Antigen–Antibody Binding

The primary union of binding sites on an antibody with specific

epitopes on an antigen depends on two characteristics of
antibody known as affinity and avidity. Such characteristics are
important because they relate to the sensitivity and specificity
of testing in the clinical laboratory.
Affinity
Affinity is the initial force of attraction that exists between a
single Fab site on an antibody molecule and a single epitope
or determinant site on the corresponding antigen.1,2 As the epitope
and binding site come into close proximity to each other,
they are held together by rather weak bonds occurring only
over a short distance of approximately 1 _ 10–7 mm.1
The strength of attraction depends on the specificity of antibody
for a particular antigen. One antibody molecule may
initially attract numerous different antigens, but it is the epitope’s
shape and the way it fits together with the binding sites
on an antibody molecule that determines whether the bonding
will be stable. Antibodies are capable of reacting with
antigens resembling the original antigen that induced antibody
production, which is known as cross-reactivity. The
more the cross-reacting antigen resembles the original antigen,
the stronger the bond will be between the antigen and
the binding site. However, if the epitope and the binding site
have a perfect lock-and-key fit, as is the case with the original
antigen, the affinity will be maximal (Fig. 10–1). When the
affinity is higher, the assay reaction is more sensitive because
more antigen–antibody complexes will be formed and visualized
more easily.