ANTIGEN ANTIBODY REACTION: The antigens and the antibodies combine specifically with each other.

. This interaction between them is called Antigen-Antibody reaction. It may be abbreviated as Ag-Ab reaction. These form the basis for humoral immunity or antibody mediated immunity. These reactions form the basis for detection of infectious disease causing agents and also some nonspecific Ags like enzymes. When Ag-Ab reactions occur invitro they are known as serological reactions. The reactions between Ag and Ab occur in three stages. !" #rimary stage- This reaction involves formation of Ag-Ab comple$. The reaction is rapid and it obeys the general laws of physical chemistry and thermodynamics. The two molecules are held together by non-covalent forces hydrogen bonding ionic bonding and sometimes hydrophobic bonding. %" The second stage leads to visible events like precipitation agglutination lysis of cells killing of Ag neutralization of to$ins fi$ation of complement and enhancement of phagocytosis. &" The third stage includes destruction of Ag or its neutralization. Salient features of Ag-Ab reactions: !"Immune comple$' (ince the reaction is specific an Ag combines only with its homologous Ab and vice versa. %" (pecificity of Ag-Ab reaction' An Ab will combine only with that Ag which causes its production. The specificity may be compared to a )ock and *ey system. &" +inding sites of Ag and Ab' The entire of the Ag participates in the reaction. +ut the part of the Ag that combines with the Ab is called epitope or antigenic determinant. An Ag may have !, -, or up to !,, antigenic determinants. The part of the Ab that combines with Ag is called paratope or antigen binding site. .ost Abs are bivalent whereas Ig. has - to !, paratopes. NATURE OF ANTIGEN-ANTIBODY REA TIONS !oc" an# $e% once&t

The combining site of an antibody is located in the /ab portion of the molecule and is constructed from the hyper variable regions of the heavy and light chains. 0-1ay crystallography studies of antigen-antibody interactions show that the antigenic determinant nestles in a cleft formed by the combining site of the antibody. Thus our concept of antigenantibody reactions is one of a key 2i.e. Ag" which fits into a lock 2i.e .Ab". Non-co'alent Bon#s The bonds that hold the antigen to the antibody combining site are all noncovalent in nature. These include hydrogen bonds electrostatic bonds 3an der Waals forces and hydrophobic bonds. .ultiple bonding between the antigen and the antibody ensures that the antigen will be bound tightly to the antibody. Re'ersibilit% (ince antigen-antibody reactions occur via non-covalent bonds they are by their nature reversible. S(E IFI ITY AND ROSS REA TI)ITY S&ecificit% (pecificity refers to the ability of an individual antibody combining site to react with only one antigenic determinant or the ability of a population of antibody molecules to react with only one antigen. In general there is a high degree of specificity in antigen-antibody reactions. Antibodies can distinguish differences in'

The primary structure of an antigen Isomeric forms of an antigen (econdary and tertiary structure of an antigen

ross reacti'it%

4ross reactivity refers to the ability of an individual antibody combining site to react with more than one antigenic determinant or the ability of a population of antibody molecules to react with more than one antigen. 4ross reactions arise because the cross reacting antigen shares an epitope in common with the immunizing antigen or because it has an epitope which is structurally similar to one on the immunizing antigen 2multi specificity". TESTS FOR ANTIGEN-ANTIBODY REA TIONS Factors affecting *easure*ent of antigen-antibo#% reactions Affinit% The higher the affinity of the antibody for the antigen the more stable will be the interaction. Thus the ease with which one can detect the interaction is enhanced. A'i#it% 1eactions between multivalent antigens and multivalent antibodies are more stable and thus easier to detect. Antigen to antibo#% ratio The ratio between the antigen and antibody influences the detection of antigen-antibody comple$es because the size of the comple$es formed is related to the concentration of the antigen and antibody. (+%sical for* of t+e antigen The physical form of the antigen influences how one detects its reaction with an antibody. If the antigen is a particulate one generally looks for agglutination of the antigen by the antibody. If the antigen is soluble one generally looks for the precipitation of the antigen after the production of large insoluble antigen-antibody comple$es.