GLYCOSYLATION

Anton Scott Goustin asg at cmb.biosci.wayne.edu
Thu Sep 14 18:57:25 EST 1995


bLangridge at ccmail.llu.edu (Bill Langridge) wrote:
>Can anyone tell me if I were to make a glycolsylated viral (HIV) 
>protein in plants, baculovirus or Pichia system. Will all these systems 
>make the proper glycosylation pattern identical to the host protein? In 
>which system would I expect the most deviation from the normal 
>glysoylation pattern?
>
>Thanks for your help!
>
>Bill Langridge
>
All systems suffer from a similar problem:  if you drive expression of 
the protein too high, the ER-Golgi can't keep up with glycosylation 
machinery and the proteins come up under-glycosylated.  If you want the 
most native glycosylation pattern, you will have to sacrifice yield.  
For example, harvest early in the baculovirus system.  Warning:  if you 
are thinking about HIV-1 gp120 or gp160:  it's been done before and it 
is not straigtforward.  Cells don't like to make (much) gp120 or gp160.





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