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This gene encodes complement factor B, a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Upon activation of the alternative pathway, it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a ...
In the alternative pathway, C3b binds to Factor B. Factor D releases Factor Ba from Factor B bound to C3b. The complex of C3b(2)Bb is a protease which cleaves C5 into C5b and C5a. C5 convertase is also formed by the classical pathway when C3b binds C4b and C2b. C5a is an important chemotactic protein, helping recruit inflammatory cells.
This change in shape allows the binding of plasma protein Factor B, which allows Factor D to cleave Factor B into Ba and Bb. Bb remains bound to C3(H 2 O) to form C3(H 2 O)Bb. This complex is also known as a fluid-phase C3-convertase. This convertase, the alternative pathway C3-convertase, although only produced in small amounts, can cleave ...
Factor B then binds to C3b and is cleaved by a plasma serine protease Factor D. The C3bBb complex (= alternative pathway C3 convertase) remains attached to the cell-surface. This complex might interact with another C3b and thus form the alternative pathway C5 convertase. [4] CVFBb is a noncovalent association product of CVF3 and the complement ...
The C1 complement complex binds to these antibodies resulting in its activation via cross proteolysis. This activated C1 complex cleaves C4 and C2 forming a C4bC2b complex that covalently bonds to the surface of the microbe and functions as a C3 convertase, binding and cleaving C3 into C3a and C3b.
Properdin (Factor P) is the only known positive regulator of complement activation that stabilizes the alternative C3 convertase (C3bBb). Properdin deficient individuals are sensitive to pyogenic infections. Properdin also promotes association of C3b with Factor B and thus it inhibits the Factor H mediated cleavage of C3b by Factor I. [6]
Cleavage of Arg-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg- bond in complement component C5 alpha-chain to yield C5a and C5b. This enzyme is a bimolecular complex of complement fragment Bb with either C3b or cobra venom factor.
Factor H can bind C3b much more easily in the presence of sialic acid, which is a component of most cells in the human body; conversely, in the absence of sialic acid, factor B can bind C3b more easily. This means that if C3b is bound to a "self" cell, the presence of sialic acid and the binding of factor H will prevent the complement cascade ...
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