Productive Folding of Human Neutrophil α-Defensins in Vitro without the Pro-peptide

摘要: Human neutrophil α-defensins (HNPs) are small, Cys-rich, cationic antimicrobial proteins. Stored in the azurophilic granules of neutrophils, they released during phagocytosis to kill ingested foreign microbes through disruption their cytoplasmic membrane. Recently, three most abundant forms human α-defensins, HNPs 1−3, have been implicated suppressing HIV-1 infection vivo, thereby exhibiting a potential therapeutic value treatment AIDS. synthesized as inactive precursors vivo and require proteolytic removal inhibitory N-terminal pro-peptide for activation. Folding 1−3 vitro without has reported be extremely difficult, which led hypothesis that 45-residue anionic may assist proHNPs folding an intramolecular chaperone interacting with C-terminal domain, mechanism reminiscent some bacterial serine proteases. Here we show pro-region can fold productively ...