ArticleJournal of natural medicines2018
Different expression systems resulted in varied binding properties of anti-paclitaxel single-chain variable fragment antibody clone 1C2.
Article in Journal of natural medicines, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 9 citations in OpenAlex.
- Anti-tau intrabodies: From anti-tau immunoglobulins to the development of functional scFv intrabodies.Molecular therapy. Methods & clinical development · 2023Article
- Plant-made antibody against miroestrol: a new platform for expression of full-length immunoglobulin G against small-molecule targets in immunoassays.Plant cell reports · 2021Article
- Expression of actively soluble antigen-binding fragment (Fab) antibody and GFP fused Fab in the cytoplasm of the engineered Escherichia coli.Molecular biology reports · 2020Article
- Engineering a single-chain antibody against Trypanosoma cruzi metacyclic trypomastigotes to block cell invasion.PloS one · 2019Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The binding properties of recombinant antibody fragments, such as affinity and specificity, determine their usefulness for therapeutic and analytical applications. Anti-paclitaxel single-chain variable fragment clone 1C2 (anti-PT scFv1C2) was expressed using Escherichia coli cell and Bombyx mori larvae expression systems. The binding characteristics of the scFvs were evaluated using indirect competitive ELISA. The linear range of binding between anti-PT scFv1C2 and paclitaxel was significantly different between the anti-PT scFv1C2s derived from E. coli (1.056-5.700 μg/ml) and B. mori (7.813-1000 ng/ml), which indicated that different expression systems resulted in different sensitivities for paclitaxel determination. In addition, the binding specificity of anti-PT scFv1C2 varied between expression systems. This finding implied that the expression system significantly affects the binding properties of recombinant antibodies, especially antibodies against low-molecular-weight targets.
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