Antibody processing and engineering in plants, and new strategies for vaccine production.
The use of transgenic plants for the production of recombinant proteins is not a universal solution for all proteins. The choice of this expression system depends very much on the type of protein and its applications. Many proteins will best be made by conventional microbial fermentation, similarly, we are already identifying proteins where plants represent the only practical option for one reason or another. It will be important to understand better the cellular mechanisms of protein folding, assembly and processing in plants, in order to maximise the potential of transgenic plants as a protein production system. One of the main advantages that plants offer is that they are higher eukaryotic organisms with an endomembrane system. Therefore, they fold and assemble recombinant proteins using protein chaperones that are homologous to those in mammalian cells, and they perform post-translational modifications. This allows, for example, the expression of monoclonal antibodies, first described in 1989, as well as a range of other types of immunoglobulin molecules and multimeric complexes.
Ma
Julian K-C
JK
Department of Cellular and Molecular Medicine, Molecular Immunology Unit, St George's Hospital Medical School University of London, Jenner Wing, Level 2, Cranmer Terrace, London, SW17 ORE, UK. jma@sghms.ac.uk
Drake
Pascal M W
PM
Chargelegue
Daniel
D
Obregon
Patricia
P
Prada
Alessandra
A
D000818:Animals; D000906:Antibodies / Q000378:metabolism*; D000917:Antibody Formation; D006031:Glycosylation; D006801:Humans; D030821:Plants, Genetically Modified / Q000235:genetics* / Q000276:immunology*; D015202:Protein Engineering; D014612:Vaccines / Q000096:biosynthesis*
D000906:Antibodies; D014612:Vaccines