Table 1.

Expression platforms used for recombinant dengue protein expression

	Strengths	Weaknesses	References
Eschericia coli	-Easy to produce -High level expression* of E domain III -Low cost of goods	-Lack of post-translational modifications – not able to support proper folding of E -Low level expression#of full-length or truncated E	31–35
Saccharomyces cerevisciae	-Easy to produce -High level expression of E domain III -Low cost of goods	-Hyperglycosylation -Lack of native conformation for E → low immunogenicity -Low level expression of full-length or truncated E	47
Pichia pastoris	-Easy to produce -High level expression of E domain III -Low cost of goods	-Lack of native conformation for E → low immunogenicity -Low level expression of full-length or truncated E	42, 43, Clements et al., unpublished data
Chinese Hamster Ovary DHFR system	-Capable of producing proteins with native conformation	-Expression levels very low -Moderate cost of goods	Coller et al. unpublished data
Vaccinia expression in mammalian cells	-Capable of producing proteins with native conformation -Immunogenicity demonstrated in mice	-Expression levels low -Not a commercially viable production system (safety and expression)	41
Baculovirus in Sf9 or High Five cells	-Capable of producing proteins with native conformation -Immunogenicity demonstrated in mice	-Expression levels moderate@ -Moderate cost of goods	30, 36–40
Stably transformed Drosophila S2 cells	-Produces proteins with native conformation -High expression levels for truncated E (> 10 mg/L) -Immunogenicity and efficacy in primates	-Expression platform not yet registered for a commercial product -Moderate cost of goods	54, 55

^*High expression level > 10 mg/L

^@Moderate expression level > 1 mg/L < 10 mg/L

^#Low expression level < 1 mg/L