I have used both although I use plants more, here are the pros and cons.

Yeast grow super fast at a very cheap cost, the number of cells that you can achieve in 48h with yeast is incredible, if you need a lot of your protein, yeast is the way to go. Besides, there are plenty of vectors available and yeast is easily transformed with basic lab material, you will select your recomninant on plates which are also dirt cheap. Over bacteria (which was not in your question) yeast can make more complex protein than bacteria, and they also possess  vacuoles like plants.

Plants come in different shapes. You ask specifically for plant cell by which I undertsand cell culture in liquid media perhaps ? Well, carrot cells, or tobacco BY2 cell grow well in liquid media (others also do) but most will clump, will get contaminated easily  and are expensive to maintain (compared with yeast), besides they grow slowly. I have not used liquid cell suspension to produce recombinant proteins.

I have used either transient expression in Nicotiana benhtamiana or stable expression in Arabidopsis thaliana. The first will give you your protein after 24-72 hours in relatively small amount but you can scale up to infiltrating many leaves from many plant but it requires logistics. Stable expression takes time (months), but 100% of your cells will express your protein.

To answer your question accuretely you have to ask yourself : what do I want to do with my protein. Test activity (start with yeast), check localisation (plant), bulk amount (yeast), make antibody (yeast), epistatic analysis (stable)

Hope that helps.

1. plant-based platform for commercial production of recombinant protein is usually considered as more cost-effective platform (ex. no need of a constant controlled environment), and a scalable-production platform to allow large-volume manufacturing, when compared to other systems. Grow yeast also have contamination worry.

2. Post-translational modification:

(1) For yeast, one major concern for producing therapeutic glycoprotein for human application is that yeast N-glycosylation is of the high-mannose type, which confers a short half-life in vivo and hyper–immunogenicity and thus render the therapeutic glycoprotein less effective. (attached paper)

3. If you want to isolate those recombinant proteins, I think yeast should be much easy to do that

Dr. Hugo Germain 

Thank you so much for your detailed explanation. I was actually searching for about what you explained in your answer.

With Regards

Sandeep  

Dr. Yuan-Yeu Yau

I did not know about the difference on post translational modification in yeast and plant cell. Thank you for pointing it out. I will read on it and also the paper you have attached. 

Thanks again.

With Regards

Sandeep 

Dr. Yuan-Yeu Yau

You said, "For yeast, one major concern for producing therapeutic glycoprotein for human application is that yeast N-glycosylation is of the high-mannose type, which confers a short half-life in vivo and hyper–immunogenicity and thus render the therapeutic glycoprotein less effective."

Can you kindly tell if it is possible to engineer yeast cells so that they can do post translational modification on the level of plants or may be mammalian cells?

Patiently awaiting for your reply.

Regards

Sandeep

Hi Sandeep K. Panda,

1. One of the problems to produce recombinant proteins (for human use) in bacteria, yeast or plants is the post-translational modification problem. Both yeasts and plants can perform post-translational modification. However, they are somewhat different from mammalian cell's post-translational modification system. Therefore, the biggest advantage for using mammalian cells (such as Chinese hamster ovary (CHO) cells) as bioreactor to produce recombinant proteins for human beings (mammalian) is that the product is humanized. But the cost for mammalian bioreactor is expensive.

2. You asked a very good question. In the paper I attached earlier, it sates "Various attempts have been made to humanize yeast N-glycosylation pathways in order to produce therapeutic glycoproteins with humanized N-glycosylation structure [65]." According to reference [65], the success is limited. The paper was published in 2005. It was 12 years ago. I do not know what is the progress now.

See this paper: The humanization of N-glycosylation pathways in yeast(2005).

Abstract

Yeast and other fungal protein-expression hosts have been extensively used to produce industrial enzymes, and are often the expression system of choice when manufacturing costs are of primary concern. However, for the production of therapeutic glycoproteins intended for use in humans, yeast have been less useful owing to their inability to modify proteins with human glycosylation structures. Yeast N-glycosylation is of the high-mannose type, which confers a short half-life in vivo and thereby compromises the efficacy of most therapeutic glycoproteins. Several approaches to humanizing yeast N-glycosylation pathways have been attempted over the past decade with limited success. Recently however, advances in the glycoengineering of yeast and the expression of therapeutic glycoproteins with humanized N-glycosylation structures have shown significant promise - this review summarizes the most important developments in the field.

As for protein glycosylation in plants:

" The protein glycosylation in plants is slightly different from the mammalian cells; the lack of sialic acid, addition of xylose and change in the core fucose linkage (β1, 6 -> β1, 3) are typical in plant glycoproteins [22]. However, these differences had less impact on the recombinant protein function and now the progress is made towards glycan engineering in plant expression systems. The inactivation/de novo expression of plant glycosyltransferases helps to re-design the glycan structures in the plant glycoprotein for the production of protein glyco-variants similar to protein expressed in mammalian cells [21]." (see attached paper)

We mentioned a lot of glycosylation above. Why it is important:

Glycosylation

Protein glycosylation is acknowledged as one of the major post-translational modifications, with significant effects on protein folding, conformation, distribution, stability and activity. Glycosylation encompasses a diverse selection of sugar-moiety additions to proteins that ranges from simple monosaccharide modifications of nuclear transcription factors to highly complex branched polysaccharide changes of cell surface receptors. Carbohydrates in the form of aspargine-linked (N-linked) or serine/threonine-linked (O-linked) oligosaccharides are major structural components of many cell surface and secreted proteins.

[ From: https://www.thermofisher.com/us/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-post-translational-modification.html ]

Thank you very much. I will go through the papers and the link. 

Regards

Sandeep

Hi ,

If i want to study posttranslational modification (glycosylation) of my desired plant protein. which expression system will be best to study posttranslational modifications. If i want to have my protein in bulk amount and study its medicinal/therapeutic impotrance.  though the glycosylation pattern will be very different but if i want to have this protein in purified form which expression system should i choose. This protein is overexpressed in plants without a tag