Ab

Membrane bound receptors or secreated proteins Secreated Proteins-blood,mucosal secreationneutralize/eliminate microbes and toxins-effector molecules of humoral immunity Ab-Ig-immunity conferring proteins-electrophoretic mobility of plasma globulins Secreated Ab-recognise Ag/toxins-V region C region-ability to bind to other molecules(receptors on phagocytes/proteins of complement system)that participate in elimination of Ag 2 function-

Ab Structure 2 identical H chains,2 identical L chains Each chain-1V and 1/more C region 4 chains assembled-Y shaped molecule Each L chain is attached to H chain and each H chain attached together by disulphide bonds L chain- 1 V+1C H chain- 1 V+3/4 C Each domain folds into characteristic 3 D-Ig domain

 Ig domain Other proteins in Sensing signals from env and other cells Proteins Ig superfamily Common ancestral gene

S I S

V-VH,/L VH- 3 CDR-gratest variability CDR3(V/C junction) CDR3-most Ag binding Regions of Ab named-properties of proteolytic fragments of Ig Fab-Ab fragment-whole L chain attached to 1 st V and C region of H chain-portion required for Ag recognition/binding Fc-fragment crystalline-tends to crystalize in soln Each Ab- 2 ID-Fab+1 Fc Fab/Fc- flexible portion (hinge region)-movement and binding Fab to distant Ag C terminal end anchored to cm/tail that lacks anchor L chain not attached to cm

Secreted IgG

VL CL VH CH1 Hinge CH2

CH3

L- 2 types- & -diff C region /no diff function 5 types H chain-,,,,- diff C regions Each light chain complex with any H chain in Ab Ab containing diff heavy chain- isotypesIgM,IgD,IgE,IgG,IgA Diff isotypes- physical,biological,effector function differ Nave B cells- IgM,IgD membrane bound Ab stimulation by Ag/Th-Ag sp clone-expand and differentiate into progeny secreates Ab Progeny can secreate- IgM,or other class Ab with other heavy chain-This change Ig isotype production- heavy chain class/isotype switching Opsonisation IgG1,IgG3-virus,Helminth-IgEeosinophils Light chain class remain fixed for each B cell clone

Epitopes
Part of Ag recognized by Ab-Ag determinants Recognition based on sequence/shape Hidden epitopes are exposed as result of physiochemical change(neo determinants) Ab bind to Ag by reversible,noncovalent interaction,including H bonds and charge interactions. Each IgG,IgD and IgE=2 Ag binding sites Secreated Ig A-dimer with 4 Ag binding sites Secreated IgM-pentamer-10 Ag binding sites

Secretory IgA

The dimeric IgA molecule. 1 H-chain 2 L-chain 3 J-chain 4 secretory component

 Affinity of interaction-strength with which Ag binding surface of Ab binds to epitope. Expressed as dissociation constant(Kd)-Molar concentration of Ag required to occupy half the available Ab molecules in a solution. Lower Kd= higher the affinity. Most Ab in primary immune response=10-6-109 Kd Sec immune response after repeated stimulation Kd=10-8 to 10-11 This increase in Ag binding strength=affinity maturation

Avidity
Ab molecule can bind 2-10 Ag as long as idential epitopes are present sufficiently close Total strength of binding is much greater than affinity of single Ag-Ab bond and is called avidity of interaction. Cross reaction-Ab produced against one Ag may bind other structurally similar Ag BCR-Ig+noncovalent binding to 2 proteins(Ig and Ig)

T dependent and T independent

B cell activation against protein Ag dependent on TH cell,by helping in heavy chain class switching and affinity maturation Absence of TH protein Ag elicit very weak or no Ab response So protein Ag and Ab response to these Ag T dependent

 Polysaccharide,lipids,non protein Ag stimulate Ab production without help from Th cells-T independent. Ab produced in response to T independent Ag show relatively little heavy chain class switching and affinity maturation