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Soluble FMDV VP1 proteins fused with calreticulin expressed in Escherichia coli under the assist of trigger factor16 (Tf16) formed into high immunogenic polymers.

Int J Biol Macromol. 2019;

Liu C, Feng H, Liu Y, Chen Y, Yang S, Deng R, Zhang G.

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Codon Optimization	… No. EU639407) at N or C terminal by using 4 × GGGGS or 5 × GGGGS linker. All these four recombinant fragments, respectively named as rV4C, rC4V rV5F and rF5V, were synthesized after codon optimization by Genscript …	Get A Quote

摘要

Foot and mouth disease virus (FMDV) is a highly contagious pathogen propagating among cloven-hoofed animals. As a major immunogenic protein, VP1 plays a pivotal role in the induction of neutralizing antibodies, which therefore is an ideal target for developing subunit vaccines. In current study, four prokaryotic expression clones (rV4C, rC4V, rV5F and rF5V) were constructed by fusing truncated calreticulin (CRT) (120-250 aa or 120-308 aa) at the N/C terminal of vp1 gene, and co-expressed with chaperone trigger factor 16 (Tf16) in E.coli, respectively. The soluble recombinant CRT-fused VP1 proteins could form into homogeneous reactive polymers with average hydrodynamic diameters around 100 nm according to the d... More