ArticleAMB Express2016
Bioscreening and expression of a camel anti-CTGF VHH nanobody and its renaturation by a novel dialysis-dilution method.
Article in AMB Express, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- A Panel of VHH Antibodies Against Sabin Type 1 Poliovirus D-Antigen Reveals Strain-Specific and Cross-Serotype Reactivity.Viruses · 2026Article
- Large-Scale Production of Anti-RNase A VHH Expressed inCurrent issues in molecular biology · 2023Article
- Review of therapeutic mechanisms and applications based on SARS-CoV-2 neutralizing antibodies.Frontiers in microbiology · 2023Review
- Identification and Characterization of a Novel Nanobody Against Human CTGF to Reveal Its Antifibrotic Effect in an in vitro Model of Liver Fibrosis.International journal of nanomedicine · 2023Article
- Production of Single-Domain Antibodies in Pichia pastoris.Methods in molecular biology (Clifton, N.J.) · 2022Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The variable regions of the camel heavy chain antibody, also known as nanobody is the smallest antibody with antigen-binding efficiency. CTGF is considered important during extracellular matrix deposition which was involved in the pathogenesis of fibrosis related diseases. There are several anti-CTGF-C nanobody drugs under developing in pharmacy. In this study, we described the screening of a novel anti-CTGF-C nanobody from the peripheral blood of immunized camel by phage display. The screened nanobody was further expressed and purified from E. coli cells. A sophisticated dialysis-dilution method was designed for the in vitro refolding of the nanobody. The results showed that the expressed nanobody was consisted of 135 amino acid and mainly expressed as inclusion body in E. coli cells. The dialysis-dilution method was very effective and the recovery rate of the renaturation was more than 80 %. The ELISA result suggested the nanobody had been well refolded showing a superior CTGF binding activity to the commercial mouse anti-CTGF-C mAb. In conclusion, the anti-CTGF-C nonobody had been successfully screened by phage display. The dialysis-dilution refolding method was very effective and the recovery rate reached over 80 %.
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