ArticleThe EMBO journal2007
Structural insights into the innate immune recognition specificities of L- and H-ficolins.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
What it found
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The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
83 citing papers in PubMed, 193 citations in OpenAlex.
- Trial
- Acute heart failure following myocardial infarction: complement activation correlates with the severity of heart failure in patients developing cardiogenic shock.ESC heart failure · 2018Trial
- Heparin-coated cardiopulmonary bypass circuits selectively deplete the pattern recognition molecule ficolin-2 of the lectin complement pathway in vivo.Clinical and experimental immunology · 2015Trial
- Structural insights into glycan recognition by plant immune receptors: a comparative perspective with animal innate immune systems.The Plant journal : for cell and molecular biology · 2026Review
- Article
- Chemical Synthesis of Oligosaccharides Derived fromJournal of the American Chemical Society · 2025Article
- Tools for investigating host-microbe crosstalk using glycan analysis probes inspired by human lectins.Glycobiology · 2025Article
- Species differences in opsonization and phagocyte recognition of preclinical poly-2-alkyl-2-oxazoline-coated nanoparticles.Nature communications · 2025Article
- The Complement System.Advances in experimental medicine and biology · 2025Review
- Collectins and Ficolins.Advances in experimental medicine and biology · 2025Review
- Glycan analysis probes inspired by human lectins for investigating host-microbe crosstalk.bioRxiv : the preprint server for biology · 2024Article
- Soluble Human Lectins at the Host-Microbe Interface.Annual review of biochemistry · 2024Review
- Microfibril-associated glycoprotein 4 forms octamers that mediate interactions with elastogenic proteins and cells.Nature communications · 2024Article
- The Lectin Pathway of the Complement System-Activation, Regulation, Disease Connections and Interplay with Other (Proteolytic) Systems.International journal of molecular sciences · 2024Review
- The Role of Ficolins in Lung Injury.Journal of innate immunity · 2024Review
- Crystal structures of human immune protein FIBCD1 suggest an extended binding site compatible with recognition of pathogen-associated carbohydrate motifs.The Journal of biological chemistry · 2024Article
- Transcriptomics of mussel transmissible cancer MtrBTN2 suggests accumulation of multiple cancer traits and oncogenic pathways shared among bilaterians.Open biology · 2023Article
- Human oral lectin ZG16B acts as a cell wall polysaccharide probe to decode host-microbe interactions with oral commensals.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Balancing selection on the complement system of a wild rodent.BMC ecology and evolution · 2023Article
- α-Pinene: Docking Study, Cytotoxicity, Mechanism of Action, and Anti-Biofilm Effect againstAntibiotics (Basel, Switzerland) · 2023Article
23 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L- and H-ficolins are soluble oligomeric defence proteins with lectin-like activity, assembled from collagen fibers prolonged by fibrinogen-like recognition domains. The X-ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 A, respectively. Both domains have three-lobed structures with clefts separating the distal parts of the protomers. Ca(2+) ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc-binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L-ficolin, three additional binding sites (S2-S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3-beta-D-glucan, as found on microbial or apoptotic surfaces.
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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.