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Updated: Jun 11, 2026
Efficient and Scalable Production of Full-length Human Huntingtin Variants in Mammalian Cells using a Transient Expression System
Published on: December 10, 2021
Production and single-step purification of Brugia malayi abundant larval transcript (ALT-2) using hydrophobic
Surianarayanan Bhuvanesh1, Chakkaravarthi Arunkumar, Perumal Kaliraj
1Centre for Biotechnology, Anna University, Chennai 600025, India.
Abstract:
Abundant larval transcript (ALT), a novel filarial protein, has been shown to have great potential as a vaccine in the prevention of human lymphatic filariasis. In this study, we report a method for the production of recombinant ALT-2 protein, expressed in the cytoplasm of bacterium Escherichia coli in soluble form and purification in a single step using hydrophobic interaction chromatography (HIC). Fermentation was done by continuous fed-batch methodology with dissolved oxygen (DO)-controlled feed addition. The culture was induced with 1 mM isopropyl-β-D: -thiogalactopyranoside (IPTG). Up to 9 g/l dry cell weight (DCW) of biomass was obtained from 1.6 l of Luria-Bertani (LB) broth in a bench-scale reactor. Around 200 mg/l of purified ALT-2 with a yield of about 60% was obtained. This is almost a 2.5-fold increase in final protein yield compared to purification using immobilized metal affinity chromatography (IMAC).
