Case 1998-610
BACKGROUND
IgA is a polymeric effector molecule of the immune system that mainly acts at mucosal surfaces and is highly resistant to extreme pH conditions, whereas IgG is monomeric and acts in the blood at a narrower pH range. IgG is known for its potent complement activation and, in contrast, IgA is unable to fix complement. Combining the characteristics of IgA and IgG into a single immunoglobulin molecule may produce more effective therapeutic agents.
INNOVATION
UCLA researchers have engineered IgA/IgG hybrid antibodies that combine characteristics of both IgA and IgG into a single immunoglobulin molecule. The IgG constant region was enhanced with the addition of IgA constant regions. This addition resulted in a molecule that has the pH stability of IgA and greater complement fixing activity than IgG due to its polymeric structure. By utilizing this technology, any variable region can be paired with the IgA/IgG hybrid to yield an immunoglobulin molecule with unique effector functions.
APPLICATIONS
Recombinant antibody therapies
ADVANTAGES