25 June 2016

Lecture #2: ANTIGEN-ANTIBODY REACTION IN BLOOD GROUP SEROLOGY




Many antigen–antibody reactions occur in vitro but the reaction commonly encountered in a blood is agglutination.

Agglutination is the clumping of those particles with antigens on their surface, such as erythrocytes, by antibody molecules that form bridges between the antigenic determinants.




Two stages of agglutination and the factor that influence each:

1.    Sensitization or adsorption

Sensitization represents the physical attachment of antibody molecules to antigens on the erythrocyte membrane. The amount of antibody that will react is affected by the equilibrium constant, affinity constant of the antibody. In most cases, the higher the equilibrium constant, the higher the rate of association and the slower the rate of dissociation of antibody molecules.

a.      Antigen–antibody ratio

Under conditions of antibody excess, a surplus of molecular antigen–combining sites which are not bound to antigenic determinants exists. The outcome of excessive antibody concentration is known as the prozone phenomenon which can produce false–negative reactions. This phenomenon can be overcome by serially diluting the antibody–containing serum until optimum amounts of antigen and antibody are present in test system.

b.     pH

A pH of 5.5 – 8.5 (average of 7.0) is used for routine laboratory testing.

c.      Temperature and length of incubation

IgM (19S) type of antibodies are cold reacting (thermal range: 4–22oC) and IgG (7S) antibodies are warm reacting with an optimum temperature reaction of 37oC.

In laboratory testing, incubation time range from 15–60 minutes. The optimum time of incubation varies according to the class of immunoglobulin and how tightly an antibody attaches to specific antigen.

d.     Ionic strength

Ionic strength is a measure of intensity of the electric field due to ions in solutions. Sodium (Na+) and Chloride (Cl–) in a solution have a shielding effect. These ions cluster around and partially neutralize the opposite charges on antigen and antibody molecules which hinder the association of antibody with antigen. Reducing or lowering the ionic strength of a reaction medium with agents such as low ionic strength saline (LISS) or polybrene enhances antibody uptake.

e.      Steric hindrance

This is the mutual blocking of dissimilar antibodies with the same binding constant and directed against antigenic determinants located in close proximity to each other on cell’s surface. Steric hindrance can occur whenever a conformation change in the relationship of an antigenic receptor site to the outside surface occurs. In addition to antibody competition, competition with bound complement, other protein molecule or the action of agents that interfere with the structural integrity of the cell surface can produce steric hindrance.

2.    Lattice formation

Lattice formation or the establishment of cross links between sensitized particles such as erythrocytes and antibodies resulting in aggregation (clumping), is a much slower process than the sensitization phase. The formation of chemical bonds and resultant lattice formation depend on the ability of a cell with attached antibody on its surface to come close enough to another cell to permit the antibody molecules to bridge the gap and combine with the antigen receptor site on the second cell.




a.      Zeta potential


Because of like charges repel one another; erythrocytes in suspension remain separated from each other. The actual distance of separation is governed by the effective net surface charge density. When erythrocytes are suspended in electrolyte solutions such as sodium chloride, the ions in a suspending solution arrange themselves about the surface of the cell and become more diffuse as the distance from the cell surfaces increases. As an erythrocyte floats in an electrolyte solution, some ions remain with it. The diffuse double layer surrounding the cell is called the ionic cloud and the outer edge of this layer is referred to as the surface of shear.

A difference in electrostatic potential exists between the net charge of the cell membrane and the charge at the surface of shear. This electrostatic potential is referred to as zeta potential. Zeta potential is believed to depend on the actual net surface charge density at the surface of the cell membrane and the dielectric constant (the measure of the electrical conductivity of a suspending medium) of the surrounding medium.

b.     Antibody type

Immunoglobulins are relatively positively charged and following sensitization or coating by particles, they reduce the zeta potential. Antibodies can bridge charged particles by extending beyond the effective rage of the zeta potential which results in the erythrocytes closely approaching each other, binding together and agglutinating.

IgM antibodies are more efficient in producing in vitro agglutination in 0.85% saline than IgG or IgA.

c.      Antigen dosage

The term “double dose” is sometimes used to depict that homozygous genotypic expression of an antigen (such as “cc), in comparison to the heterozygous genotypic expression of an antigen (such “Cc”), which is referred to as a single dose. In some blood group system, the presence of a homozygous genotype expresses itself with more antigen than the heterozygous genotype. The consequence of possessing a double dose of some blood group antigens (such as “c”) is that a greater proportion of erythrocytes are agglutinated. This variation in strength of agglutination is referred to as the dosage effect.

Method of enhancing agglutination

1.     Centrifugation

Centrifugation attempts to overcome the problem of disturbance by subjecting sensitized cells to a high gravitational force, which counteracts repulsive effect and physically forces the cells together.

2.     Treatment with proteolytic enzyme

Treatment with a weak proteolytic enzyme can strip off some of the negative charges on the cell membrane by removing surface sialic acid (cleaving sialoglycoproteins from the cell surface) residues, thereby reducing the surface charge of the cells, lowering the zeta potential and permitting the cells to come closer together for chemical link by specific antibody molecules. The risk of enzyme treatment is that it destroys some blood group antigens such as M, N, and Duffy.

3.     Use of colloid media

The most frequently used colloidal reagent is bovine albumin solution. This product is manufactured from raw bovine serum. Processing results in a solution with a 22% protein concentration and a pH of 7.2, specifically designed for laboratory use. The solution additionally contains 0.1% sodium azide as a preservative.

4.     Use of LISS media

The principle of low ionic strength saline (LISS) is that, the rate of antibody association increases as the ionic strength of the medium decreases. The use of LISS not only increases the sensitivity of antibody detection compared to bovine albumin but also allows a shortened period of incubation.

The most frequent disadvantage of LISS technique is the increased number of non– specific or false positive reactions observed. A more serious problem is the difficulty in detecting some examples of anti–Kell using LISS.

5.     Use of PEG media

The addition of polyethylene glycol (PEG) to serum cell test mixtures has been reported to be more effective in detecting weak antibodies than LISS and manual polybrene. In general, polybrene glycol does not produce non–specific reactions.

6.     Use of polybrene media



The principle of this technique is that the addition of macromolecules brings the red cell closer together to facilitate strong cross–linking by cell–bound antibodies. It offers a benefit of detecting clinically significant blood group alloantibodies failed to be detected by saline–albumin technique. 




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