ArticlePLoS pathogens2010
Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens.
Article in PLoS pathogens, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed.
- Biomolecular Crystallisation Through Soft Templates and Seeding.Advances in biochemical engineering/biotechnology · 2026Review
- Relationship Between Cell Surface Viral Glycoprotein Expression and Resistance of Parainfluenza Virus Persistently Infected Cells to Complement-Mediated Lysis.Pathogens (Basel, Switzerland) · 2025Article
- Extended receptor repertoire of an adenovirus associated with human obesity.PLoS pathogens · 2025Article
- Identification and characterization of a novel human adenovirus type HAdV-D116.Frontiers in microbiology · 2025Article
- Two noncompeting human neutralizing antibodies targeting MPXV B6 show protective effects against orthopoxvirus infections.Nature communications · 2024Article
- Immunologic and Genetic Contributors to CD46-Dependent Immune Dysregulation.Journal of clinical immunology · 2023Article
- Structure of Bovine CD46 Ectodomain.Viruses · 2023Article
- Genetic variability shapes the alternative pathway complement activity and predisposition to complement-related diseases.Immunological reviews · 2023Review
- The immunobiology and clinical use of genetically engineered porcine hearts for cardiac xenotransplantation.Nature cardiovascular research · 2022Article
- Edwardsiella tarda TraT is an anti-complement factor and a cellular infection promoter.Communications biology · 2022Article
- CD46 Isoforms Influence the Mode of Entry by Human Herpesvirus 6A/B in T Cells.Journal of virology · 2022Article
- Article
- Genetic analysis of CFH and MCP in Egyptian patients with immune-complex proliferative glomerulonephritis.Frontiers in immunology · 2022Article
- Desmoglein 2 (DSG2) Is A Receptor of Human Adenovirus Type 55 Causing Adult Severe Community-Acquired Pneumonia.Virologica Sinica · 2021Article
- A Novel Homozygous In-Frame Deletion in Complement Factor 3 Underlies Early-Onset Autosomal Recessive Atypical Hemolytic Uremic Syndrome - Case Report.Frontiers in immunology · 2021Article
- Human adenovirus binding to host cell receptors: a structural view.Medical microbiology and immunology · 2020Review
- Real Time Analysis of Bovine Viral Diarrhea Virus (BVDV) Infection and Its Dependence on Bovine CD46.Viruses · 2020Article
- Molecular engineering of an efficient four-domain DAF-MCP chimera reveals the presence of functional modularity in RCA proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- C3 glomerulopathy - understanding a rare complement-driven renal disease.Nature reviews. Nephrology · 2019Review
- Diversity within the adenovirus fiber knob hypervariable loops influences primary receptor interactions.Nature communications · 2019Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors.
Funding
Abstract
The human membrane cofactor protein (MCP, CD46) is a central component of the innate immune system. CD46 protects autologous cells from complement attack by binding to complement proteins C3b and C4b and serving as a cofactor for their cleavage. Recent data show that CD46 also plays a role in mediating acquired immune responses, and in triggering autophagy. In addition to these physiologic functions, a significant number of pathogens, including select adenoviruses, measles virus, human herpes virus 6 (HHV-6), Streptococci, and Neisseria, use CD46 as a cell attachment receptor. We have determined the crystal structure of the extracellular region of CD46 in complex with the human adenovirus type 11 fiber knob. Extracellular CD46 comprises four short consensus repeats (SCR1-SCR4) that form an elongated structure resembling a hockey stick, with a long shaft and a short blade. Domains SCR1, SCR2 and SCR3 are arranged in a nearly linear fashion. Unexpectedly, however, the structure reveals a profound bend between domains SCR3 and SCR4, which has implications for the interactions with ligands as well as the orientation of the protein at the cell surface. This bend can be attributed to an insertion of five hydrophobic residues in a SCR3 surface loop. Residues in this loop have been implicated in interactions with complement, indicating that the bend participates in binding to C3b and C4b. The structure provides an accurate framework for mapping all known ligand binding sites onto the surface of CD46, thereby advancing an understanding of how CD46 acts as a receptor for pathogens and physiologic ligands of the immune system.
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