ArticleFrontiers in immunology2018
C1q and Mannose-Binding Lectin Interact with CR1 in the Same Region on CCP24-25 Modules.
Article in Frontiers in immunology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- LAIR1 prevents excess inflammatory tissue damage in Staphylococcus aureus skin infection and Cutaneous T-cell Lymphoma.JCI insight · 2025Article
- The Molecular Mechanisms of Complement Receptor 1-It Is Complicated.Biomolecules · 2023Review
- Mannan-Binding Lectin Promotes Murine Graft-versus-Host Disease by Amplifying Lipopolysaccharide-Initiated Inflammation.Transplantation and cellular therapy · 2022Article
- The Complement System in Metabolic-Associated Kidney Diseases.Frontiers in immunology · 2022Review
- Identification and development of a novel 5-gene diagnostic model based on immune infiltration analysis of osteoarthritis.Journal of translational medicine · 2021Article
- Review
- Insights into the ligand binding specificity of SREC-II (scavenger receptor expressed by endothelial cells).FEBS open bio · 2021Article
- Molecular Basis of Complement C1q Collagen-Like Region Interaction with the Immunoglobulin-Like Receptor LAIR-1.International journal of molecular sciences · 2021Article
- Collectins: Innate Immune Pattern Recognition Molecules.Advances in experimental medicine and biology · 2020Review
- Complement C1q Interacts With LRP1 Clusters II and IV Through a Site Close but Different From the Binding Site of Its C1r and C1s-Associated Proteases.Frontiers in immunology · 2020Article
- Complement system in Anti-CD20 mAb therapy for cancer: A mini-review.International journal of immunopathology and pharmacologyReview
- A novel soluble complement receptor 1 fragment with enhanced therapeutic potential.The Journal of biological chemistryArticle
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement receptor type 1 (CR1) is a multi modular membrane receptor composed of 30 homologous complement control protein modules (CCP) organized in four different functional regions called long homologous repeats (LHR A, B, C, and D). CR1 is a receptor for complement-opsonins C3b and C4b and specifically interacts through pairs of CCP modules located in LHR A, B, and C. Defense collagens such as mannose-binding lectin (MBL), ficolin-2, and C1q also act as opsonins and are involved in immune clearance through binding to the LHR-D region of CR1. Our previous results using deletion variants of CR1 mapped the interaction site for MBL and ficolin-2 on CCP24-25. The present work aimed at deciphering the interaction of C1q with CR1 using new CR1 variants concentrated around CCP24-25. CR1 bimodular fragment CCP24-25 and CR1 CCP22-30 deleted from CCP24-25 produced in eukaryotic cells enabled to highlight that the interaction site for both MBL and C1q is located on the same pair of modules CCP24-25. C1q binding to CR1 shares with MBL a main common interaction site on the collagen stalks but also subsidiary sites most probably located on C1q globular heads, contrarily to MBL.
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