Lecture #4: Adaptive Ag Recognition Flashcards
Fab/Fc Fragments
Fab = fragment Ag binding
Fc = fragment crystallized)
Both have effector functions
Where are most Abs found in the globulins?
Third, slowest migrating group i.e. “gamma” globulins
Effector Properties of Abs
Immunomodulation
Reduce host damage from inflammation
Organized T cell response
Opsonization
Activate complement system
Toxin neutralization
Direct antibacterial activity
Papain
Cleaves IgG at the heavy chain into two Fab fragments and complement: Fc receptors binding the Fc fragment
Proteolysis of IgG by Pepsin
Generates a single bivalent Ag-binding fragment F(ab’)2
Five classes of Abs
IgM, IgD, IgG, IgE, IgA
Two different kinds of light chains:
K and delta
Ab unit can only have one or the other at one time
Ig Superfamily Proteins
T cell receptor MHC Molecules CD4 coreceptor of T cells CD28 ICAM-1
Properties of Secreted IgG
Ag-binding sites formed by juxtaposition of VL and Vh domains
Heavy chains C regions end in tail pieces
The locations of complement-Fc RC-binding sites within the heavy chain constant regions are approximation
Properties of Membrane-bound IgM on B cell
One more CH4 domain than IgG
Has C terminal transmembrane and cytoplasmic portions that anchor in the plasma membrane
Locations of Ab Hinges
Between Ch1 and Ch2 domains
Structure/function/concentration of IgA
Mainly dimer, also monomer, trimer
Mucosal immunity
3.5mg/ml
Structure/function/concentration of IgD
Monomer
Naive B cell Ag Rc
Trace
Structure/function/concentration of IgE
Monomer
0.05mg/ml
Defense against helminthic parasites, immediate hypersensitivity
Structure/function/concentration of IgG
Monomer
13.5mg/ml
Opsonization, complement, Ab dependent cell mediated cytotoxicity, neonatal immunity, feedback inhibition of B cells