Preprint Article Version 1 This version is not peer-reviewed

Expression of Pokeweed Antiviral Protein Isoform S1 (PAP-S1) and of Ricin-A-Chain/PAP-S1 Novel Fusion Protein (RTA/PAP-S1) in Escherichia coli and Their Comparative Inhibition of Protein Synthesis in Vitro

Version 1 : Received: 30 April 2017 / Approved: 1 May 2017 / Online: 1 May 2017 (10:51:21 CEST)

How to cite: Hassan, Y.; Ogg, S. Expression of Pokeweed Antiviral Protein Isoform S1 (PAP-S1) and of Ricin-A-Chain/PAP-S1 Novel Fusion Protein (RTA/PAP-S1) in Escherichia coli and Their Comparative Inhibition of Protein Synthesis in Vitro. Preprints 2017, 2017050015 (doi: 10.20944/preprints201705.0015.v1). Hassan, Y.; Ogg, S. Expression of Pokeweed Antiviral Protein Isoform S1 (PAP-S1) and of Ricin-A-Chain/PAP-S1 Novel Fusion Protein (RTA/PAP-S1) in Escherichia coli and Their Comparative Inhibition of Protein Synthesis in Vitro. Preprints 2017, 2017050015 (doi: 10.20944/preprints201705.0015.v1).

Abstract

Fusion protein therapeutics engineering is advancing to meet the need for novel medicine. Herein, we further characterize the development of novel RTA & PAP-S1 antiviral fusion proteins. In brief, RTA/PAP-S1 and PAP-S1/RTA fusion proteins were produced in both cell free and E. coli in vivo expression systems, purified by His-tag affinity chromatography, and protein synthesis inhibitory activity assayed by comparison to the production of a control protein, CalmL3. Results showed that the RTA/PAP-S1 fusion protein is amenable to standardized production and purification and has both increased potency and less toxicity compared to either RTA or PAP-S1 alone. Thus, this research highlights the developmental potential of novel fusion proteins with reduced cytotoxic risk and increased potency.

Subject Areas

fusion proteins; protein therapeutics; ricin; pokeweed antiviral protein; protein engineering; immunotoxins; ribosome-inactivating proteins.

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