Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris

Genome sequence of the recombinant protein production host Pichia pastoris

“…P. pastoris grows to high cell density, provides tightly controlled methanol-inducible transgene expression and efficiently secretes heterologous proteins in defined media. Several P. pastoris-produced biopharmaceuticals that are either not glycosylated (such as human serum albumin 2 ) or for which glycosylation is needed only for proper folding (such as several vaccines 3 ) are already on the market. An important recent breakthrough has been the development of P. pastoris strains with humantype N-glycosylation [4][5][6] .…”

Poster session

“…Affinity separation is a well stablished technique for the purification and recovery of biological molecules [4,3]. Within this tecnique, mAb for Hepatitis B surface antigen immunopurification have been successfully used to obtain this antigen for human use [6][7][8] but regulatory constrains of mAb production in animals, the high cost and the low scale-up capacity of mammalian cell culture production brakes the massive application of this technique for large-scale production of this biological. Alternatively, the use of plants for antibody production has gained great importance in the last years [9,10].…”

Application of Quality by Design Paradigm to the Manufacture of Protein Therapeutics

“…Although yeast can perform many PTMs, similar to higher eukaryotic cells, they produce a non-human N-glycosylation profile of high mannose content, which can elicit an immune response in humans. Therefore microbial expression systems are only employed in the production of therapeutic proteins if the protein is functional without PTM, such as human insulin which is produced in E. coli [128], or where the PTM is required for folding and stability but does not affect drug efficacy, such as in several vaccines which are produced in Pichia pastoris [129,130] (examples are presented in Table 2). …”