ArticleNature communications2018
The first transmembrane region of complement component-9 acts as a brake on its self-assembly.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Molecular mechanism of pore formation by Plasmodium Perforin-like Protein 2.Nature communications · 2026Article
- Excessive C5 conversion prevents C9 polymerisation and subsequent MAC-dependent killing of Klebsiella pneumoniae.PLoS pathogens · 2026Article
- Advances in cryo-EM that have shaped mechanistic models of membrane-attack-complex assembly and regulation.IUCrJ · 2026Review
- Design of miniprotein inhibitors targeting complement C9 to block membrane attack complex assembly.Nature communications · 2026Article
- CD59, Disulphide-Locked Human C9 and Horse C9 Inhibit Human Membrane Attack Complex Assembly by Similar Mechanisms.Immunology · 2025Article
- Action of the Terminal Complement Pathway on Cell Membranes.The Journal of membrane biology · 2025Review
- Targeting EGFR-TKI resistance in lung cancer: Role of miR-5193/miR-149-5p loaded NK-EVs and Carboplatin combination.International journal of pharmaceutics · 2025Article
- Structural basis for the pore-forming activity of a complement-like toxin.Science advances · 2025Article
- Exosomal-complement system activation in preeclampsia.The journal of obstetrics and gynaecology research · 2025Review
- Large and Stable Nanopores Formed by Complement Component 9 for Characterizing Single Folded Proteins.ACS nano · 2025Article
- Acinetobacter baumannii Clinical Isolates Resist Complement-Mediated Lysis by Inhibiting the Complement Cascade and Improperly Depositing MAC.Journal of innate immunity · 2025Article
- Klebsiella LPS O1-antigen prevents complement-mediated killing by inhibiting C9 polymerization.Scientific reports · 2024Article
- Distant relatives of a eukaryotic cell-specific toxin family evolved a complement-like mechanism to kill bacteria.Nature communications · 2024Article
- Proteomics and Its Applications in Cancers 2.0.International journal of molecular sciences · 2024Article
- Epitomics: Analysis of Plasma C9 Epitope Heterogeneity in the Plasma of Lung Cancer Patients and Control Subjects.International journal of molecular sciences · 2023Article
- Structural basis for membrane attack complex inhibition by CD59.Nature communications · 2023Article
- The neoepitope of the complement C5b-9 Membrane Attack Complex is formed by proximity of adjacent ancillary regions of C9.Communications biology · 2023Article
- Proteomics Analysis of Plasma-Derived Exosomes Unveils the Aberrant Complement and Coagulation Cascades in Dermatomyositis/Polymyositis.Journal of proteome research · 2023Article
- Article
- Comparative serum proteomic analysis of a selected protein panel in individuals with schizophrenia and bipolar disorder and the impact of genetic risk burden on serum proteomic profiles.Translational psychiatry · 2022Article
Corrections and comments
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Complement component 9 (C9) functions as the pore-forming component of the Membrane Attack Complex (MAC). During MAC assembly, multiple copies of C9 are sequentially recruited to membrane associated C5b8 to form a pore. Here we determined the 2.2 Å crystal structure of monomeric murine C9 and the 3.9 Å resolution cryo EM structure of C9 in a polymeric assembly. Comparison with other MAC proteins reveals that the first transmembrane region (TMH1) in monomeric C9 is uniquely positioned and functions to inhibit its self-assembly in the absence of C5b8. We further show that following C9 recruitment to C5b8, a conformational change in TMH1 permits unidirectional and sequential binding of additional C9 monomers to the growing MAC. This mechanism of pore formation contrasts with related proteins, such as perforin and the cholesterol dependent cytolysins, where it is believed that pre-pore assembly occurs prior to the simultaneous release of the transmembrane regions.
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