11.3 Adaptive Immunity Flashcards
“Immunoglobulin” vs “antibody”: terminology
- Immunoglobulin: Refers only to shape of protein
- Antibody: Specific (e.g. Hep B antibodies)
What happens to a B cell as it moves from a Pro-B cell to a pre-IG B cell?
It expresses an immunoglobulin on the surface that has two “surrogate” light chains; not functional, but in the process of becoming functional.
What Ig isotype is expressed on the surface of an immature B cell?
IgM; Single, not pentameric
What two antibody isotypes are expressed on the surface of a mature, naive B cell?
M and D
Which Chromosome codes for the heavy chain of an immunoglobulin?
Chromosome 14
Which chromosome codes for the light chain of an immunoglobulin?
Chromosome 2
Which is the most common Ig isotype found in the body? Which two isotypes are most associated with an immune response?
- IgG is the most common isotype
- IgM and IgG are associated with an immune response
How long do IgG vs IgM antibodies last in the blood? Why is this significant?
- IgG: 20-21 days
- IgM: 10 days
This is significant because, the longer the antibody can last in the blood, the more likely it is to identify its antigen.
Which antibody classes activate the complement system?
IgM, IgG1, and IgG3
Which isotype of antibody is best transferred across the placenta?
IgG
Which parts of antigens do antibodies bind to?
Epitopes
Is AbAg bonding covalent? How does this affect reversibility?
- Non-covalent
- Therefore, reversible
How many complementary determining region (CDRs) are there on each variable region of an antigen (i.e. each side of the Y)?
Six
In terms of CDRs, what influences the strength of a bond between antibody and antigen?
The more CDRs come into contact with the antigen, the stronger the bond
What are the four possible outcomes of an antibody binding to an antigen?
- Agglutination
- Neutralization (cannot enter tissue)
- Complement activation
- Opsonisation