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Updated: May 1, 2026
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Fusion Partner Facilitates Expression of Cell-Penetrating Peptide L2 in Pichia pastoris
Xuan Li1,2,3, Na Yang1,2,3, Yuxin Fang4
1Gene Engineering Laboratory, Feed Research Institute, Chinese Academy of Agricultural Sciences, 12 Zhongguancun Nandajie St., Haidian District, Beijing 100081, China.
Background:
L2 is formed by combining the pheromone of Streptococcus agalactiae (S. agalactiae) and a cell-penetrating peptide (CPP) with cell-penetrating selectivity. L2 has more significant penetration and better specificity for killing S. agalactiae. However, the production of AMPs by chemical synthesis is always a challenge because of the production cost.
Methods:
This study was devoted to the heterologous expression of the cell-penetrating peptide L2 in Pichia pastoris using SUMO and a short acidic fusion tag as fusion partners, and the high-density expression of SUMO-L2 was achieved in a 5 L fermenter.
Results:
The results showed that SUMO-L2 expression in the 5 L fermenter reached 629 mg/L. The antibacterial activity of recombinant L2 was examined; the minimum inhibitory concentration (MICs) and minimum bactericidal concentration (MBCs) of purified L2 were 4-8 μg/mL and 8-16 μg/mL against S. agalactiae after 84 h of lysis with 50% formic acid.
Conclusions:
The findings suggest that SUMO is a suitable fusion tag to express cell-penetrating peptide L2.
