ArticleNature communications2025
Calcium-dependent oligomerization of scavenger receptor CD163 facilitates the endocytosis of ligands.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Engineered haptoglobin β fusion protein targets myoglobin and ameliorates rhabdomyolysis-associated acute kidney injury.EMBO molecular medicine · 2026Article
- Cryo-EM provides insight into how thebioRxiv : the preprint server for biology · 2026Article
- Review
- Structural basis for hemoglobin scavenging by CD163 reveals mechanism of ligand promiscuity.PLoS biology · 2026Article
- Article
- Pigs with CD163 Mutation Conferred PRRSV Resistance.Animals : an open access journal from MDPI · 2026Article
- A Hemoglobin-Based Nanoparticle Delivery System Enhances the Pharmacokinetics and Efficacy of Tigecycline inBME frontiers · 2026Article
- Strength in numbers: how multimerization drives HpHb uptake by CD163 scavenging receptor.Nature communications · 2025Article
- Identification and validation of core biomarkers for sepsis: a comprehensive analysis using bioinformatics and machine learning.Frontiers in immunology · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
Scavenger receptor CD163 is a marker of M2 type macrophages that play important roles in anti-inflammatory processes. The most extensively studied function of CD163 is related to the elimination of hemoglobin-haptoglobin (Hb-Hp) complexes, to prevent potential oxidative toxicity of the iron-containing heme. However, the structural mechanism of CD163 in ligand binding and internalization remains elusive. Here, we present the cryo-electron microscopy structure of human Hb-Hp recognition by the full ectodomain of CD163. We illuminate that CD163 forms calcium-dependent oligomers and primarily exists as trimeric form under the condition of 2.5 mM calcium. It mainly utilizes two protomers to interact with Hb-Hp complex asymmetrically, while the third protomer of the trimer also has the potential to form calcium-mediated contacts with Hp. Flow cytometry analyses reveal that oligomerization of CD163 significantly enhances the efficiency of ligand endocytosis. These results advance our understanding of the role of CD163 in ligand scavenging.
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