convertase (33, 40, 49).…”

Section: Methods Of Detection and Binding Epitopesmentioning

confidence: 99%

See 1 more Smart Citation

Autoantibodies Against C3b—Functional Consequences and Disease Relevance

et al. 2019

Self Cite

View full text Add to dashboard Cite

The complement component C3 is at the heart of the complement cascade. It is a complex protein, which generates different functional activated fragments (C3a, C3b, iC3b, C3c, C3d). C3b is a constituent of the alternative pathway C3 convertase (C3bBb), binds multiple regulators, and receptors, affecting thus the functioning of the immune system. The activated forms of C3 are a target for autoantibodies. This review focuses on the discovery, disease relevance, and functional consequences of the anti-C3b autoantibodies. They were discovered about 70 years ago and named immunoconglutinins. They were found after infections and considered convalescent factors. At the end of the twentieth century IgG against C3b were found in systemic lupus erythematosus and recently in lupus nephritis, correlating with the disease severity and flare. Cases of C3 glomerulopathy and immune complex glomerulonephritis were also reported. These antibodies recognize epitopes, shared between C3(H2O)/C3b/iC3b/C3c and have overt functional activity. They correlate with low plasmatic C3 levels in patients. In vitro, they increase the activity of the alternative pathway C3 convertase, without being C3 nephritic factors. They perturb the binding of the negative regulators Complement Receptor 1 and Factor H. The clear functional consequences and association with disease severity warrant further studies to establish the link between the anti-C3b autoantibodies and tissue injury. Comparative studies with such antibodies, found in patients with infections, may help to uncover their origin and epitopes specificity. Patients with complement overactivation due to presence of anti-C3b antibodies may benefit from therapeutic targeting of C3.

show abstract

Section: Methods Of Detection and Binding Epitopesmentioning

confidence: 99%

“…Interestingly, these Ab differed also in terms of the stability of the formed complexes with C3b. The ones from C3G/IC-GN showed a rapid association but fast dissociation, while the C3-Ab from LN had a slow association rate but formed more stable complexes (49). This may explain in part the apparent functional differences.…”

Section: Functional Consequencesmentioning

confidence: 99%