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Licensed Unlicensed Requires Authentication Published by De Gruyter July 16, 2015

Inactivation of human kininogen-derived antimicrobial peptides by secreted aspartic proteases produced by the pathogenic yeast Candida albicans

  • Oliwia Bochenska , Maria Rapala-Kozik , Natalia Wolak , Wojciech Kamysz , Daria Grzywacz , Wataru Aoki , Mitsuyoshi Ueda and Andrzej Kozik EMAIL logo
From the journal Biological Chemistry

Abstract

Ten secreted aspartic proteases (Saps) of Candida albicans cleave numerous peptides and proteins in the host organism and deregulate its homeostasis. Human kininogens contain two internal antimicrobial peptide sequences, designated NAT26 and HKH20. In our current study, we characterized a Sap-catalyzed cleavage of kininogen-derived antimicrobial peptides that results in the loss of the anticandidal activity of these peptides. The NAT26 peptide was effectively inactivated by all Saps, except Sap10, whereas HKH20 was completely degraded only by Sap9. Proteolytic deactivation of the antifungal potential of human kininogens can help the pathogens to modulate or evade the innate immunity of the host.


Corresponding author: Andrzej Kozik, Faculty of Biochemistry, Biophysics and Biotechnology, Department of Analytical Biochemistry, Jagiellonian University in Krakow, Gronostajowa 7, 30-387 Krakow, Poland, e-mail:

Acknowledgments

This work was supported in part by the National Science Centre, Poland (grant no. 2013/09/N/NZ1/00201, awarded to O.B.). The Faculty of Biochemistry, Biophysics and Biotechnology of the Jagiellonian University in Krakow is a beneficiary of structural funds from the European Union (grant no. POIG.02.01.00-12-064/08 – “Molecular biotechnology for health”) and a partner of the Leading National Research Center (KNOW) supported by the Ministry of Science and Higher Education, Poland.

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Received: 2015-4-27
Accepted: 2015-7-8
Published Online: 2015-7-16
Published in Print: 2015-12-1

©2015 by De Gruyter

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