Introduction of an N-Glycosylation Site Increases Secretion of Heterologous Proteins in Yeasts

AUTOR(ES)

Sagt, C. M. J.

FONTE

American Society for Microbiology

RESUMO

Saccharomyces cerevisiae is often used to produce heterologous proteins that are preferentially secreted to increase economic feasibility. We used N-glycosylation as a tool to enhance protein secretion. Secretion of cutinase, a lipase, and llama VHH antibody fragments by S. cerevisiae or Pichia pastoris improved following the introduction of an N-glycosylation site. When we introduced an N-glycosylation consensus sequence in the N-terminal region of a hydrophobic cutinase, secretion increased fivefold. If an N-glycosylation site was introduced in the C-terminal region, however, secretion increased only 1.8-fold. These results indicate that the use of N glycosylation can significantly enhance heterologous protein secretion.

Documentos Relacionados

• N-glycosylation in sugarcane
• Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site.
• Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition of an N-glycosylation site.
• Membrane topology influences N-glycosylation of the prion protein
• Mannose corrects altered N-glycosylation in carbohydrate-deficient glycoprotein syndrome fibroblasts.