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Strategies for maximizing recombinant protein production in tobacco plants

Plant molecular farming (PMF) is a modern, sophisticated technology that utilizes plants' biosynthetic machinery to synthesize a plethora of recombinant proteins, including industrial and therapeutic enzymes. It has several advantages over traditional approaches, such as microbial fermentation and mammalian cell culture, including lower costs, high-yield production, and absence of human pathogens and endotoxins. Plants also provide considerable flexibility that allows customized protein production.

Tobacco species like Nicotiana benthamiana and Nicotiana tabacum are known for having compromised basal immunity and a less robust ribonucleic acid (RNA) silencing pathway involving the degradation of foreign RNA as a defense mechanism. This, along with its short life cycle and large biomass production capacity, makes it an ideal choice for quick and efficient recombinant protein production.

However, despite these multiple advantages, there are certain limitations to this protein production. Tobacco cells require engineering for specific subcellular localization of each recombinant protein.

While multiple studies explored the recombinant protein production in tobacco, a comprehensive study on subcellular localization strategies was required. A review published in BioDesign Research addresses this issue and focuses on targeting strategies for directing the recombinant proteins to four subcellular compartments—endoplasmic reticulum (ER), vacuole, chloroplast and apoplast.

Providing more context, Dr. Shi-Jian Song, a researcher from the Chinese Academy of Agricultural Sciences, China and one of the corresponding authors of this study, says, "Optimizing subcellular localization for individual target proteins is crucial for successful protein synthesis and its utilization in the pharmacological industry."

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