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Updated: Jul 18, 2026

Modifying Baculovirus Expression Vectors to Produce Secreted Plant Proteins in Insect Cells
Published on: August 20, 2018
Structural requirements of signal peptide in insect cell
Yoshinori Tsuchiya1, Kazuki Morioka, Jyunsuke Shirai
1Department of Exotic Diseases, National Institute of Animal Health, Jyosuihoncho 6-20-1, Kodaira, Tokyo 187-0022, Japan.
Abstract:
In order to increase the proteinic secretion quantity of production in insect cell, the N-terminal and the hydrophobic core region of the chicken lysozyme signal peptide (CLSP) was altered. A hybrid gene composed of CLSP gene and human lysozyme (HLY) gene from short DNA oligomers was used for the production of recombinant HLY in insect cell using vacuole virus expression system. In contrast with the results in yeast, the introduction of basic residues in the N-terminal region did not make the amount of secretion increase in insect cell. On the other hand, when the sequence of CLSP was changed into Leu-rich type, the amount of HLY secretion increased sharply. Although they are eukaryotes, the structural requirements of signal peptides may have some differences in yeast and insect cell.
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