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Opinión actual en biología vegetal
Banda 71,
February 2023
, 102331
Author links open overlay panel
https://doi.org/10.1016/j.pbi.2022.102331Get rights and content
resume
Soy is one of the most important protein sources for human and animal nutrition. Soybean production also allows for the biosynthesis of edible oils, biodiesel, and biofertilizers. With the advent of modern agricultural biotechnology, soybean plants have also become bioreactors for therapeutic proteins and industrial enzymes. The properties of soybean, such as protein storage vacuoles (PSVs) and other unique organelles, allow the plant to be used as an accumulator of heterologous proteins under conditions of high stability and scalability, while retaining its basic functions. This review reports the main aspects of heterologous protein accumulation in soybean PSV.
excerpts section
Together as recombinant protein bioreactors
Plants have emerged as a viable alternative to microbial fermentation and mammalian cell culture for the production of industrial enzymes and recombinant pharmaceutical proteins, a process known as plant culture [1]. Inexpensive and scalable methods of recombinant protein production are highly desirable [2]. The plant-based system offers a number of advantages over other systems, such as B. Scalability; low production costs and are free of human pathogens, microbial toxins, prions or oncogenes
Soybeans as a storage enhancer of heterologous protein accumulation
Many legume seed storage protein gene promoters have previously been shown to direct the correct transcription of exogenous genes in seeds, and the corresponding recombinant proteins have primarily been shown to pattern processing and intracellular transport in developing seeds [5]. Among dicot promoters, those from legumes appear to offer the most significant potential for protein accumulation at high levels [13]. Some of them have already been validated as
Soy protein storage vacuoles (PSV)
Plant vacuoles are commonly divided into two categories: i) LV (lytic vacuoles), acidic organelles corresponding to mammalian lysosomes that harbor hydrolases for protein degradation and are predominantly observed in vegetative tissues ii) PSV, specialized vacuoles found In organs protein storage facilities are found, such as seeds, which are capable of accumulating, storing and preserving large amounts of protein [47,48].
PSVs are unique membranous subcellular structures whose membrane is derived from plasma
Protein-targeted soybean PSVs
Between 1982 and 1986 the first studies were published showing in more detail the regulatory elements of the α' subunit of the β-conglycinin protein that is directed and stored in the PSV of soybean plants [56, 59, 60, 61]. . Since then, various efforts have allowed for a better understanding of the molecular mechanisms of protein targeting for soybean-derived PSVs. Recently, soybean PSVs have gained prominence and several molecules have been created that target these subcellular compartments.
Conclusion and future directions
Soybean-derived PSVs have been used as a platform for large-scale and stable expression of various functional heterologous proteins. The high production that is obtained for most of the proteins when using this system allows obtaining them at a lower cost. This fact becomes fundamental due to the large volume that some drug candidates require to go through all the necessary stages of clinical evaluation. According to O'keefe et al., 2015, one of the difficulties in comprehensively evaluating the CV-N as a
financing
This work was funded by Embrapa Genetic Resources and Biotechnology/National Institute of Science and Technology in Synthetic Biology, CNPq - National Council for Scientific and Technological Development (465603/2014-9), FAP/DF - District Research Support Foundation Federal (0193.001.262/2017) and CAPES - Coordination for the improvement of university personnel.
Conflict of Interest Statement
The authors declare that they have no competing financial interests or known personal relationships that might influence the work described in this article.
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