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Updated: Jul 5, 2025

Production of IgG Fusion Proteins Transiently Expressed in Nicotiana benthamiana
Published on: January 16, 2021
Expressing recombinant human lactoferrin with antibacterial activity in Nicotiana benthamiana
Kenji Miura1,2, Yuriko Nagai2, Akira Yokouchi3
1Faculty of Life and Environmental Sciences, University of Tsukuba, Ibaraki 305-8572, Japan.
Abstract:
Lactoferrin is a non-hematic iron-binding 80-kDa protein that exhibits antimicrobial activity. Higher plants function as "green bioreactors" for large-scale recombinant protein production. In this study, we transiently expressed recombinant human lactoferrin (rhLF) in Nicotiana benthamiana at a yield of approximately 40 µg g-1 fresh mass (gFM) using the Tsukuba system. Additionally, the expression level of rhLF increased when it was fused with KDEL, an endoplasmic reticulum retention motif. Purified plant-derived rhLF possesses antibacterial activity that inhibits the growth of Escherichia coli. These results indicated that rhLF containing antimicrobial activity can be produced in N. benthamiana using the Tsukuba system.

