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Research in plants producing human antibodies!!?

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Research in plants producing human antibodies!!?

Postby seamoro » Wed Jul 01, 2009 6:15 pm

I thinking of doing my PhD in manipulating plants to produce antibodies for humans. I’m kind of stuck on the part of working out the gene that makes the antibody?...I know they are companies online that can produce a specific antibody from injecting a mammal with an antigen. I think I can get 20uL for a cost. I assume I derive the DNA sequence from this, thus allowing me to create the gene.....right?..through an automated technique. I guess my question is...what technique I need to determine the DNA of the antibody?.....how much antibody do I need to use with this technique?...any other advice you could give me would greatly appreciated. Also, understand I haven’t started the PhD...I am just preparing the research proposal.
Thanks in advance
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Re: Research in plants producing human antibodies!!?

Postby jonmoulton » Wed Jul 01, 2009 10:47 pm

A place you are likely to run into problems is in getting the pattern of glycosylation right. B cells & plasma cells attach sugars to antibodies. The pattern of glycosylation might be critical for interaction with other systems in the animal, such as T cells or complement proteins. Can you get the plant to attach sugars in similar places?
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Postby MrMistery » Thu Jul 02, 2009 1:45 am

as far as I know, glycosylation signals are conserved among all eukaryotes. For example, I just expressed chicken avidin into yeast and it gets glycosylated just fine
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Postby biohazard » Thu Jul 02, 2009 6:04 am

There are differences in glycosylation even among eukaryotes, and even among quite closely related species. Yeasts often over-glycosylate their products, although this is not to say they couldn't get it right in many cases. Even such commonly used species as S. cerevisiae and P. pastoris can have differences in glycosylation if you express the same protein in them.

Unfortunately I don't remember what was the case with plants and glycosylation, but like Jonmoulton said, antibodies have very specific places for sugar residues that you need to get right (in some proteins sugars don't play a crucial role, but here you might want them in their right places). Then again, if I recall correctly, they make (humanised) recombinant proteins for therapeutical uses even in E. coli (a species that has no clue about glycosylation whatsoever...)

Another problem you may encounter with plants is protein extraction: it is much more laborous to isolate your specific proteins from plant mass than it is from neatly secreted products that hybridoma cells and bacteria make.
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Postby roman » Wed Nov 04, 2009 7:38 am

Plant is not a good host for you to generate human antibodies.The glycosylation is different bewteen plants and human.
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Postby JackBean » Wed Nov 04, 2009 8:26 am

Really, why that are produces plantibodies, than?
I also don't think, that his aim is to isolate the antibodies, instead use the plants as food probably.
http://www.biolib.cz/en/main/
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