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2007 | 54 | 3 | 567-573

Article title

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

Content

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EN

Abstracts

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.

Year

Volume

54

Issue

3

Pages

567-573

Physical description

Dates

published
2007
received
2007-02-24
revised
2007-06-21
accepted
2007-07-06
(unknown)
2007-07-26

Contributors

  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland
author
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland
  • Laboratory of Biochemistry, Faculty of Biotechnology, University of Wrocław, Wrocław, Poland

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv54p567kz
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