Proteomics

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The red alga Porphyridium as a host for molecular farming: Efficient production of immunologically active hepatitis C virus glycoprotein


ABSTRACT: Microalgae are promising production platforms for the cost-effective production of recombinant proteins. We have recently established that the red alga Porphyridium purpureum provides superior transgene expression properties, due to the episomal main- tenance of transformation vectors as multicopy plasmids in the nucleus. Here, we have explored the potential of Porphyridium to synthesize complex pharmaceutical proteins to high levels. Testing expression constructs for a candidate subunit vaccine against the hepatitis C virus (HCV), we show that the soluble HCV E2 glycoprotein can be produced in transgenic algal cultures to high levels. The antigen undergoes faithful posttranslational modification by N-glycosylation and is recognized by conformationally selective antibodies, suggesting that it adopts a proper antigenic conformation in the endoplasmic reticulum of red algal cells. We also report the experimental determina- tion of the structure of the N-glycan moiety that is attached to glycosylated proteins in Porphyridium. Finally, we demonstrate the immunogenicity of the HCV antigen produced in red algae when administered by injection as pure protein or by feeding of algal biomass.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Porphyridium Purpureum

SUBMITTER: Lara Hoepfner  

LAB HEAD: Michael Hippler

PROVIDER: PXD052401 | Pride | 2024-05-21

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
2023-04-17-decoys-contam-Porphyridium_purpuneum_HCV_HBV.fasta.fas Fasta
HL_170423_HCV_1h_80ISF_750ng_120ms.raw Raw
Identified_HCV_peptides.txt Txt
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