Humoral Immunity and the Generation of Antibody Diversity Flashcards
structure of an antibody
tetrameric proteins (2 light chains two heavy chains)
- has variable region
- has constant region (Fc) - responsible for effector functions. binds complement, phagocytes with Fc
structure of variable region of antibody
3 complementarity determining regions (CDR)
in primary structure the 3 are seperate buy in final structure they align adjacent to form the structure that binds the antigen.
where are bcells generated and developed
generated and develop in bm.
what happens when a bcell is activated
activated by its specific antigen
differentiates into a plasma cell that proliferates and secretes Ig.
does body design Ig
body does not design a specific antibody in response to a specific antigen.
body generates over 100,000,000 different B-cells each making a different random immunoglobulin, this is initially as a cell surface molecule (acting as a receptor).
what happens when bcell are activated
are activated and begin to multiply. this is clonal selection and expansion.
some activate cells become memory cells some become plasma cells which secrete Ig
what is required by a bcell to mount an immune response
must bind to cd4 tcells and the release of cytokines.
how does genome encode so many Ig
there is no complete Ig gene, rather Ig gene segments that in different combinations produce different Ig
how does genome encode so many Ig using kappa light chain as an example
any given cell contains KCL gene. this contains one constant region (C)35 variable regions (V) 5 joining regions (J)
is an endonuclease binding site immediately after every V segment & in front of each J segment. randomly cut after V segment and before J segment. this DNA discarded. In this way dsDNA joining allows us to choose certain parts of DNA to transcribe.