Humoral immunity is the aspect of immunity that is mediated by macromolecules – including secreted antibodies, complement proteins, and certain antimicrobial peptides – located in extracellular fluids. Humoral immunity is named so because it involves substances found in the humorism, or . It contrasts with cell-mediated immunity. Humoral immunity is also referred to as antibody-mediated immunity.
The study of the molecular and cellular components that form the immune system, including their function and interaction, is the central science of immunology. The immune system is divided into a more primitive innate immune system and an acquired or adaptive immune system of , each of which contain both humoral and cellular immune elements.
Humoral immunity refers to antibody production and the coinciding processes that accompany it, including: Th2 activation and cytokine production, germinal center formation and isotype switching, and affinity maturation and memory cell generation. It also refers to the effector functions of antibodies, which include pathogen and toxin neutralization, classical complement activation, and opsonin promotion of phagocytosis and pathogen elimination.
Following the 1888 discovery of the bacteria that cause diphtheria and tetanus, Emil von Behring and Kitasato Shibasaburō showed that disease need not be caused by microorganisms themselves. They discovered that cell-free were sufficient to cause disease. In 1890, filtrates of diphtheria, later named , were used to vaccinate animals in an attempt to demonstrate that immunized serum contained an antitoxin that could neutralize the activity of the toxin and could transfer immunity to non-immune animals. In 1897, Paul Ehrlich showed that antibodies form against the plant ricin and abrin, and proposed that these antibodies are responsible for immunity. Ehrlich, with his colleague von Behring, went on to develop the diphtheria antitoxin, which became the first major success of modern immunotherapy. The discovery of specified compatible antibodies became a major tool in the standardization of immunity and the identification of lingering .
An antibody is used by the acquired immune system to identify and neutralize foreign objects like bacteria and viruses. Each antibody recognizes a specific antigen unique to its target. By binding their specific antigens, antibodies can cause agglutination and precipitation of antibody-antigen products, prime for phagocytosis by Macrophage and other cells, block virus receptors, and stimulate other immune responses, such as the complement pathway.
An incompatible blood transfusion causes a transfusion reaction, which is mediated by the humoral immune response. This type of reaction, called an acute hemolytic reaction, results in the rapid destruction (hemolysis) of the donor red blood cells by host antibodies. The cause is usually a clerical error, such as the wrong unit of blood being given to the wrong patient. The symptoms are fever and chills, sometimes with back pain and pink or red urine (hemoglobinuria). The major complication is that hemoglobin released by the destruction of red blood cells can cause acute kidney failure.
Activation of this system leads to cytolysis, chemotaxis, opsonization, immune clearance, and inflammation, as well as the marking of pathogens for phagocytosis. The proteins account for 5% of the blood serum globulin fraction. Most of these proteins circulate as , which are inactive until proteolytic cleavage.
Three biochemical pathways activate the complement system: the classical complement pathway, the alternate complement pathway, and the mannose-binding lectin pathway. These processes differ only in the process of activating C3 convertase, which is the initial step of complement activation, and the subsequent process are eventually the same.
The classical pathway is initiated through exposure to free-floating antigen-bound antibodies. This leads to enzymatic cleavage of smaller complement subunits which synthesize to form the C3 convertase.
This differs from the mannose-binding lectin pathway, which is initiated by bacterial carbohydrate motifs, such as mannose, found on the surface of bacterium. After the binding process, the same subunit cleavage and synthesis occurs as in the classical pathway. The alternate complement pathway completely diverges from the previous pathways, as this pathway spontaneously initiates in the presence of hydrolyzed C3, which then recruits other subunits which can be cleaved to form C3 convertase. In all three pathways, once C3 convertase is synthesized, complements are cleaved into subunits which either form a structure called the membrane attack complex (MAC) on the bacterial cell wall to destroy the bacteria or act as cytokines and chemokines, amplifying the immune response.
+ Major discoveries in the study of humoral immunity
! Substance Discovery Buchner (1890),
Ehrlich (1892)von Behring and Shibasaburō (1890) Richard Pfeiffer (1895) von Gruber and Herbert Durham (1896),
Rudolf Kraus (1897)Jules Bordet (1899) Almroth Wright and Douglas (1903) Ehrlich
Antibodies
Antibody production
B cell activation
B cell proliferation
Antibody-antigen reaction
Complement system
See also
Further reading
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