ArticleProceedings of the National Academy of Sciences of the United States of America2004
Origin of the classical complement pathway: Lamprey orthologue of mammalian C1q acts as a lectin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 142 citations in OpenAlex.
- The Establishment of Complement System Is from Gene Duplication and Domain Shuffling.International journal of molecular sciences · 2024Article
- The role of complement in kidney disease.Nature reviews. Nephrology · 2023Review
- X-linked C1GALT1C1 mutation causes atypical hemolytic uremic syndrome.European journal of human genetics : EJHG · 2023Article
- Immune diversity in lophotrochozoans, with a focus on recognition and effector systems.Computational and structural biotechnology journal · 2023Review
- Balancing the View of C1q in Transplantation: Consideration of the Beneficial and Detrimental Aspects.Frontiers in immunology · 2022Article
- On Origin and Evolution of the Antibody Molecule.Biology · 2021Review
- The immune system of jawless vertebrates: insights into the prototype of the adaptive immune system.Immunogenetics · 2021Review
- Role of MafB in macrophages.Experimental animals · 2020Review
- Functional Characterization of OXYL, A SghC1qDC LacNAc-specific Lectin from The Crinoid Feather StarMarine drugs · 2019Article
- The Complement System of Agnathans.Frontiers in immunology · 2018Review
- Epidermal mucus, a major determinant in fish health: a review.Iranian journal of veterinary research · 2018Review
- MafB is a critical regulator of complement component C1q.Nature communications · 2017Article
- Keeping It All Going-Complement Meets Metabolism.Frontiers in immunology · 2017Review
- A pore-forming protein implements VLR-activated complement cytotoxicity in lamprey.Cell discovery · 2017Article
- Novel Evasion Mechanisms of the Classical Complement Pathway.Journal of immunology (Baltimore, Md. : 1950) · 2016Review
- Protective natural autoantibodies to apoptotic cells: evidence of convergent selection of recurrent innate-like clones.Annals of the New York Academy of Sciences · 2015Review
- mRNA-Seq and microarray development for the Grooved Carpet shell clam, Ruditapes decussatus: a functional approach to unravel host-parasite interaction.BMC genomics · 2013Article
- Protective autoantibodies in the rheumatic diseases: lessons for therapy.Nature reviews. Rheumatology · 2013Review
- Fundamental roles of the innate-like repertoire of natural antibodies in immune homeostasis.Frontiers in immunology · 2013Article
- MAPK phosphatase-1 is required for regulatory natural autoantibody-mediated inhibition of TLR responses.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The lectin complement pathway in innate immunity is closely related to the classical complement pathway in adaptive immunity, with respect to the structures and functions of their components. Both pathways are initiated by complexes consisting of collagenous proteins and serine proteases of the mannose-binding lectin (MBL)-associated serine protease (MASP)/C1r/C1s family. It has been speculated that the classical pathway emerged after the lectin pathway, and that the activation mechanism of the latter was partially conserved. The classical and lectin pathways can be traced back to at least cartilaginous fish and ascidian (urochordata), respectively. To elucidate the evolution of the complement system, we isolated and characterized a GlcNAc-binding lectin from sera of lamprey (agnathans), the most primitive vertebrate that lacks the classical pathway. Lamprey GlcNAc-binding lectin was an oligomer consisting of 24-kDa subunits. cDNA and phylogenetic analyses revealed that the lamprey GlcNAc-binding lectin is an orthologue of mammalian C1q, a collagenous subcomponent of the first component involved in binding to immunoglobulins in the classical pathway. Lamprey C1q copurified with MASP-A, a serine protease of the MASP/C1r/C1s family, which exhibited proteolytic activity against lamprey C3. Surface plasmon resonance analysis showed that lamprey C1q specifically bound to GlcNAc, but not various other carbohydrates tested. These results suggest that C1q may have emerged as a lectin and may have functioned as an initial recognition molecule of the complement system in innate immunity before the establishment of adaptive immunity such as immunoglobulins in the cartilaginous fish.
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