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. 2020 Jun 24;11:1172. doi: 10.3389/fmicb.2020.01172

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Copyright © 2020 Santajit, Seesuay, Mahasongkram, Sookrung, Pumirat, Ampawong, Reamtong, Chongsa-Nguan, Chaicumpa and Indrawattana.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Production and characterization of HuscFvs to 3O-C12-HSL. (A) Schematic diagram of the inserted DNA construct in pLATE52 where the DNA sequence coding for HuscFv (vh-linker-vl) was flanked with DNA sequences of 6 × His at the 5′ end and E-tag at the 3′ end. (B) Amplicons of huscfv-LIC fragments (∼ 850 bp) for sub-cloning into pLATE52 vector. M, 100 bp-plus DNA ladder; 1–3, huscfv-LIC amplicons of three representatives transformed NiCo21(DE3) E. coli clones. Numbers at the left are DNA sizes in bp. (C) Stained SDS-PAGE-separated purified recombinant HuscFvs. M, protein standard; 1–3, purified HuscFv-E44, HuscFv-F15 and HuscFv-F19, respectively. Numbers at the left are protein masses in kDa. (D) CD spectra of the refolded HuscFv-E44, HuscFv-F15, and HuscFv-F19.