Scientists explore synthesis of griffithsin in cell-free systems biorxivpreprint UMBC Synthesis Griffithsin CellFreeSystems
By Tarun Sai LomteDec 28 2022Reviewed by Aimee Molineux A recent study posted to the bioRxiv* preprint server described the cell-free manufacturing of griffithsin , a broad-spectrum antiviral protein.
The study and findings In the present study, researchers described an approach for the rapid production of GRFT using plant-based and bacterial cell-free protein synthesis methods. First, GRFT CFPS was evaluated in Escherichia coli using a gene containing the frequently used codons. This resulted in a low product solubility and yield , despite tweaking expression temperatures, chaperone additions, ionic strengths, amino acid concentrations, and incubation times.
Microsomal accumulation with the pALiCE-02 plasmid was not detected, whereas with the other plasmid, the total protein yield was 410 μg/ml, and the product was 75% soluble. The tagged product was purified by immobilized metal affinity chromatography with a recovery of 36% after imidazole elution. Around 33% of the tagged-GRFT mix was collected in the flow-through fraction, suggestive of incomplete collection.
Next, the researchers determined if GRFT was functionally active against viruses. The protein was first assessed for its ability to bind to the envelope glycoprotein of the human immunodeficiency virus . ALiCE and E. coli cell-free system-expressed GRFT exhibited a comparable binding affinity to gp120, implying that both CFPS systems could yield active GRFT.
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