Two 'heavy' (long) polypeptide chains bonded by disulfide bonds to two 'light' (short) polypeptide chains
Each polypeptide chain has a constant region and variable region
Constant regions
Do not vary within a class (isotype) of antibodies but do vary between the classes. Determine the mechanism used to destroy the antigens
Classes of mammalian antibodies
5 classes, each with different roles
Variable regions
Amino acid sequence in the variable regions of the antibodies (the tips of the "Y") are different for each antibody. Where the antibody attaches to the antigen to form an antigen-antibody complex
Antigen-binding site
Composed of 110 to 130 amino acids, includes both the ends of the light and heavy chains. Specific to the epitope (the part of the antigen that binds to the antibody)
A pathogen or virus may present multiple antigens meaning different antibodies need to be produced
Hinge region
Gives flexibility to the antibody molecule which allows the antigen-binding site to be placed at different angles when binding to antigens
Antibodies
Produced by B-lymphocytes
Antibodies
Bind to specific antigens that trigger the specific immune response. Every antigen has one antibody
Antigens
Pathogens and their toxins
Pollen
Blood cell surface molecules
Surface proteins found on transplanted tissues
Function of antibodies
Destroy pathogens within the body either directly, or by recruiting other immune cells
Ways antibodies function
Anti-toxins
Opsonins
Agglutinins
Anti-toxins
Antibodies can combine with viruses and toxins of pathogens (e.g. bacteria) to block them from entering or damaging cells
Opsonins
Antibodies can attach to bacteria making them readily identifiable to phagocytes, enabling phagocytosis
Agglutinins
Antibodies can attach to the flagella of bacteria making them less active, and cause pathogens carrying antigen-antibody complexes to clump together (agglutination)
Antibodies
Can create holes in the cell walls of pathogens causing them to burst (lysis) when water is absorbed by osmosis