All three pathways merge at the proteolytic cleavage of component C3 by C3 convertases to form two fragments C3b and C3a. The cleavage of component C3 exposes a reactive thioester bond on C3b, leading to the covalent attachment of C3b to glycoproteins on the target cell surface (Law SK et al. 1979; Tack BF et al. 1980). The opsonization with C3b enables the recruitment of phagocytes (Newman SL et al. 1985; Gadjeva M et al. 1998). In addition, C3b anchors the assembly of C3/C5 convertases leading to an amplification of C3 cleavage and effecting C5 activation (Fearon DT 1979; Takata Y et al 1987; Kinoshita T et al. 1988). Moreover, the activation of C3b exposes binding sites for factors B, H and I, properdin, decay accelerating factor (DAF), membrane cofactor protein (MCP), complement receptor 1 (CR1) and microbial molecules such as vaccinia virus complement-control protein and staphylococcal complement inhibitor (SCIN) from Staphylococcus aureus (Forneris F et al. 2010; Morgan HP et al. 2011; Nilsson SC et al. 2010; Lambris JD et al. 1984; Medof ME et al.1984; Barilla-LaBarca ML et al. 2002; Smith BO et al. 2002; Bernet J et al. 2004; Garcia Bl et al. 2010) . C3b associates with these molecules to mediate the activation, amplification and regulation of the complement response.", "cellular_location": "extracellular region, plasma membrane", "input_participant_list": [], "output_participant_list": [], "enzyme_list": [ "P00751-1", "P06681-1" ], "evidence": [ { "id": "R-HSA-166817", "database": "Reactome", "url": "https://www.reactome.org/PathwayBrowser/#R-HSA-166817" } ] }, { "id": "R-HSA-173680", "name": "Activation of C5", "equation": "", "summary": "Cleavage of C5 by C5 convertases is the last enzymatic step in the complement activation. C5 convertases are formed when C3b molecule is covalently deposited in the immediate vicinity of pre-assembled C3 convertases switching them to C5 convertases C4bC2aC3b and C3bBbC3b (Takata Y et al 1987; Kinoshita T et al. 1988; Rawal N and Pangburn MK 2001, 2003). The additional C3b acts like an anvil for C5; it interacts with C5 and presents C5 in the correct conformation for cleavage by the C2a or Bb enzyme. The proteolytic cleavage of C5 generates the small fragment C5a and the large fragment C5b.
C5b initiates an assembly of terminal complement components (C6-C9) leading to the formation of membrane attack complex (MAC) on the target surface (Aleshin AE et al. 2012; Hadders MA et al. 2012). MAC disrupts the cell membrane causing a subsequent cell death through osmotic lysis.
Anaphylatoxin C5a mediates pro-inflammatory and immunemodulatory signals via its receptors C5aR and C5L2. The anaphylatoxin receptors are found on surfaces of phagocytes as well as other cell types. In inflammation, they induce cytokine production, degranulation and chemotaxis of leukocytes (Monk PN et al. 2007).
",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1",
"P06681-1"
],
"evidence": [
{
"id": "R-HSA-173680",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-173680"
}
]
},
{
"id": "R-HSA-173740",
"name": "Factor B binds to C3(H2O)",
"equation": "",
"summary": "Thioester bond hydrolysis causes conformational rearrangements that give C3(H2O) the ability to bind Factor B (Schreiber et al. 1978). The spontaneous hydrolysis rate of C3 under physiological conditions and temperature is about l% per hour, thus the C3b-like properties of C3(H2O) provide a continuous low level initiation of the alternative pathway of complement activation (Pangburn & Muller-Eberhard 1983).",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-173740",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-173740"
}
]
},
{
"id": "R-HSA-173745",
"name": "Factor D cleaves C3(H2O)-bound Factor B",
"equation": "",
"summary": "Factor D, a constitutively active serine protease found in trace amounts in the blood, cleaves a specific Arg-Lys bond in the Factor B component of the soluble C3(H2O):Factor B complex, yielding C3(H2O):Factor Bb and an inactive polypeptide, Factor Ba (Fearon and Austin 1975; Lesavre and Muller-Eberhard 1978; Lesavre et al. 1979; Schreiber et al. 1978).",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P51124-1",
"P00746-1",
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-173745",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-173745"
}
]
},
{
"id": "R-HSA-173754",
"name": "Properdin stabilizes C3b:Bb bound to cell surfaces",
"equation": "",
"summary": "C3b:Bb is naturally labile with a half-life of ~90 s; association of the complex with properdin extends the half-life to ~30 min. (Medicus et al. 1976). Properdin is found in the blood as a mixture of multivalent oligomers: 30% dimers, 45% trimers, 10% tetramers, and 15% higher oligomers. Monomers associate with one another in a head-to-tail arrangement, producing closed circular structures (Smith et al. 1984; Alcorlo M et al. 2013). These features suggest that the properdin oligomer associated with a C3b:Bb complex on a surface such as a cell membrane can facilitate recruitment of additional C3b:Bb complexes to the site (Farries et al. 1988; Hourcade 2006).",
"cellular_location": "external side of plasma membrane",
"input_participant_list": [
"R-HSA-173749",
"R-HSA-182548"
],
"output_participant_list": [],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-173754",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-173754"
}
]
},
{
"id": "R-HSA-174551",
"name": "Formation of alternative pathway C5 convertase",
"equation": "",
"summary": "The complex of C3b:Factor Bb, stabilized on the cell surface by properdin, catalyzes the cleavage of C3 to yield C3b and C3a. The C3b is recruited to the C3b:Factor B complex through its interaction with properdin (Daha et al. 1976; Medicus et al. 1976; Hourcade 2006), yielding the alternate C5 convertase.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [
"R-HSA-173752"
],
"output_participant_list": [
"R-HSA-166828"
],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-174551",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-174551"
}
]
},
{
"id": "R-HSA-183122",
"name": "Factor D cleaves C3b-bound Factor B",
"equation": "",
"summary": "Factor D, a constitutively active serine protease found in trace amounts in the blood, cleaves a specific Arg-Lys bond in the Factor B component of the cell surface-associated C3b:Factor B complex, yielding the alternate C3 convertase C3bBb on the surface and releasing an inactive polypeptide, Factor Ba (Lesavre and Muller-Eberhard 1978; Lesavre et al. 1979; Schreiber et al. 1978).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P51124-1",
"P00746-1",
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-183122",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-183122"
}
]
},
{
"id": "R-HSA-183126",
"name": "Factor B binds to surface-associated C3b",
"equation": "",
"summary": "C3b on a surface binds Factor B from solution to form a complex (Schreiber et al. 1978; Muller-Eberhard 1988).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-183126",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-183126"
}
]
},
{
"id": "R-HSA-183130",
"name": "C3(H2O):Factor Bb cleaves C3 to C3b and C3a",
"equation": "",
"summary": "C3(H2O):Factor Bb is a C3 convertase, sometimes referred to as the initial C3 convertase (iC3). The Factor Bb component catalyzes the hydrolysis of C3 to produce C3b and C3a. This reaction is not known to be directly coupled to the association of C3b complexes with a cell surface. It is believed that a small proportion of C3b spontaneously associates with the cell surface, otherwise it is rapidly inactivated (Muller-Eberhard 1988).",
"cellular_location": "extracellular region",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-183130",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-183130"
}
]
},
{
"id": "R-HSA-977363",
"name": "Factor H binds to C3bBb",
"equation": "",
"summary": "Factor H (CFH) binds to C3bBb, leading to displacement of Bb. Complement factor H-related protein 3 (FHR3) has also been reported to bind C3Bb leading to inhibition of C3Bb C3 convertase activity (Fritsche et al. 2010). CFH also acts as a cofactor for the factor I-mediated proteolytic inactivation of C3b to iC3b.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-977363",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-977363"
}
]
},
{
"id": "R-HSA-977375",
"name": "CR1 binds C3bBb/C4bC2a",
"equation": "",
"summary": "Complement Receptor 1 (CR1) is a widely distributed cell surface protein that is a decay accelerating factor for the conventional (C4bC2a) and alternative (C3bBb) C3 convertases (Coico & Sunshine 2009).",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1",
"P06681-1"
],
"evidence": [
{
"id": "R-HSA-977375",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-977375"
}
]
},
{
"id": "R-HSA-977605",
"name": "Factor H displaces Bb",
"equation": "",
"summary": "Factor H (CFH) greatly accelerates the displacement (decay) of Complement factor Bb from C3b.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1"
],
"evidence": [
{
"id": "R-HSA-977605",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-977605"
}
]
},
{
"id": "R-HSA-977619",
"name": "CD55 (DAF) promotes C3bBb/C4bC2a dissociation",
"equation": "",
"summary": "Decay accelerating factor (DAF, CD55) is a widely distributed membrane protein. It accelerates the dissociation of C3bBb and C4C2a, thereby inhibiting the amplification of complement. DAF can bind C3b and Bb but must bind both for efficient decay acceleration. The regulatory function of DAF is believed to be inhibition of activated C3 convertase enzymes rather than binding of inactive proenzymes (Harris et al. 2007).",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1",
"P06681-1"
],
"evidence": [
{
"id": "R-HSA-977619",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-977619"
}
]
},
{
"id": "R-HSA-977629",
"name": "Displacement of C2a/Bb by CR1",
"equation": "",
"summary": "Complement Receptor 1 (CR1) displaces the activated enzyme components Bb and C2a from the conventional and alternative C3 convertases C4bC2a and C3bBb, respectivley.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1",
"P06681-1"
],
"evidence": [
{
"id": "R-HSA-977629",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-977629"
}
]
},
{
"id": "R-HSA-981535",
"name": "CD55 (DAF) binds C3bBb, C4bC2a",
"equation": "",
"summary": "Decay-accelerating-factor (DAF, CD55) is a membrane- bound complement regulatory protein that inhibits autologous complement cascade activation. It is expressed on all cells that are in close contact with serum complement proteins, but also on cells outside the vascular space and on tumour cells. DAF binds to C3bBb and C4bC2a on cell surfaces, accelerating their dissociation and thereby inhibiting the amplification of complement. DAF can bind C3b and Bb, and must bind both for efficient decay acceleration. Although it can bind the inactive proenzymes C3b and C4b, the regulatory function of DAF is believed to be inhibition of activated C3 convertase enzymes (Harris et al. 2007).;",
"cellular_location": "plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1",
"P06681-1"
],
"evidence": [
{
"id": "R-HSA-981535",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-981535"
}
]
},
{
"id": "R-HSA-981621",
"name": "C3 convertases spontaneously dissociate",
"equation": "",
"summary": "C3b:Bb is naturally labile with a half-life of ~90 s. unless bound to properdin on the cell surface (Medicus et al. 1976). C4bC2a is also unstable, lasting at best a few minutes (Kerr et al. 1980). Decay is associated with the release of the Bb or C2a fragments respectively into the fluid phase. The liberated C3b/C4b is able to re-bind Bb/C2a if Factor B/C2 are present.",
"cellular_location": "extracellular region, plasma membrane",
"input_participant_list": [],
"output_participant_list": [],
"enzyme_list": [
"P00751-1",
"P06681-1"
],
"evidence": [
{
"id": "R-HSA-981621",
"database": "Reactome",
"url": "https://www.reactome.org/PathwayBrowser/#R-HSA-981621"
}
]
}
],
"reaction_participants": [
{
"participant_id": "R-HSA-166828",
"participant_name": "C3a [extracellular region]",
"crossref": [
{
"id": "2XWB",
"database": "PDB",
"url": ""
},
{
"id": "P01024",
"database": "ZINC target",
"url": ""
},
{
"id": "7NOZ",
"database": "PDB",
"url": ""
},
{
"id": "7AKK",
"database": "PDB",
"url": ""
},
{
"id": "7UE9",
"database": "PDB",
"url": ""
},
{
"id": "5O35",
"database": "PDB",
"url": ""
},
{
"id": "P01024",
"database": "Pharos - Targets",
"url": ""
},
{
"id": "2WII",
"database": "PDB",
"url": ""
},
{
"id": "3D5S",
"database": "PDB",
"url": ""
},
{
"id": "P01024",
"database": "GeneCards",
"url": ""
},
{
"id": "6RUR",
"database": "PDB",
"url": ""
},
{
"id": "5FO8",
"database": "PDB",
"url": ""
},
{
"id": "1W2S",
"database": "PDB",
"url": ""
},
{
"id": "2ICF",
"database": "PDB",
"url": ""
},
{
"id": "7QIV",
"database": "PDB",
"url": ""
},
{
"id": "3OXU",
"database": "PDB",
"url": ""
},
{
"id": "ENST00000245907",
"database": "Ensembl",
"url": ""
},
{
"id": "P01024",
"database": "PRO",
"url": ""
},
{
"id": "ENSG00000125730",
"database": "OpenTargets",
"url": ""
},
{
"id": "6RMU",
"database": "PDB",
"url": ""
},
{
"id": "4ZH1",
"database": "PDB",
"url": ""
},
{
"id": "17446",
"database": "Orphanet",
"url": ""
},
{
"id": "2QKI",
"database": "PDB",
"url": ""
},
{
"id": "3T4A",
"database": "PDB",
"url": ""
},
{
"id": "6EHG",
"database": "PDB",
"url": ""
},
{
"id": "2XWJ",
"database": "PDB",
"url": ""
},
{
"id": "7ZGK",
"database": "PDB",
"url": ""
},
{
"id": "4HW5",
"database": "PDB",
"url": ""
},
{
"id": "7PI6",
"database": "PDB",
"url": ""
},
{
"id": "1C3D",
"database": "PDB",
"url": ""
},
{
"id": "5FOA",
"database": "PDB",
"url": ""
},
{
"id": "3L5N",
"database": "PDB",
"url": ""
},
{
"id": "5FOB",
"database": "PDB",
"url": ""
},
{
"id": "2WIN",
"database": "PDB",
"url": ""
},
{
"id": "2A73",
"database": "PDB",
"url": ""
},
{
"id": "7TV9",
"database": "PDB",
"url": ""
},
{
"id": "7BAG",
"database": "PDB",
"url": ""
},
{
"id": "2ICE",
"database": "PDB",
"url": ""
},
{
"id": "3NMS",
"database": "PDB",
"url": ""
},
{
"id": "2XQW",
"database": "PDB",
"url": ""
},
{
"id": "3G6J",
"database": "PDB",
"url": ""
},
{
"id": "5O32",
"database": "PDB",
"url": ""
},
{
"id": "5FO7",
"database": "PDB",
"url": ""
},
{
"id": "6YO6",
"database": "PDB",
"url": ""
},
{
"id": "3L3O",
"database": "PDB",
"url": ""
},
{
"id": "2WY8",
"database": "PDB",
"url": ""
},
{
"id": "6RUV",
"database": "PDB",
"url": ""
},
{
"id": "4I6O",
"database": "PDB",
"url": ""
},
{
"id": "2I07",
"database": "PDB",
"url": ""
},
{
"id": "4ONT",
"database": "PDB",
"url": ""
},
{
"id": "5NBQ",
"database": "PDB",
"url": ""
},
{
"id": "3RJ3",
"database": "PDB",
"url": ""
},
{
"id": "ENSP00000245907",
"database": "Ensembl",
"url": ""
},
{
"id": "P01024",
"database": "UniProt",
"url": ""
},
{
"id": "NP_000055.2",
"database": "RefSeq",
"url": ""
},
{
"id": "3OHX",
"database": "PDB",
"url": ""
},
{
"id": "2WY7",
"database": "PDB",
"url": ""
},
{
"id": "1GHQ",
"database": "PDB",
"url": ""
},
{
"id": "2NOJ",
"database": "PDB",
"url": ""
},
{
"id": "2A74",
"database": "PDB",
"url": ""
},
{
"id": "6RMT",
"database": "PDB",
"url": ""
},
{
"id": "8HK2",
"database": "PDB",
"url": ""
},
{
"id": "4M76",
"database": "PDB",
"url": ""
},
{
"id": "2GOX",
"database": "PDB",
"url": ""
},
{
"id": "4HWJ",
"database": "PDB",
"url": ""
},
{
"id": "3OED",
"database": "PDB",
"url": ""
},
{
"id": "5FO9",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000125730-C3",
"database": "HPA",
"url": ""
},
{
"id": "3D5R",
"database": "PDB",
"url": ""
},
{
"id": "ENSG00000125730",
"database": "Ensembl",
"url": ""
},
{
"id": "6S0B",
"database": "PDB",
"url": ""
}
]
},
{
"participant_id": "R-HSA-173749",
"participant_name": "Cell surface:C3b:Bb [plasma membrane]",
"crossref": [
{
"id": "CPX-5601",
"database": "ComplexPortal",
"url": ""
}
]
},
{
"participant_id": "R-HSA-173752",
"participant_name": "Cell surface:C3b:Bb:Properdin [plasma membrane]",
"crossref": [
{
"id": "CPX-5602",
"database": "ComplexPortal",
"url": ""
}
]
},
{
"participant_id": "R-HSA-182548",
"participant_name": "Properdin oligomer [extracellular region]",
"crossref": [
{
"id": "36080",
"database": "ChEBI",
"url": ""
}
]
}
],
"reaction_enzymes": [
{
"uniprot_ac": "P00746",
"gene_name": "CFD",
"activity": [
{
"ec_number": "3.4.21.46",
"activity": "Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.",
"evidence": [
{
"id": "P00746",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00746"
}
]
},
{
"ec_number": "3.4.21.46",
"activity": "",
"evidence": [
{
"id": "P00746",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00746"
}
]
}
]
},
{
"uniprot_ac": "P00751",
"gene_name": "CFB",
"activity": [
{
"ec_number": "3.4.21.47",
"activity": "Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b.",
"evidence": [
{
"id": "P00751",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00751"
}
]
},
{
"ec_number": "3.4.21.47",
"activity": "",
"evidence": [
{
"id": "P00751",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P00751"
}
]
}
]
},
{
"uniprot_ac": "P06681",
"gene_name": "C2",
"activity": [
{
"ec_number": "3.4.21.43",
"activity": "Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.",
"evidence": [
{
"id": "P06681",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06681"
}
]
},
{
"ec_number": "3.4.21.43",
"activity": "",
"evidence": [
{
"id": "P06681",
"database": "UniProtKB",
"url": "https://www.uniprot.org/uniprot/P06681"
}
]
}
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