Antibody Stucture And Function- Lecture 9/29/21 Flashcards
Complementary Determining Region (CDR)
Also called the hypervariable region, 3 spots in each variable region that recognize specific isotope
Five main Ig Isotypes
IgM (mu) IgD (delta) IgG (gamma) IgA (Alpha) IgE (epsilon)
Ig’s with subclasses
IgG (4) and IgA (2)
Light chain isotopes
Kappa and Lambda, don’t really contribute to the function
IgM structure
Pentameric, always 5 antibodies in a circle
IgA formation
Dimeric, can be free
Protein that aids in the formation of polymeric Ig
J chain
Ig chains on Naive B cells
IgM and IgD
Memory B cells Ig make up
IgG, IgA, IgE
Agglutination
Clumping antigen mediated by IgM pentamers, readily removed by amcrophages
Neutralization of virus
Antibody blocks binding to virus receptor, can’t enter cells
Inhibition of bacterial adhesion by antibody
Binds to bacterial binding sites, inhibits binding
Opsonization
Aggregation of immunoglobulin on bacterial surface, causes the activation of macrophages via Fcgamma receptors
Fcgamma receptors
Receptors on phagocytes that recognize IgG that mediates opsonization
Antibody dependent cellular phagocytosis (ADCP)
IgG specific for tumor antigens, mediated by Fcgamma receptor
Antibody-dependent cellular cytotoxicity (ADCC)
Natural killer (NK) cells express Fc-receptors for IgG, induce apoptosis
Mast-cell activation via IgE cross-linking
Mast cells accumulate IgE, when bound to substrate they cross link and trigger degranulization, immunity to worms and allergic reactions
Fcepsilon receptor
On mast cells for IgE
Ag-specific receptor (BCR) Ig type
All isotypes
Agglutination Ig type
IgM
Neutralization Ig type
IgG and IgA
Complement activation Ig type
IgM and IgG
Opsonization isotype
IgG
ADCP isotype
IgG