Monoclonal Antibody Purification ( Plants).

Plant-based expression systems provide an alternative biomanufacturing platform for recombinant proteins (Matoba ., 2011). In particular, plant virus-based vectors can overexpress proteins within days in the leaf tissue of (). To overcome the issues of genetic instability and limited infectivity of recombinant viruses, -mediated delivery of "deconstructed" virus vectors has become the mainstay for the production of large and/or multicomponent proteins, such as immunoglobulin (Ig)G monoclonal antibodies (mAbs). Here, we describe a method of producing human IgG mAbs in using the tobamoviral replicon vector magnICON. The vector can express up to a few hundred mg of a mAb per kg of leaf material in 7 days. A representative case for the broadly neutralizing anti-HIV and anti-influenza mAbs, VRC01 and CR6261 respectively, is shown (Hamorsky ., 2013). Leaf tissue is homogenized and the extract is clarified by filtration and centrifugation. The mAb is purified by fast protein liquid chromatography (FPLC) using Protein A affinity and Phenyl HP hydrophobic interection resins.