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• W2477359722 startingPage "219" @default.
• W2477359722 abstract "This chapter focuses on interactions of immunoglobulins with molecules that react with sites located outside the antigen-combining site of immunoglobulins. Molecules of all immunoglobulin isotypes can interact through their Fc portions with cell Fc receptors (FcR), which are an important part of the immune system. Interaction of immunoglobulins and immune complexes with the complement components is important for activation and function of the complement system. There are several aspects of the complement-immunoglobulin interactions such as activation of C1 complement component by immunoglobulin M and immunoglobulin G (IgG) antibody binding, initiating the classical complement pathway; noncovalent binding of immunoglobulins with anaphylatoxins C3a, C4a, and C5a; and covalent linkage of C3b and C4b components with IgG. Several proteins react with the Fc portion of immunoglobulins such as clusterin, fibronectin, human plasma glycoprotein 60 (gp60), Fc-binding peptides, seminal plasma proteins, G-actin, placental alkaline phosphatase, and herpes simplex virus proteins. Proteins reacting with the Fab portion of immunoglobulins include prolactin, protein Fv, T-helper cell glycoprotein CD4, human immunodeficiency virus protein gp120, and lectins. Proteins capable of binding immunoglobulins in a nonimmune fashion are expressed on the surface of many microorganisms such as Streptococcal protein G, Staphylococcal protein A, and protein H. They are probably involved in the process of infection and are able to weaken the immune response." @default.
• W2477359722 created "2016-08-23" @default.
• W2477359722 creator A5041968085 @default.
• W2477359722 date "1998-01-01" @default.
• W2477359722 modified "2023-10-14" @default.
• W2477359722 title "Interactions Outside the Antigen-Combining Site" @default.
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