Multimer of the antimicrobial peptide Mytichitin-A expressed in Chlamydomonas reinhardtii exerts a broader antibacterial spectrum and increased potency.

In this study, an antimicrobial peptide composed of three tandem repeats of Mytichitin-A (3 × Mytichitin-A) with a designed molecular weight of approximately 25 kDa was expressed in the green alga Chlamydomonas reinhardtii. The yield of 3 × Mytichitin-A reached 0.28% of the total soluble protein of the 3 × Mytichitin-A-expressing transgenic cells and the expression level was stable following continuous passaging of the cells for six months.

A novel bicistronic expression system composed of the intraflagellar transport protein gene ift25 and FMDV 2A sequence directs robust nuclear gene expression in Chlamydomonas reinhardtii.

Chlamydomonas reinhardtii offers a great promise for large-scale production of multiple recombinant proteins of pharmaceutical and industrial interest. However, the nuclear-encoding transgenes usually are expressed at a low level, which severely hampers the use of this alga in molecular farming. In this study, the promoter of the endogenous intraflagellar transport 25 (IFT25) gene of C.