Two-in-one protein tag enables the soluble expression and calcium-dependent purification of single-chain antibody fragments

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Authors: Jonghwan Lee, Heesun Park, Suhyeon Jeong, Kyuhyuk Im, Seho Park, Sangyong Jon, Sanguine Byun, Sunghyun Kim
Cited by: 2
References: 56

Abstract

Single-chain variable fragments (scFvs) antibodies are used in diagnostic and therapeutic biopharmaceuticals. However, its production is limited due to insoluble expression and lack of a universal purification ligand. Here, we report a novel two-in-one protein tag, termed CSQ-tag, utilizing a calsequestrin (CSQ) protein to enable the soluble expression and calcium-dependent purification for scFvs. The CSQ-tag enhanced the solubility of four different therapeutic scFvs with an average solubility of 83.8 ± 4.6% in the BL21(DE3) strain, despite its reducing cytoplasmic environment. Compared to other tags, CSQ-tag showed superior solubility, with 1.8-fold higher solubility than MBP-tag across four scFvs. The solubility enhancement of the CSQ-tag is attributed to two main characteristics: highly acidic sequences with a low isoelectric point of 3.95, and intrinsically disordered protein properties. Furthermore, CSQ-tag can cost-effectively purify therapeutic scFvs with high purity over 95% using the calcium-dependent phase transition properties. Importantly, the anti-VEGF-scFv produced with the CSQ-tag showed a binding affinity of 25.8 pM, similar to that of the existing therapeutic brolucizumab. Therefore, CSQ-tag can significantly improve productivity and simultaneously maintain scFvs' functional integrity, thereby serving as a promising tool for universal expression and purification of therapeutic scFvs.

Fields of Study & Subjects

Monoclonal and Polyclonal Antibodies Research Protein purification and stability HER2/EGFR in Cancer Research

Publication details

Journal / source
Communications Biology
Publisher
Springer Science and Business Media LLC
Volume
9
Issue
1
Publication date
26 January 2026
Language
EN