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Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]
C1q association eventually leads to the recruitment of complement C4b and C3b, both of which are recognized by complement receptor 1, 3, and 4 (CR1, CR3, CR4), which are present on most phagocytes. [4] In this way, the complement system participates in the adaptive immune response. Opsonization by C3b. CR1 recognizes C3b deposited on antigen
The "upper" part of an antibody.The complementarity-determining regions of the heavy chain are shown in red (. Complementarity-determining regions (CDRs) are polypeptide segments of the variable chains in immunoglobulins (antibodies) and T cell receptors, generated by B-cells and T-cells respectively.
[2] [16] Among the many functions of C1q, C1q triggers clearance of immune complexes and apoptotic cells by activating the classical pathway and binding directly onto phagocytes. [ 1 ] [ 17 ] Consequently, systemic lupus erythematosus from insufficient amounts of C1q is characterized by the accumulation of autoantibodies and apoptotic cells. [ 4 ]
After an antigen-antibody reaction, the immune complexes can be subject to any of a number of responses, including complement deposition, opsonization, [2] phagocytosis, or processing by proteases. Red blood cells carrying CR1 -receptors on their surface may bind C3b -coated immune complexes and transport them to phagocytes , mostly in liver ...
1) Antibodies (A) and pathogens (B) circular in the blood. 2) The antibodies bind to pathogens with complementary antigen sequences, engaging in opsonization (2a), neutralisation (2b), and agglutination (2c). 3) A phagocyte (C) approaches the pathogen, and Fc region (D) of the antibody binds to one of the Fc receptors (E) on the phagocyte.
The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
Recently another enzyme for generation of F(ab') 2 has been commercially available. The enzyme IdeS (Immunoglobulin degrading enzyme from Streptococcus pyogenes, trade name FabRICATOR) cleaves IgG in a sequence specific manner at neutral pH. The F(ab') 2 fragment can be split into two Fab' fragments by mild reduction. [1]