ABSTRACT

Proteins that require extensive modifications for in vivo activity will need to be analyzed extensively prior to use as therapeutics, vaccines, or pharmacologic agents. In summary, the baculovirus expression system is a valuable resource for pharmaceutical research projects to produce vaccines, therapeutic proteins and research tools. The engineered FG gene encodes the first 489 amino acids of the F glycoprotein, including the signal sequences but lacking the carboxyl terminal anchor region. Genes from plants, fungi, viruses, bacteria, and animals have been expressed and found to be active when produced in infected insect cells. The protein is composed of three domains, a 319 amino acid extracellular domain containing seven potential glycosylation sites, a 21 amino acid transmembrane domain, and a 217 amino acid cytoplasmic domain. Tissue plasminogen activator became a model enzymatically active glycoprotein to evaluate in insect cells.