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Updated: Jun 2 2020


  • Overview
  • Introduction
    • Antibodies are immunologically active circulating proteins that
      • are composed of two heavy chains paired with two light chains
      • serve as a primary component of humoral immunity
      • are produced by B-cells that can further
        • differentiate into plasma cells that specialize in secreting antibodies
        • mature to make antibodies with higher affinity
        • remain dormant as memory cells
      • bind antigens from a wide variety of pathogens
      • are also known as immunoglobulins (Ig)
    • Antibodies are able to fight infections through multiple mechanisms including
      • opsonization of the surface of the pathogen leading to
        • phagocytosis by innate immune cells like macrophages
        • cytotoxicity by triggering release of toxic compounds by innate immune cells
      • neutralization of pathogens and viruses by
        • blocking interaction of pathogenic proteins with host receptors
        • inactivating virulence factors expressed by pathogens
      • activation of the complement cascade through the classical pathway
  • Antibody Structure
    • Antibodies are composed of two heavy chains paired with two light chains
    • Together these chains create distinct regions of the antibody such as
      • the constant fragment (Fc)
      • two identical variable antigen binding fragments (Fab)
    • These regions differ in both structure and function
      • Differences Between Antibody Regions
      • Feature
      • Antibody Binding (Fab)
      • Constant (Fc)
      • Composition
      • One heavy and one light chain
      • Linked by disulfide bonds
      • Two heavy chains
      • Linked by disulfide bonds
      • Attached to carbohydrate chains
      • Terminus
      • N-terminus of protein chains
      • C-terminus of protein chains
      • Function
      • Binds to antigen in specific manner
      • Binds to complement proteins
      • Binds to effector regions of innate immune cells
      • Variability
      • Site of idiotype diversity
      • Changed in affinity maturation
      • Unique for every antibody
      • Site of isotype diversity
      • Changed in isotype switching
      • 5 types that are shared among all antibodies
  • Antibody Variation and Diversity
    • Antibodies are able to fight an incredible range of infections because of
      • idiotype diversity which
        • governs what antigens can be recognized by antibodies
        • is generated by multiple diversity mechanisms including
          • random recombination of VDJ regions of antibody coding regions
          • random addition of nucleotides to hypervariable regions by TdT
          • random assortment of heavy chains with light chains
          • affinity maturation through somatic hypermutation after antigen exposure
        • ensures that any moiety can be recognized by the variable region of an antibody
      • isotype diversity through five types of constant regions
      • Antibody Isotypes
      • Feature
      • IgA
      • IgD
      • IgE
      • IgM
      • IgG
      • Constant chain type
      • α chain
      • δ chain
      • ε chain
      • μ chain
      • γ chain
      • Concentration
      • High in mucus membranes and in secretions
      • Low
      • Low
      • High in serum during early response
      • High in serum during late response
      • Valence
      • Dimer
      • Monomer
      • Monomer
      • Pentamer
      • Monomer
      • Function
      • Mucosal immunity
      • Transported into mucosal lumens by poly Ig
      • Present on B-cell surfaces
      • Unclear role
      • Defense against parasites
      • Mediates allergies
      • Low affinity
      • Main antibody in early response
      • High affinity
      • Main antibody in late response
      • Recognized by
      • Innate immune cells
      • Complement
      • Unknown
      • Mast cells
      • Basophils
      • Innate immune cells
      • Phagocytes
      • Complement
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