
Antibodies, antigens and enzymes for replacement therapies and virus-like particles (VLPs) have all been produced successfully in plants as part of the concept of ‘Molecular Farming’ (Lomonossoff and D’Aoust, 2016). There have been several differences noted between plant-expressed proteins, and their equivalents produced in other systems, such as CHO cells, particularly regarding their glycosylation. However, several publications have also indicated that preparations of plant-expressed proteins, including antibodies, VLPs and soluble molecules such as HIV gp120, have a higher proportion of multimers or aggregates than their CHO- or yeast-expressed equivalents (e.g. Mechtcheriakova et al., 2006; Ramessar et al., 2008; Rosenberg et al., 2013). The cause of this has not been investigated in detail because the molecules expressed in the different systems are often not identical and may have been purified to different extents.