Chapter 5

Immunoglobulin
 Contents
Introduction
Section Molecular Structure of Ig
Section Characteristics and Functions of the 5
Classes of Ig
Section Fc Receptors for Ab Molecules
Section Biological Activity of Ab
Section Immunogenicity of Ig
Section Artificial Ab
 Concepts
Antibody (Ab): Glycoprotein molecules
that are produced by plasma cells and can
combine with the corresponding Ag
specifically are called Ab.

ü Ab is produced by B cells in the response to

a stimulation of Ag.
ü Ab possesses a high degree of specificity
and affinity
• Immunoglobulin (Ig):
It refers to all globulins that possess the
activity of Ab or show a similar structure to
Ab

• Therefore, All Abs are Igs, but not all Igs

possess the functions of Abs
 Other Concepts
γ- Globulin
Antiserum
Humoral Immunity
sIg and mIg(BCR) Immune response
Section Molecular Structure of
Ig
 Basic structure
l Ig is composed of four polypeptide chains
joined by S-S bonds.
inter-chain disulfide bonds (S-S)
intra-chain disulfide bonds (S-S)
l It shows “T” or “Y” shape.
 1. H and L chain:

. Heavy chains (H):

450 ~ 550 aa,
50 ~ 75 KD

. Light chains (L):

214 aa, 25 KD
Two terminal ends for each peptide
chain

“N” terminal end

“C” terminal end

L chains attach to H chains

from “N” end
 2. classes and types of Ig
(1) According to the differences of H chains
(amino acid composition, sequence)
Igs can be divided into 5 classes
subclasses
• Five classes of H Chain: g a µ d e
• Five classes of Igs: IgG IgA IgM IgD IgE

IgG1~ IgG4 IgA1, IgA2

(2) According to the differences of L chains:
Two types of L chain: k, l

l 1~ l 4
k : l 20:1 (in mice); 2:1 (in human)
3. Two regions of each peptide chain

(1) Constant region (C)

(2) Variable region (V)
(3) Hinge region
 3. Two regions of each peptide chain

(1) Constant region ( C )

• CH: 3/4 or 4/5 (µ,e) of H chain from the c end
• CL: 1/2 of L chain from the c end

(2) Variable region ( V )

• CH: 1/4 or 1/5 (µ,e) of H chain from the N end
• CL: 1/2 of L chain from the N end
 (2) Variable region ( V ):
Ø Hypervariable region(HVR)
There are three highly
diversity stretches within the
V egion,
they are called HVR.
Ø Framework region(FR): FR1-FR4
Ag-binding sites
Complementarity determining regions(CDR)
 (2) Variable region (V)

Complementarity determining regions(CDR)

L: CDR1, CDR2, CDR3
H: CDR1, CDR2, CDR3
 Idiotype of Ig
Igs produced by different B cells possess unique
structure respectively in hypervariable region
(HVR), the unique structure of Ig is called
idiotype or idiotypic determinant
In fact:
HVR
CDR
Idiotype
are in the same sites of Ig
(3) Hinge region:
• Flexible and suitable for CDR of Ig
binding to antigenic determinants.
• Sensitive to proteolytic enzyme
• IgM, IgE
 Other structures of Ig
• Joining chain(J)
l Secretory piece(SP)
 Joining chain(J ) :
l Produced by plasma cells
l Functions:linker, to compose dimer
pentamer or polymer(IgA, IgM)
 Secretory piece( SP):
. Produced by mucosa epithelial cells
. Secretory IgA (sIgA)
. Functions: protect sIgA, resist
proteolysis in extra secretory liquid.

IgA
. Domains of Ig
 1. Domain :

Polypeptide chains of Ig are folded into a

globular structure by intra chain s-s bond
within each 110aa region which is called a
domain
 2. Domains of Ig

• L chain(2) : VL, CL
• H chain(4~5):
VH,
CH1, CH2, CH3
CH4(in IgM,IgE)
hinge region
 3. Function of each
domain
• VH, VL: antigen-binding site
• CH1, CL: allogeneic marker
• CH2/CH3: complement-fixing site,
permeate placenta(IgG)
• CH3/CH4: cell-binding site
l Hinge region :flexible and suitable for CDR of

Ig binding to antigenic determinants

 . Hydrolytic fragments of Ig
Ig can be digested by papain and
pepsin
• Position
• Fragments
• Function
 1. Digested by papain
• Position:
near the S-S bonds of H inter-chains fromthe N end

l Fragments:
2Fab:fragment antigen-binding
Fc:fragment crystallizable

l Function:
Fab: recognize and bind Ag
Fc:
(1) fix complement
(2) crossing the placenta
(3) bind to FcR in different cells

•
2. Digested by pepsin
• Position:
near the S-S bond of H inter-chains from the C end
• Fragments and function :
F(ab′)2: bind antigen(2 valence)
pFc′: no function
 Significance
l Elucidating the relationships
between the structure and function
of Igs

l Decrease the immunogenicity of

Ig for clinical treatment