There are currently many systems currently available for recombinant protein expression. Currently there are no bacterial systems that are able to produce proteins with mammalian-like glycosylation. Extensive glycosylation is of paramount for the function eukaryotic cell surface antigens for example and must be present when expressed recombinantly. This system solves the problem of generating fully functioning recombinant proteins, presenting the correct folding and post-translational modifications. Such a tool is envisaged to be useful in generating a wide variety of recombinant eukaryotic proteins from higher organisms.
