Affinity vs. avidity

Affinity

Antibody affinity refers to the total strength of non-covalent interactions between the paratope of the antibody and the epitope of the antigen (Figure 1).

Diagram of an antibody (immunoglobulin) structure. The Y-shaped antibody is shown in black. A colored diamond shape, indicated by a blue arrow, highlights the variable region of the light chain on one of the antibody arms.

Figure1: Antibody affinity

Avidity

Antibodies are bivalent to multivalent, meaning they bind to two or more epitopes at the same time. Antibody avidity (or also called functional affinity) refers to the overall strength of the interaction of multivalent antibodies to their epitopes. In other words, it is the sum of all affinities in the antibody-antigen complex (Figure 2).

Diagram comparing linear and conformational (discontinuous) epitopes. On the left is a single Y-shaped IgG antibody with two antigen-binding sites, and on the right is a circular pentameric IgM antibody with ten binding sites. The diamond shapes represent the antigen.

Figure 2: Antibody avidity

High avidity can compensate for low affinity. As shown in Figure 3, pentameric IgM has a lower affinity than IgG, but has a higher avidity than IgG due to its multivalence.

Diagram showing the progression of antigen structure from a single residue to linear and conformational epitopes. From left to right: a single antigenic residue is depicted, followed by a linear epitope composed of three adjacent residues on a straight segment, and finally a conformational epitope formed by non-adjacent residues brought together through protein folding into a curved structure. Antigenic sites are marked with small diamond shapes.

Figure 3: Affinity vs. avidity