B cells and antibodies Flashcards
What is an antibody?
Antibodies are glycoproteins with a minimum molecular weight of around 150,000 Daltons that bind to specific antigens.
How does the specificity of antibodies work?
Each antibody binds to a single specific antigen.
What is the role of B lymphocytes in antibody production?
Each individual B lymphocyte produces antibodies that bind to the same antigen, but the structure of the antibody changes over time.
How many different B lymphocytes are there in the human body?
There are billions of different B lymphocytes in the human body, each capable of producing an antibody to a different antigen.
What is the term used for the part of an antigen to which the antibody binds?
The part of an antigen to which the antibody binds is known as the epitope.
What is the structure of an antibody in a naïve B cell?
In a naïve B cell, the antibody includes an additional transmembrane domain that anchors it on the surface of the B cell, where it is known as a B cell receptor (BCR).
What activates the B cell receptor (BCR)?
The BCR is activated by antigen cross-linking and additional cytokine-mediated stimulation by T helper cells.
What happens to a mature B cell after BCR activation?
After BCR activation, the mature B cell undergoes BCR gene rearrangements, which allow the secretion of a soluble antibody form of the BCR.
Does the structure of the antigen-binding site change during BCR activation?
No, the structure of the antigen-binding site remains identical throughout the activation process.
What is the name of the domain responsible for antigen binding in an antibody?
The domain responsible for antigen binding is called the Fv (variable fragment) domain.
What are the components of an antibody structure?
An antibody structure consists of heavy chains, light chains, variable regions (V), constant regions (C), disulfide bonds (SS), and an antigen-binding site.
What are the hypervariable regions in an antibody?
The hypervariable regions are parts of the antibody that differ between antibodies and contribute to their specificity for different antigens.
What determines the antibody classes?
The heavy chains of antibodies determine the antibody classes, including IgG, IgD, IgE, IgA, and IgM.
Which antibody class is primarily found as monomers and dimers?
IgG is primarily found as monomers and dimers.
Which antibody class is the majority of total serum immunoglobulins?
IgG is the majority of total serum immunoglobulins.
How many constant domains does each light chain and heavy chain have in an IgG antibody?
Each light chain has one constant domain, while each heavy chain has three constant domains in an IgG antibody.
What is the effect of affinity and avidity on antibody function?
Affinity and avidity impact antibody function by influencing the binding strength and multivalency of the antibody with its target.
What is the difference between univalent and bivalent antibodies?
Univalent antibodies have a single binding site, while bivalent antibodies have two binding sites.
What primarily determines the functional differences among human immunoglobulin isotypes?
The three-dimensional structure of the heavy chain constant region largely determines the functional variations among human immunoglobulin isotypes.
How do differences in the heavy chain constant region influence antibody function?
Differences in the heavy chain constant region impact antibody function by determining which immune system partner the antibody molecule interacts with, such as antibody receptors on macrophages or complement proteins.
Does the three-dimensional structure of the heavy chain constant region affect the antigen-binding capability of the antibody?
No, the three-dimensional structure of the heavy chain constant region does not directly affect the antigen-binding capability of the antibody. It primarily influences the interaction with immune system partners.
How does IgM exist in terms of its structure?
IgM exists in a pentameric form, where five individual antibody molecules are linked together by the J chain.
How many antigen binding sites does IgM have?
IgM has 10 antigen binding sites due to its pentameric structure.
How does the pentameric structure of IgM compensate for its affinity for antigens?
Even if the affinity for antigen is not fully developed, the pentameric structure of IgM provides an avidity effect by having multiple antigen binding sites.
What is the structure of secretory IgA (sIgA)?
Secretory IgA (sIgA) exists as a dimer, where two individual antibody molecules are linked together by a J chain and a secretory piece.
What is the function of the secretory piece in sIgA?
The secretory piece protects sIgA from proteolysis and facilitates its secretion across mucus membranes.