"Mammalian cell cultures currently used for most therapeutic protein production produce a mixture of glycoforms and typically do not allow for the control of glycosylation," [GTCB would probably disagree with this assertion—see #msg-9352093]
I extracted the pertinent passages, which may or may not fully address the question. IMHO they do not:
The advantage of mammalian production is that the basic protein structure itself--what I'm talking about are the amino acids, their sequence, and how they're physically structured--is very much the same. The difference is in what's known as the sugars or carbohydrates--what the scientists like to call the "glycosylation pattern." The glycosylation pattern in each biologic system will be different. The issue isn't, "Is it different?" The answer to that is "Yes." The issue is, "Does it mean anything?"
Now to some degree, there are really two issues that you're concerned about with glycosylation. One is when it's given to a person, will the person's immune system react to it and try to kill it, quote unquote, by having a reaction, or will you end up with a material that doesn't have a sufficient half life [because] it gets cleared out by the liver too fast so that you don't have a practical medicine?
For the most part, we've determined that that's not a problem for transgenic mammalian production just as it's typically not a big problem for bioreactor-based materials that have had to face exactly the same issue.
Now, let's assume for a moment that you do run into a glycosylation pattern that's a challenge. Does that mean you can't do it? Well, typically the answer is no. You still have options. One is if we know that there's a glycosylation pattern early on we have some flexibility in making this DNA construct to try to adjust the glycosylation pattern. That's one way to try and address it.
Another way is, after the protein's been made and the mammary gland comes out, we can do what's known as "post-translational modification." That's typically the use of some sort of an enzyme to either add a sugar or snip a sugar off or perhaps snip the entire sugar off so you just have the base protein. And in that way you can attempt to treat the molecule to get to the kind of profile that you need. But the main basic message is that each biologic system does make protein slightly differently in the glycosylation, and that's usually not a showstopper. You usually have options to try to address that.
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