Expression data of antibody fragments from Saccharomyces cerevisiae

Saccharomyces cerevisiae has been used as a secretion host for production of various products, including pharmaceuticals. However, few antibody molecules have been functionally expressed in S. cerevisiae due to the incompatible surface glycosylation. Our laboratory previously isolated a group of yeast mutant strains with different α-amylase secretory capacities, and these evolved strains have showed advantages for production of some heterologous proteins. However, it is not known whether these secretory strains are generally suitable for pharmaceutical protein production. Here, three non-glycosylated antibody fragments with different configurations (Ran-Fab fragment Ranibizumab, Pex-the scFv peptide Pexelizumab, and Nan-a single V-type domain) were successfully expressed and secreted in three background strains with different secretory capacities, including HA (wild type), MA (evolved strain), and LA (evolved strain). However, the secretion of Ran and Nan were positively correlated with the strains’ secretory capacity, while Pex was most efficiently secreted in the parental strain. Therefore, transcriptional analysis was performed to explore the fundamental changes triggered by the expression of the different pharmaceutical proteins in these selected yeast strains. To gain a sufficient comparative information, we designed a sample pool: four constructed strains LA.Nan, HA.Nan, LA.Pex and HA.Pex, each strain has biological triplicates. The expression of antibody fragments Nan and Pex has a opposite trend in the LA and HA strains. The production of Nan was higher in the HA.Nan strain in comparison to the LA.Nan strain. On the contrary, the production of Pex was lower in the HA.Pex strain than in the LA.Pex strain.