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Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi

100%

Kruszewska J. S., Perlińska-Lenart U., Górka-Nieć W., Orłowski J., Zembek P., Palamarczyk G.

2008

vol. 55

issue 3

447-456

Due to its natural properties, Trichoderma reesei is commonly used in industry-scale production of secretory proteins. Since almost all secreted proteins are O-glycosylated, modulation of the activity of enzymes of the O-glycosylation pathway are likely to affect protein production and secretion or change the glycosylation pattern of the secreted proteins, altering their stability and biological activity. Understanding how the activation of different components of the O-glycosylation pathway influences the glycosylation pattern of proteins and their production and secretion could help in elucidating the mechanism of the regulation of these processes and should facilitate creation of engineered microorganisms producing high amounts of useful proteins. In this review we focus on data concerning Trichoderma, but also present some background information allowing comparison with other fungal species.

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

100%

Indyk K., Olczak T., Ciuraszkiewicz J., Wątorek W., Olczak M.

2007

vol. 54

issue 3

567-573

Azurocidin is an inactive serine protease homolog with primary sequence similarity to neutrophil elastase, cathepsin G, and proteinase 3. The aim of this study was to investigate possible consequences of differential glycosylation of azurocidin in regard to its secretion, protein stability as measured by susceptibility to proteolysis, and antibacterial activity. Site-directed mutagenesis was employed to generate mutant azurocidin variants lacking individual N-glycosylation sites. Our results show that N-linked glycans may play a role in proper azurocidin folding and subsequent secretion by insect cells. We also demonstrate that N-linked glycosylation contributes to azurocidin stability by protecting it from proteolysis. The lack of N-glycosylation at individual sites does not significantly influence the azurocidin antibacterial activity.

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation.

88%

Perlińska-Lenart U., Kurzątkowski W., Janas P., Kopińska A., Palamarczyk G., Kruszewska J. S.

2005

vol. 52

issue 1

195-205

O-glycosylation has been considered a limiting factor in protein secretion in filamentous fungi. Overexpression of the yeast DPM1 gene encoding dolichylphosphate mannose synthase (DPMS) in an Aspergillus nidulans mutant (BWB26A) deficient in O-glycosylation caused an increase in the number of secretory vesicles and changes in protein secretion. However, the secretory proteins, primarily O-mannosylated glucoamylase and N-glycosylated invertase, were mainly trapped in the periplasmic space. Different glycoforms of invertase were found insite the cells, in the periplasmic space and in the cultivation medium. Our data point to the importance of the cell wall as a barrier in protein secretion.

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3 Acta Biochimica Polonica

1 2008

1 2007

1 2005

2 Kruszewska J. S.

2 Palamarczyk G.

2 Perlińska-Lenart U.

1 Ciuraszkiewicz J.

1 Górka-Nieć W.

1 Indyk K.

1 Janas P.

1 Kopińska A.

1 Kurzątkowski W.

1 Olczak M.

1 Olczak T.

1 Orłowski J.

1 Wątorek W.

1 Zembek P.

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Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi

Analysis of individual azurocidin N-glycosylation sites in regard to its secretion by insect cells, susceptibility to proteolysis and antibacterial activity

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation.