The Structure and Function of Antibodies Flashcards
What is an antibody?
The secreted form of the B cell’s B cell receptor
What mediates recognition of an antigen?
The recognition of antigen is mediated by the two antigen binding sites of the variable regions.
What determines the antibody’s biological role in the immune response?
The constant region of the heavy chain
How many polypeptide chains do all immunoglobulin molecules consist of?
Four polypeptide chains: two identical heavy (H) chains and two identical light (L) chains, held together by disulfide bonds.

How many types of L and H chains are there?
There are two types of L chains and five types of H chain.
The chains have Greek letter names.
What are the two types of L chain?
kappa (κ) chain and lambda (λ) chain
What are the five types of H chain?
the gamma (γ), mu (μ), delta (δ), epsilon (ε), and alpha (α) chains
What does the type of H chain define?
The type of H chain defines the immunoglobulin class or isotype.
The immunoglobulin may have a κ chain or λ chain L chain, but never both.
For example, both γ2λ2 and γ2κ2 antibodies are IgG antibodies because they have the same γ heavy chain even though they have different light chains.

What regions do all antibodies have?
Variable
Hypervariable
Constant
How many identical H and L chains does a single antibody molecule have?
A single antibody molecule has two identical H and two identical L chains.
Thus, a single antibody molecule has two identical antigen-binding sites.
Another way of saying this is that antibodies are bivalent.
What are the variable regions of antibodies?
The N-terminal portions of both the H and L chains are different for different antibodies and are therefore referred to as variable (V) regions

What are the hypervariable regions of the immunoglobulins?
Within the variable regions of the immunoglobulins, there are three short stretches of amino acids that vary the most from one antibody to another.
These are called the hypervariable (HV) regions.
The H and L chain V regions (VH and VL) combine to form the antigen-binding region of the antibody.
The hypervariable regions (HVH and HVL) contribute significantly to the antigen-binding site and are the part of the antibody that contacts the antigen.

The rest of the H and L chains are the constant (C) region.
Within a given species of mammals, the amino acid sequences of the constant regions are identical for all antibodies of that particular isotype.
Compare the C region of the H chain and L chain.
Each H chain (μ, δ, γ ε, α) has a different amino acid sequence in its C region. These determine the function of the antibody (how it helps eliminate the antigen). Different isotypes of antibodies have different roles in the immune system.
The C regions of the L chains (κ and λ) have different amino acid sequences but this doesn’t influence the function of the antibodies.
Describe the significance of the difference in the amino acid sequences of the C regions of the heavy chains between species.
It can cause problems in a clinical setting when a human patient needs to be transfused with antibody from a non-human species.
Immunologists can also exploit these differences to generate reagents for detecting and quantifying antibody.
For example, it is possible to generate an antibody in a goat that recognizes the heavy chain C region of the human antibody (because, in a goat, the human C region is recognized as a foreign protein).
These antibodies are called “goat anti-human Ig” antibodies because it is a goat antibody that recognizes the constant region of a human antibody.
What is the complementarity determining region?
Hypervariable regions are also called “complementarity determining region” or CDR.
What is the framework of an immunoglobulin?
The variable regions are sometimes called “framework” - while there is some variability in the amino acid sequences of different antibodies, there is also some conserved features.
These conserved features are important in the overall folding of the protein.
What part of the antibody makes contact with the antigen?
The hypervariable region shows extreme amino acid sequence variability - this is the part of the antibody that makes contact with the antigen.
In the three-dimensional structure, the hypervariable regions would be at the “tips” of the antibody.
What determines the specificity of the antibody?
The antigen-binding site is a three-dimensional pocket.
The side chains of the amino acids that make up the H and L chain hypervariable regions determine the shape of the antigen-binding site.
The shape of the antigen-binding site determines the specificity of the antibody (i.e., which epitopes it will bind).

What is an epitope?
A single antibody molecule binds to only to a small portion of the antigen molecule called the epitope or antigenic determinant.
An epitope has a unique three-dimensional structure.
The antigen-binding site of the antibody has a shape that is complementary to that of the epitope.
The epitope on the antigen fits into the antibody’s antigen-binding site in the same way a key fits into a lock.

How many epitopes does a single antigen have?
A single antigen can have many epitopes.
For a protein antigen, an epitope may be only 4–5 amino acids long (the average protein is 200–1000 amino acids long).
There may be many copies of the same epitope, different epitopes, or both.
Epitopes on the surface of the antigen are accessible to the antibody.
Therefore, many antibodies, each with different specificities, can bind to their particular epitope on one antigen particle.
Different antibodies have antigen-binding sites with different shapes, and will therefore bind epitopes with different three-dimensional structures.
It is possible for two different antigens to have an epitope in common.
True or false?
True
What is the chemical nature of an epitope?
The chemical nature of an epitope can be carbohydrate, lipid, amino acids, nucleic acid etc.
What is required for strong binding between the antibody and the epitope?
The antibody will only bind epitopes with a complementary shape (remember the lock and key analogy).
Close contact between the surface of epitope and surface of antigen-binding site is required.
A poor fit would suggest there is weak binding or no binding.
Close contact allows the formation of hydrogen bonds as well as ionic and hydrophobic interactions between the epitope and the antigen-binding site.
How many epitopes will a single antibody bind?
Only one or a few similarly shaped epitopes.








