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.
