The proper glycosylation of glycoproteins is important for their structure and function. This is an especially important consideration when choosing a platform to express recombinant glycoproteins destined for therapeutic use. Chinese hamster ovary (CHO) cells have been the choice expression platform for their ability to produce recombinant glycoproteins with glycosylation profiles similar to those observed in humans. However, consistency with glycosylation has been noted as problematic, and sialylation, an important modification in human glycoproteins, has not been achieved to an acceptable degree in CHO cells. Plant biotechnology and glycoengineering has now made it possible to produce therapeutic recombinant glycoproteins in plants with glycosylation profiles observed in humans, including sialylation. Furthermore, the glycosylation profiles of recombinant therapeutic glycoproteins produced in plants are homogenous and consistently reproducible. Here, entirely via transient expression, two therapeutic monoclonal antibodies are produced in glycoengineered Nicotiana benthamiana plants that carry human glycosylation profiles including sialylation.
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