Antibodies

  • Produced by plasma cells; known collectively as immunoglobulins (Ig) and consist of two identical heavy chains and light chains linked by disulfide bonds
  • Each Ab with unique domain which recognizes and binds Ag epitope
  • Ab function: neutralize microbes/toxins by direct binding, through enhanced opsonization and/or lysis (latter via complement activation)
  • Different classes based on structure of heavy chain; Ig class switching regulated by cytokines derived from T cells
  •    
     
    Fc stands for fragment that spontaneous crystallizes
     
       
    Opsonizing Abs: IgG1/IgG3
  • Neutralizing Abs: IgA1/IgA2 (mucosal), IgG2/IgG4 (tissue)
  • Cleavage of immunoglobulin by papain results in two identical Fab fragments (antigen-binding fragment) and one Fc fragment (involved in complement activation and opsonization)
   
 
Table 1-16 Classes of Immunoglobulins
  IgCharacteristics
 IgA 
Dimer, predominantly in mucosal surfaces, can activate complement system via alternative pathway (not classical pathway)
 IgD 
Little known function; present as surface receptor on mature B cells
 IgE 
Classic anaphylactoid antibody; binds allergens and releases mast cell mediators; increased in atopic patients
 IgG 
Most abundant Ig; four subclasses (IgG1–IgG4) which differ in ability to activate complement, IgG1/IgG3 (potent activators) > IgG2 > IgG4 (weak to none), able to cross placenta, abundant production with secondary response, best for opsonizing/fixing complement
 IgM 
Pentamer (five Ig molecules), largest in size, major Ig production in primary immune response, most efficient at activating complement cascade, not involved in opsonization, does not cross placenta