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Location: Home > Information Center > Technical FAQs > Antibody Technology Column > Definition and classification of the antibodies

Definition and classification of the antibodies

Date: 2015-04-23 Author: Leading Biology Click: 1257

1. antibody definition

Antibody (immunoglobulin is not just an antibody) is a large Y-shaped protein secreted by plasma cells (effector B cells) and used by the immune system to identify and neutralize foreign substances such as bacteria and viruses. It is found in body fluids such as blood of vertebrates, and the cell membrane surface of its B cells. Antibodies can recognize a unique feature of a particular foreign object called as antigen.


Related concepts

Antigen (Ag): Any substance that induces an immune response. The foreign molecule can be identified by immunoglobulin on B cells or treated by antigen-presenting cells and combined with a major histocompatibility complex to form a complex to reactivate T cells, triggering a continuous immune response.


T cells and B cells: immune cells can be roughly divided into two major categories, T cells and B cells, both from the bone marrow, but T cells are formed in the thymus, its main function is to phagocytose foreign invaders. The main function of B cells is to produce a variety of antibodies, just like weapons in the army, so that we can resist foreign invaders. Human B cells can produce more than one billion different types of antibodies. T cells do not produce antibodies, but act directly. Therefore, the immune function of T cells is called "cell immunity." B cells act by producing antibodies. Antibodies are present in body fluids, so the immune function of B cells is called "humoral immunity."


2. Structure of the antibody

An antibody is a symmetric structure with four polypeptide chains, two of which are longer, the same heavy chain (H chain) with a relatively larger molecular weight, and two shorter, relatively lighter, identical light chains (L chain). The interchains are linked by a disulfide bond and a non-covalent bond to form a monomer molecule composed of four polypeptide chains. The light chain has two kinds of κ and λ, and the heavy chain has five kinds of μ, δ, γ, ε and α.


The entire antibody molecule can be divided into two parts, a constant region and a variable region. In a given species, the constant regions of different antibody molecules have the same or nearly identical amino acid sequences. The variable zone is located at the ends of the arms of the "Y". A small portion of amino acid residues are particularly strongly changed in the variable region, and the residue composition and arrangement order of these amino acids are more likely to occur in the variable region called hypervariable region. The hypervariable region is located on the surface of the molecule and consists of range from 17 amino acid residues to 2 or 3 amino acid residues. The hypervariable region amino acid sequence determines the specificity of the antigen. The two antigen binding sites on one antibody molecule are identical and are located at the ends of the arms and are called antigens.


Related concepts

Fab segment and Fc segment: The Fab segment is a fragment of the antigen binding (Fab), which corresponds to two arms of an antibody molecule, and consists of a complete light and heavy chain VH and CH1 domains. The Fc segment is a fragment crystallizable (Fc) corresponding to the CH2 and CH3 domains of Ig, and is a site where Ig interacts with an effector molecule or a cell. The Fab segment contains the complete variable region and the CH1 region of the constant region. The Fc segment refers only to the region of the Ig constant region CH2 and CH3, which corresponds to the portion below the Y-shaped structure.


3. Antibody classification

(1)By the targeting objects

According to the target, it can be divided into anti-toxin, anti-bacterial antibody, anti-viral antibody and pro-cell antibody (immunoglobulin capable of binding to cells, such as lgE-reactive antibody in type 1 allergy, which can be adsorbed on the target cell membrane)


(2)Animal antibody functions

Antiviral serum antibodies of different immunological properties are obtained depending on the nature of the injected bacteria or virus, and injection into different kinds of animals. Animal serum antibodies on the market are broadly classified into the following types:

1 Porcine antibody: swine fever antibody, swine blue ear antibody, porcine circovirus antibody, pig pseudorabies antibody, porcine parvovirus antibody, swine aftosa antibody, swine flu antibody, etc.

2 Avian antibodies: gosling scorpion antibody, duck liver antibody, duck serositis antibody, avian influenza antibody, Newcastle disease antibody, etc.

3 Bovine antibodies: bovine foot and mouth disease antibody, cow mastitis antibody, bovine epidemic fever antibody, bovine viral diarrhea antibody, bovine hemorrhagic sepsis antibody, etc.

4 Sheep antibodies: sheep pox antibody, sheep foot-and-mouth disease antibody, sheep small ruminant antibody, sheep fast-acting antibody, sheep enterotoxemia antibody, sheep scorpion antibody, sheep black plague antibody, etc.

5 Canine antibodies: canine rabies antibody, canine distemper antibody, canine parainfluenza antibody, canine adenovirus antibody and canine parvovirus antibody, pseudorabies antibody, parvovirus antibody, JE antibody, etc.


(3)According to physicochemical properties

According to physicochemical properties and biological functions, the antibodies can be divided into IgM, IgG ,IgA, IgE, and IGD five kinds.

Antibodies of IgM are the first antibodies secreted in an immune response. They initiate a cascade of complements after binding to the antigen. They also link invaders together and bunch them into a heap that facilitates phagocytosis by macrophages;

The IgG antibody activates complement and neutralizes multiple toxins. IgG lasts for a long time and is the only antibody that protects the fetus from the placenta during pregnancy. They also secrete from the mammary gland into the colostrum to protect the newborn babies.

The IgA antibody enters the mucosal surface of the body, including the mucous membranes of the respiratory, digestive, reproductive, etc., and neutralizes the infectious agents. It can also be delivered to the digestive tract mucosa of newborns through the colostrum of breast milk, which is the most important and most quantity type of antibody in breast milk;

The tail of the IgE antibody binds to the cell membrane of basophils and mast cells. When the antibody binds to the antigen, basophils and mast cells release tissue-like substances to promote the development of inflammation, which is also an antibody that triggers an allergic reaction;

The role of IGD antibodies is not well studied. They mainly appear on the surface of mature B lymphocytes and may be involved in the differentiation of B cells. (IGD was found in human myeloma protein in 1995, and its molecular weight is 175kD. It is mainly produced by atherosclerotic cells such as tonsils and spleen. The concentration of IGD in human serum is 3~40μg/ml, which is less than1% of the total Ig in the serum, synthesized late in the development of the individual. The IgD hinge region is very long and sensitive to protease hydrolysis, so the half-life of IGD is very short, which is only 2.8 days. The exact immune function of IGD in serum is still unclear. In the cell stage, in addition to the expression of SmIgD, the antigen is stimulated to exhibit immune tolerance. SmIgD gradually disappears after activation or activation of mature B cells or into memory cells.


(4)According to the visible reaction

According to whether there is a visible reaction after binding to the antigen, it can be divided into: a complete antibody with visible binding reaction in the presence of medium, that is, the so-called antibody, and Incomplete antibodies, which can suppress the antigen corresponding antibodies without any visible reaction


(5)By antibody source

According to the source of the antibody, it can be divided into natural antibodies and immune antibodies.

An antibody is an immunoglobulin, the altered globulin molecule. It is produced by specific antigen stimulation. The antibody is produced because the antigen invades the body and causes various immune cells to interact, so that the B cells in the lymphocytes differentiate and proliferate to form plasma cells, and the plasma cells can produce secreted antibodies.


(6)Development of the antibody

The development of monoclonal antibodies has gone through four phases: murine monoclonal antibodies, chimeric monoclonal antibodies, humanized monoclonal antibodies, and fully human monoclonal antibodies.

Murine monoclonal antibody: murine hybridoma monoclonal antibody mainly combines B cells derived from immunized mice with myeloma cells, and then selects mouse hybrid fusion cells which can proliferate in an endless manner and secrete antibodies. Further screening, antibody preparation and antibody purification are performed.

Chimeric monoclonal antibody: refers to the replacement of the constant region of a mouse with a human constant region, retaining the variable region sequence of the murine monomer antibody, and forming a human-mouse hybrid antibody. The development process is fast, and the immunogenicity of the heterologous antibody can be greatly reduced, but the specificity and affinity of the parent mouse monoclonal antibody are almost maintained. In addition, it also has the effector functions of human antibodies, such as complement fixation, antibody-dependent cell-mediated cytotoxicity (ADCC).

Humanized monoclonal antibody: using the existing numerous mouse antibodies that have been analyzed in detail, the antibody fragment (complementarity determining region, CDR) which is directly contacted with the antigen is grafted with the human antibody framework, and is reshaped by affinity. It maintains its specificity and most of its affinity while removing almost all immunogenicity and side effects.

Fully human monoclonal antibodies: The variable and constant regions of their antibodies are all human, removing immunogenicity and toxic side effects. Related technologies for the preparation of fully human antibodies include human hybridoma technology, EBV transformed B lymphocyte technology, phage display technology, transgenic mouse antibody production technology (transgenic mouse) and single B cell antibody preparation technology.

The humanized and fully human antibody drugs prepared by humanized and fully human antibodies overcome various shortcomings of animal-derived antibodies and chimeric antibodies due to their high affinity, high specificity and low toxic side effects. It has become an inevitable trend in the development of therapeutic antibody drugs.

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