PT  - JOURNAL ARTICLE
AU  - Aram Shaldzhyan
AU  - Nikita Yolshin
AU  - Yana Zabrodskaya
AU  - Tatiana Kudling
AU  - Alexey Lozhkov
AU  - Marina Plotnikova
AU  - Edward Ramsay
AU  - Aleksandr Taraskin
AU  - Peter Nekrasov
AU  - Mikhail Grudinin
AU  - Andrey Vasin
TI  - CLEAN AND FOLDED: OPTIMIZED PRODUCTION OF HIGH QUALITY RECOMBINANT HUMAN INTERFERON-Λ1
AID  - 10.1101/2020.12.09.417527
DP  - 2020 Jan 01
TA  - bioRxiv
PG  - 2020.12.09.417527
4099  - http://biorxiv.org/content/early/2020/12/10/2020.12.09.417527.short
4100  - http://biorxiv.org/content/early/2020/12/10/2020.12.09.417527.full
AB  - Type III interferons exhibit antiviral activity against influenza viruses, coronaviruses, rotaviruses, and others. In addition, this type of interferon theoretically has therapeutic advantages, in comparison with type I interferons, due to its ability to activate a narrower group of genes in a relatively small group of target cells. Hence, it can elicit more targeted antiviral or immunomodulatory responses. Obtaining biologically-active interferon lambda (hIFN-λ1) is fraught with difficulties at the stage of expression in soluble form or, in the case of expression in the form of inclusion bodies, at the stage of refolding. In this work, hIFN-λ1 was expressed in the form of inclusion bodies, and a simple, effective refolding method was developed. Efficient and scalable methods for chromatographic purification of recombinant hIFN-λ1 were also developed. High-yield, high-purity product was obtained through optimization of several processes including: recombinant protein expression; metal affinity chromatography; cation exchange chromatography; and an intermediate protein refolding stage. The obtained protein was shown to have expected, specific biological activity in line with published effects: induction of MxA gene expression in A549 cells.Competing Interest StatementThe authors have declared no competing interest.