Why do we use Saccharomyces cerevisiae for insulin production as opposed to Picha pastoris?
Surely the hyperglycosylation of S. cervisae would trigger an immunogenic response in humans, P. pastoris doesnt hyper glycosylate to the same degree and is easier to humanise its protein production.
Also why make insulin in yeast at all-to make a therapeutic protein your best bet for it not to be immunogenic is to go with some mamalian cell host.
Obviously insulin production in S. cervisae isnt immunogenic otherwise people wouldnt do it, but how was this overcome?
If its a matter of engineering the strain to immobilize or somehow prevent an immunogenic reaction, why not use the same or similar technique (theoretically) for all therapeutic proteins made in recombinant expression systems-it would eliminate the need for mamalian cell expression hostes (theoretically) which are much more expensive to use and time consuming than expression hosts of lower organisms.
Hi there,
Insulin is not naturally glycosylated therefore its production in S. cerevisiae is not a problem at the immunogenic level.
Production of therapeutic proteins is optimized on a case-by-case base - mammalian systems are predominantly used where correct glycosylation matters.
- Badges
- Science topic
- Similar topics
- Biological Science
- Molecular Biology
- Biomolecules
- Proteins