Site-Specific Glycosylation of Recombinant Viral Glycoproteins Produced in Nicotiana benthamiana

There is an urgent need to establish large scale biopharmaceutical manufacturing capacity in Africa where the infrastructure for biologics production severely limited. Molecular farming, whereby pharmaceuticals are produced plants, offers a cheaper alternative mainstream expression platforms, and amenable rapid large-scale production. However, there several differences along plant protein secretory pathway compared mammalian systems, which constrain of complex pharmaceuticals. Viral envelope glycoproteins important targets immunization, yet some cases they accumulate poorly plants may not be properly processed. Whilst co-expression human chaperones furin proteases has shown promise, it presently unclear how plant-specific glycosylation impact these proteins. In many necessary reproduce features their native produce immunologically relevant vaccines, given that central folding immunogenicity antigens. Building on previous work, we transiently expressed model from HIV Marburg virus Nicotiana benthamiana cells. The proteins were purified site-specific was determined by mass-spectrometry. Both yielded increased amounts aggregates when equivalent cell-derived profiles plant-produced distinct cell proteins: displayed lower levels glycan occupancy, reduced glycans paucimannosidic structures. elucidation viral N. step toward producing heterologous with authentic human-like glycosylation.