ArticleNature communications2025
Scavenger receptor CD163 multimerises to allow uptake of diverse 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 8 papers.
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Who cites it
8 citing papers in PubMed.
- 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
- Macrophage Cluster of Differentiation 163 promotes post-infarction cardiac repair and preserves left ventricular function via osteopontin.Clinical and translational medicine · 2026Article
- Impact of clarithromycin on monocytes-macrophages in patients with coronary arterial disease: a crucial study in cardiovascular research.Molecular biology reports · 2026Article
- Strength in numbers: how multimerization drives HpHb uptake by CD163 scavenging receptor.Nature communications · 2025Article
- Structural elucidation of the haptoglobin-hemoglobin clearance mechanism by macrophage scavenger receptor CD163.PLoS biology · 2025Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
CD163 is an archetypal scavenger receptor and mediates detoxification of free haemoglobin. Release of haemoglobin from lysed erythrocytes causes oxidative tissue and organ damage. Detoxification involves haemoglobin binding to the abundant serum protein haptoglobin, followed by CD163-mediated uptake of stoichiometrically diverse haptoglobin-haemoglobin complexes into macrophages for degradation. We show that CD163 adopts dimeric and trimeric assemblies due to calcium-mediated interactions within a membrane-associated base. Arms protrude from this base and create a ligand-binding site. Flexibility within the base, coupled with multiple small ligand-binding surfaces on each arm, allow the receptor to mould around its ligands, resulting in promiscuous uptake of ligands with different structures and stoichiometries. Monomeric CD163 lacks this ability to internalise lower-avidity ligands. Arms from adjacent protomers can also self-associate, blocking ligand-binding surfaces in an autoinhibited state. Therefore, through calcium-dependent multimer formation and flexible ligand binding, CD163 scavenges ligands with different structures and avidities, mediating haemoglobin detoxification.
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Registered trials
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