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2007 | 54 | 3 |

Tytuł artykułu

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

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
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.

Wydawca

-

Rocznik

Tom

54

Numer

3

Opis fizyczny

p.567-573,fig.,ref.

Twórcy

autor
  • University of Wroclaw, Tamka 2, 50-137 Wroclaw, Poland
autor
autor
autor

Bibliografia

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Typ dokumentu

Bibliografia

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