Immunology Lecture 4_Antibodies Flashcards
Define Immunoglobulin (antibody)
Immunoglobulins (IgX) are protiens that are secreted by B cell lymphocytes to neutralize pathogens. They do this by by binding to a pathogen or it’s products and recruting other leukocytes to destroy the pathogen.
Identify the following structures on an IgX: Heavy chains, light chains, constant region, veriable region, flexible hinge (what tertiary bond forms this), antigen binding site, C terminus and N terminus, Fc, and Fab
Draw a picture, refer to slide 5 if needed
What does the Fab region do?
Fragment Antigen Binding (Fab) is the part of the IGX that binds to the epitope on the antigen (they are epitope specific)
What does the Fc region do?
Fc binds to Fc receptors on other cells, often to iniciate phagocytosis
Define Autoantigen
A self molecue that incorrectly induces an immune response
Explain combinatorial diversity
recombination activating gene (RAG) mediates multiple V -(D)-J combinations in the veriable protion of the heavy and light chains.
Define Junctional diversity
Additions and deletions of necleotides at junctions durring recombination.
Define valence
Valence is the number of pathogen binding sites. A single anti body has a valence of 2
Define Affinity
The strength of binding at a single site
Define Avidity
Total strength when all binding sites are included (Avidity increases as valence increases similar to the strength of a rope as you add strands)
What kind of IgX do naive B cells have as BCR
both IgM and IgD
What kind of IgX do memory b cells express as BCRs
they can express any one isotype as a BCR
Where is the IgG isotype high?
in blood and epithelial tissue
Where is the IgA isotype high?
at the mucosal surfaces
How is the Classical Complement Cascade triggered?
It is triggered with one Pentameter of IgM or at least 2 monomers of IgG