Antibodies, also known as immunoglobulins, are glycoproteins produced by the immune system in response to foreign substances, such as pathogens or antigens. They play a crucial role in the body's defense mechanism by recognizing and binding to specific antigens, thereby neutralizing or removing them from the body.
An antibody consists of two main regions: the Fab (Fragment, Antigen Binding) region and the Fc (Fragment, Crystallizable) region. The Fab region is responsible for binding to antigens, while the Fc region interacts with immune effector cells and molecules, such as complement proteins and Fc receptors on immune cells .
| Region | Function |
|---|---|
| Fab | Binds to antigens |
| Fc | Interacts with immune effector cells and molecules |
Antibodies can be cleaved into smaller fragments, each with specific functions:
Fab Fragment: Contains the antigen-binding site.
F(ab')2 Fragment: A dimeric form of Fab, created by cleaving below the hinge region.
scFv (Single-Chain Variable Fragment): A smaller version of Fab, consisting of linked variable regions of heavy and light chains.
Diabody: Two scFvs connected by a short linker, enhancing affinity for antigens .
Recent studies have shown that antibodies can be engineered to enhance their effector functions. For example, Fc-engineered antibodies have been developed to improve their ability to control infections like tuberculosis by promoting neutrophil-dependent mechanisms .
KEGG: ath:AT5G23800
UniGene: At.54962