Purification of recombinant trichodysplasia spinulosa-associated polyomavirus VP1-derived virus-like particles using chromatographic techniques

Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences
Mindaugas ZaveckasAlma Gedvilaite

Abstract

Trichodysplasia spinulosa-associated polyomavirus (TSPyV) has been linked to a rare and recently characterized skin disease occurring in immunocompromised patients. In analogy with other polyomaviruses, the major capsid protein VP1 of TSPyV can self-assemble into virus-like particles (VLPs). VLPs are increasingly applied for the vaccination and diagnostics. Mostly, non-scalable and labor intensive ultracentrifugation-based techniques are used for the purification of VLPs. In this work, we developed a purification procedure for TSPyV VP1 VLPs based on two chromatographic steps, ion-exchange monolith and core bead chromatography. Prior to chromatography, ammonium sulfate precipitation was used for the initial purification of TSPyV VP1 VLPs from yeast lysate. The VLPs were further purified using CIMmultus QA ion-exchange monolith in bind-elute mode. Most of TSPyV VP1 VLPs bound to the monolith and were subsequently eluted by a linear NaCl gradient. After ion-exchange monolith chromatography, the purity of TSPyV VP1 protein was about 75%. The final purification step of TSPyV VP1 VLPs was core bead chromatography using Capto Core 700 resin in flow-through mode. After core bead chromatography, 42% of TSPyV VP1 protein was recovered w...Continue Reading

Citations

Jan 24, 2021·Biotechnology and Bioengineering·Lukas GerstweilerAnton Peter Jacob Middelberg
Jun 19, 2021·Journal of Chromatography. a·Xue MiGiorgio Carta
Jul 2, 2021·The Analyst·Sagar DhamaneRichard C Willson

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