ArticleMolecules and cells2020
Moieties of Complement iC3b Recognized by the I-domain of Integrin αXβ2.
Article in Molecules and cells, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- Glycoproteomic and genetic analysis of N-glycosylation of complement component C3 reveals immune pathway regulation.Genome biology · 2026Article
- Therapeutic strategies targeting complement in myasthenia gravis patients.Journal of neurology · 2025Review
- Determining Ligand Binding and Specificity Within the βBiomolecules · 2025Article
- Enhancing AAV-microdystrophin gene therapy after repeat dosing by blocking phagocytosis.Frontiers in immunology · 2025Article
- C3-dependent effector functions of complement.Immunological reviews · 2023Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement fragment iC3b serves as a major opsonin for facilitating phagocytosis via its interaction with complement receptors CR3 and CR4, also known by their leukocyte integrin family names, αMβ2 and αXβ2, respectively. Although there is general agreement that iC3b binds to the αM and αX I-domains of the respective β2-integrins, much less is known regarding the regions of iC3b contributing to the αX I-domain binding. In this study, using recombinant αX I-domain, as well as recombinant fragments of iC3b as candidate binding partners, we have identified two distinct binding moieties of iC3b for the αX I-domain. They are the C3 convertase-generated N-terminal segment of the C3b α'- chain (α'NT) and the factor I cleavage-generated N-terminal segment in the CUBf region of α-chain. Additionally, we have found that the CUBf segment is a novel binding moiety of iC3b for the αM I-domain. The CUBf segment shows about a 2-fold higher binding activity than the α'NT for αX I-domain. We also have shown the involvement of crucial acidic residues on the iC3b side of the interface and basic residues on the I-domain side.
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