ArticleJournal of immunology (Baltimore, Md. : 1950)2015
Factor H-related protein 5 interacts with pentraxin 3 and the extracellular matrix and modulates complement activation.
Article in Journal of immunology (Baltimore, Md. : 1950), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 83 citations in OpenAlex.
- Association of FHR5 With Disease Severity in ANCA-Associated Vasculitis.Kidney international reports · 2026Article
- Decoding the Factor H-Related Proteins: Gatekeepers of Complement Dysregulation in AMD.European journal of immunology · 2026Review
- A novel fusion protein reduces kidney complement in experimental C3 glomerulopathy.Clinical and experimental immunology · 2026Article
- Functional and structural characterization of mouse Factor H-related B protein unveils a novel dimerization domain shared by FHR-B and FH.Frontiers in immunology · 2025Article
- The human factor H protein family - an update.Frontiers in immunology · 2024Review
- Role of factor H-related protein 3 inFrontiers in immunology · 2024Article
- Elevated plasma complement factor H related 5 protein is associated with venous thromboembolism.Nature communications · 2023Article
- The role of fibromodulin in inflammatory responses and diseases associated with inflammation.Frontiers in immunology · 2023Review
- Structural insights into the biological functions of the long pentraxin PTX3.Frontiers in immunology · 2023Review
- The diagnostic effectiveness of serum sialic acid predicts both qualitative and quantitative prostate cancer in patients with prostate-specific antigen between 4 and 20 ng/mL.Frontiers in endocrinology · 2023Article
- The Factor H protein family: The switchers of the complement alternative pathway.Immunological reviews · 2023Review
- Factor H related proteins modulate complement activation on kidney cells.Kidney international · 2022Article
- PathogenicInfection and immunity · 2022Article
- Complement Factor H-Related Proteins FHR1 and FHR5 Interact With Extracellular Matrix Ligands, Reduce Factor H Regulatory Activity and Enhance Complement Activation.Frontiers in immunology · 2022Article
- Overactivation of the complement system may be involved in intrarenal arteriolar lesions in IgA nephropathy.Frontiers in medicine · 2022Article
- Systems Biology Modeling of the Complement System Under Immune Susceptible Pathogens.Frontiers in physics · 2021Article
- Serum complement proteomics reveal biomarkers for hypertension disorder of pregnancy and the potential role of Clusterin.Reproductive biology and endocrinology : RB&E · 2021Article
- Gain-of-function factor H-related 5 protein impairs glomerular complement regulation resulting in kidney damage.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Low factor H-related 5 levels contribute to infection-triggered haemolytic uraemic syndrome and membranoproliferative glomerulonephritis.Clinical kidney journal · 2021Article
- Analysis of complement deposition and processing on Chlamydia trachomatis.Medical microbiology and immunology · 2021Article
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Authors and funding
13 authors at 7 institutions in 4 countries.
Funding
Abstract
The physiological roles of the factor H (FH)-related proteins are controversial and poorly understood. Based on genetic studies, FH-related protein 5 (CFHR5) is implicated in glomerular diseases, such as atypical hemolytic uremic syndrome, dense deposit disease, and CFHR5 nephropathy. CFHR5 was also identified in glomerular immune deposits at the protein level. For CFHR5, weak complement regulatory activity and competition for C3b binding with the plasma complement inhibitor FH have been reported, but its function remains elusive. In this study, we identify pentraxin 3 (PTX3) as a novel ligand of CFHR5. Binding of native CFHR5 to PTX3 was detected in human plasma and the interaction was characterized using recombinant proteins. The binding of PTX3 to CFHR5 is of ∼2-fold higher affinity compared with that of FH. CFHR5 dose-dependently inhibited FH binding to PTX3 and also to the monomeric, denatured form of the short pentraxin C-reactive protein. Binding of PTX3 to CFHR5 resulted in increased C1q binding. Additionally, CFHR5 bound to extracellular matrix in vitro in a dose-dependent manner and competed with FH for binding. Altogether, CFHR5 reduced FH binding and its cofactor activity on pentraxins and the extracellular matrix, while at the same time allowed for enhanced C1q binding. Furthermore, CFHR5 allowed formation of the alternative pathway C3 convertase and supported complement activation. Thus, CFHR5 may locally enhance complement activation via interference with the complement-inhibiting function of FH, by enhancement of C1q binding, and by activating complement, thereby contributing to glomerular disease.
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