It was recently discovered that 75% of the IgG (IgG2 and IgG3 molecules of camellids (camels and lamas) are devoid of light chains. These molecules exhibit a comprehensive binding |repertoire, agglutinating activity and complement binding. They are therefore bonafide antibodies. |Cloning of the molecules have shown these molecules to be devoid of the CH1 domain, the VH being immediately followed by the hinge. This explains how the heavy chain can be secreted as it lacks the BIP chaperon binding site : it has a structure comparable to heavy chains encountered in heavy chain disease.However the IgM and another class of IgG (IgG1) carry light chains. The aim of the |research is to understand how the switch IgM-IgG (devoid of light chain) occurs. The obiectives are to determine : 1) Whether the CH1 domain of the IgGM and IgG is deleted at the genetic level or are some of the lntron splicing sites deleted so that CH1 is removed by processing. 2) Whether the light chain is acting solely in a structural role to permit secretion of IgG1 and IgM. In this case we expect the light chain to be very homogeneous and the expressed Vh repertoire to be similar if not identical in the IgM and the heavy chain IgG2 and IgG3 molecules.
|Effective start/end date||1/01/95 → 31/12/97|
Flemish discipline codes
- Earth sciences