ArticleCommunications biology2026
Two-in-one protein tag enables the soluble expression and calcium-dependent purification of single-chain antibody fragments.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
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Authors and funding
8 authors.
Funding
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.
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