ArticleFrontiers in immunology2019
Neuropilin-1 Acts as a Receptor for Complement Split Products.
Article in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- A spatial atlas of the complement system uncovers unique expression patterns in postnatal brain development in mice.Nature communications · 2025Article
- C4d, a high-affinity LilrB2 ligand, is elevated in Alzheimer's disease and mediates synapse pruning.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Review
- New insights into neuropathology and pathogenesis of autoimmune glial fibrillary acidic protein meningoencephalomyelitis.Acta neuropathologica · 2024Article
- Interrogating ligand-receptor interactions using highly sensitive cellular biosensors.Nature communications · 2023Article
- Detailed Analysis of Simultaneous Renal and Liver Allografts in the Presence of DSA.Transplantation direct · 2023Article
- Semaphorin 3A in the Immune System: Twenty Years of Study.Biochemistry. Biokhimiia · 2022Review
- A widespread viral entry mechanism: The C-end Rule motif-neuropilin receptor interaction.Proceedings of the National Academy of Sciences of the United States of America · 2021Review
- Complement C4, Infections, and Autoimmune Diseases.Frontiers in immunology · 2021Review
- Complement C4A Regulates Autoreactive B Cells in Murine Lupus.Cell reports · 2020Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement split products (CSPs), such as the fragments C4d and C3d, which are generated as a consequence of complement regulatory processes, are established markers for disease activity in autoimmunity or antibody-mediated graft rejection. Since immunoglobulin-like transcript 4 (ILT4) was previously shown to interact with soluble CSPs, but not with CSPs covalently-bound to target surfaces following classical complement activation, the present study aimed to identify novel cellular receptors interacting with covalently-deposited CSPs. By applying an unbiased screening approach using a cDNA mammalian expression library generated from human monocyte-derived dendritic cells and probed with recombinant human C4d, we identified neuropilin-1 (NRP1) as a novel receptor for C4d, C3d, and iC3b. NRP1, a highly conserved type 1 transmembrane protein, plays important roles in the development of the nervous and cardiovascular system as well as in tumorigenesis through interaction with its established binding partners, such as vascular endothelial growth factor (VEGF) and semaphorin 3A (Sema3A). NRP1 is also expressed on immune cells and serves as a marker for murine Tregs. Although NRP1 contains domains homologous to ones found in some complement proteins, it has not been linked to the complement system. We demonstrate that binding of C4d to NRP1 expressing cells was dose-dependent and saturable, and had a K
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