Inactivation of human kininogen-derived antimicrobial peptides by secreted aspartic proteases produced by the pathogenic yeast Candida albicans.
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.
Oliwia
O
Bochenska
Maria
M
Rapala-Kozik
Natalia
N
Wolak
Wojciech
W
Kamysz
Daria
D
Grzywacz
Wataru
W
Aoki
Mitsuyoshi
M
Ueda
Andrzej
A
Kozik
D000595:Amino Acid Sequence; D023181:Antimicrobial Cationic Peptides / Q000037:antagonists & inhibitors*; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism / Q000494:pharmacology*; D002176:Candida albicans / Q000201:enzymology*; D002853:Chromatography, Liquid; D054884:Host-Pathogen Interactions; D006801:Humans; D007704:Kininogens / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data
D023181:Antimicrobial Cationic Peptides; D007704:Kininogens; D016282:Aspartic Acid Endopeptidases