Antibodies in plants

n° 393 - May-June 2001


Antibody-based therapies (immunotherapies) are being applied to the treatment of a wide range of diseases, including immune disorders, cancer and inflammatory diseases. Such therapies will require an inexpensive and safe source of antibodies. Transgenic plants offer an attractive method for large-scale production of antibodies for immunotherapy.

The expression of human antibody genes in plants results in the production of antibodies that are free from contamination (e.g. viruses or prions). However, a serious obstacle to the use of transgenic plants to produce immunotherapy reagents is the fundamental difference in the process of glycosylation between mammalian and plant cells.

Glycosylation (the addition of sugar groups to a protein molecule) can affect the activity of many antibody molecules. This hurdle has now been overcome by ingenious experiments performed by Loïc Faye and colleagues in the "Signaux et régulations chez les végétaux," (Plant Signaling and Regulation) Laboratory, CNRS-Université de Rouen together with collaborators in Wageningen, the Netherlands. They produced transgenic tobacco plants that have modified sugar metabolism. They then crossed these plants with transgenic plants expressing antibody proteins. This cross resulted in tobacco plants that produced recombinant antibody molecules with a glycosylation pattern that was partially humanized. These results represent a major advance towards the use of transgenic plants for the production of human proteins compatible with therapeutic applications in humans.


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