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Cloning, expression and purification of serprocidins in Pichia pastoris

100%

Indyk K., Wezyk P., Watorek W., Olczak M.

Acta Biochimica Polonica

2006

tom 53

nr Supplement 1

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

88%

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

Acta Biochimica Polonica

2007

tom 54

nr 3

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.

Ograniczanie wyników

2 Acta Biochimica Polonica

2 Indyk K.

2 Olczak M.

2 Watorek W.

1 Ciuraszkiewicz J.

1 Olczak T.

1 Wezyk P.

1 2007

1 2006

Wyniki wyszukiwania

Cloning, expression and purification of serprocidins in Pichia pastoris

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