Imunoglobulinas

Fig 3.21 J aneway 4th ed.

Structural organisation of the main human
immunoglobulin isotype monomers
IgM & IgE lack hinge regions, but contain an extra
heavy chain domain
IgA and IgM can form multimers:
Both contain an 18 amino acid C-region tailpiece with a cysteine residue
esential for polymerisation
A single 15 kDa J chain initiates polymerisation
IgA is a dimer in mucous secretions (but not plasma)
IgM is a pentamer (or hexamer) in plasma
Fig 4.13
Kuby
4th ed.
Immunoglobulin isotypes are selectively
distributed in the body
Plasma: IgG + IgM
Extracellular fluids: IgG + monomeric
IgA
Secretions (including breast milk):
polymeric IgA
Beneath epithelia: IgE (associated with
mast cells)
Transplacental transport: IgG
Fig 9.19 J aneway 4th ed.
Size: IgG, IgE and monomeric IgA are
small and can diffuse from blood easily
Transcytosis: dimeric IgA
Fig 4.15
Kuby 4th ed.
Structure and formation of secretory IgA
basolateral membrane
Secretory component masks protease cleavage sites in the IgA hinge region,
allowing secretory IgA to survive longer in the mucosal environment
Activation of complement: Flexibility (even without a hinge) allows access
for complement binding (IgG3, IgM)
Figs. 9.35 &
9.36,
J aneway
4th ed
Summary: Properties of the human
immunoglobulin isotypes:
Fig 4-2 Kuby 4th ed. Or Fig 3.20 J aneway 4th ed.
Table 4-2 Kuby 4th ed.
The B-cell receptor (BCR)
Fig. 5.7 J aneway 4th ed
Gerao de Diversidade Imunolgica - LB 2 parte