ArticleThe Journal of biological chemistry2010
Complement protein C1q forms a complex with cytotoxic prion protein oligomers.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 36 citations in OpenAlex.
- Innate Immune Mechanisms in the Central Nervous System.Advances in experimental medicine and biology · 2025Review
- Article
- Neuronal transcriptome, tau and synapse loss in Alzheimer's knock-in mice require prion protein.Alzheimer's research & therapy · 2023Article
- Membrane attack complexes, endothelial cell activation, and direct allorecognition.Frontiers in immunology · 2022Review
- Nanobodies Provide Insight into the Molecular Mechanisms of the Complement Cascade and Offer New Therapeutic Strategies.Biomolecules · 2021Review
- Posttranslational modifications define course of prion strain adaptation and disease phenotype.The Journal of clinical investigation · 2020Article
- Formation of Protein Corona on Nanoparticle Affects Different Complement Activation Pathways Mediated by C1q.Pharmaceutical research · 2019Article
- Congo Red and amyloids: history and relationship.Bioscience reports · 2019Review
- C1 Complex: An Adaptable Proteolytic Module for Complement and Non-Complement Functions.Frontiers in immunology · 2017Review
- Low activity of complement in the cerebrospinal fluid of the patients with various prion diseases.Infectious diseases of poverty · 2016Article
- Structural and Functional Characterization of a Single-Chain Form of the Recognition Domain of Complement Protein C1q.Frontiers in immunology · 2016Article
- Analysis of the Interaction between Globular Head Modules of Human C1q and Its Candidate Receptor gC1qR.Frontiers in immunology · 2016Article
- Emerging and Novel Functions of Complement Protein C1q.Frontiers in immunology · 2015Review
- Mechanisms of action of therapeutic amyloidogenic hexapeptides in amelioration of inflammatory brain disease.The Journal of experimental medicine · 2014Article
- Global protein differential expression profiling of cerebrospinal fluid samples pooled from Chinese sporadic CJD and non-CJD patients.Molecular neurobiology · 2014Article
- Article
- The human c1q globular domain: structure and recognition of non-immune self ligands.Frontiers in immunology · 2011Article
- Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A growing number of studies have investigated the interaction between C1q and PrP, but the oligomeric form of PrP involved in this interaction remains to be determined. Aggregation of recombinant full-length murine PrP in the presence of 100 mm NaCl allowed us to isolate three different types of oligomers by size-exclusion chromatography. In contrast to PrP monomers and fibrils, these oligomers activate the classical complement pathway, the smallest species containing 8-15 PrP protomers being the most efficient. We used Thioflavine T fluorescence to monitor PrP aggregation and showed that, when added to the reaction, C1q has a cooperative effect on PrP aggregation and leads to the formation of C1q-PrP complexes. In these complexes, C1q interacts through its globular domains preferentially with the smallest oligomers, as shown by electron microscopy, and retains the ability to activate the classical complement pathway. Using two cell lines, we also provide evidence that C1q inhibits the cytotoxicity induced by the smallest PrP oligomers. The cooperative interaction between C1q and PrP could represent an early step in the disease, where it prevents elimination of the prion seed, leading to further aggregation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.