NT*-HRV3CP: An optimized construct of human rhinovirus 14 3C protease for high-yield expression and fast affinity-tag cleavage

J Biotechnol. 2021 Jan 10:325:145-151. doi: 10.1016/j.jbiotec.2020.11.005. Epub 2020 Nov 6.

Abstract

The human rhinovirus 14 3C protease (HRV3C protease), in fusion with glutathione S-transferase also referred to as PreScission™ protease, is a cysteine protease of particular interest for affinity tag removal from fusion proteins due to its stringent recognition sequence specificity (LEVLFQ/GX) and superior activity at low temperature. Here we report the expression, purification and use of a fusion construct of HRV3C protease, NT*-HRV3CP, that affords high expression yield in E. coli (over 300 mg/L cell culture), facile single-step purification, high solubility (>10 mg/mL) and excellent storage properties. NT*-HRV3CP cleaves affinity tags at 4 °C in minutes, making it an attractive tool for the production of recombinant proteins for biotechnological, industrial and pharmaceutical applications.

Keywords: Fusion tag cleavage; Human rhinovirus 14 3C protease; NT* fusion protein; PreScission protease.

MeSH terms

  • 3C Viral Proteases
  • Chromatography, Affinity
  • Cysteine Endopeptidases / genetics
  • Enterovirus
  • Escherichia coli* / genetics
  • Humans
  • Peptide Hydrolases*
  • Recombinant Fusion Proteins / genetics
  • Rhinovirus / genetics

Substances

  • Recombinant Fusion Proteins
  • Peptide Hydrolases
  • Cysteine Endopeptidases
  • 3C Viral Proteases

Supplementary concepts

  • Rhinovirus B