Abstract
Quinol peroxidase (QPO) catalyzes peroxidase activity using a quinol on respiratory chain as a substrate. QPO was purified from the membrane fraction of Actinobacillus actinomycetemcomitans, a bacterial species associated with a variety of human infections, including localized aggressive periodontitis (LAP). The cytoplasmic membrane of A. actinomycetemcomitans exhibited QPO-dependent peroxidase activity in the presence of NADH or succinate, known physiological substrates of the respiratory chain. QPO is an approximately 50-kDa protein that contains three heme c molecules. Cloning and sequencing shows that QPO is encoded as a bacterial cytochrome c peroxidase (BCCP) with N-terminal extensions containing an additional potential heme c-binding motif. Despite the high sequence homology to BCCP, QPO does not catalyze peroxidation by cytochrome c. A qpo null mutant exhibits an oxidative stress phenotype, suggesting that QPO plays an important role in scavenging endogenously generated reactive oxygen species (ROS) such as hydrogen peroxide. In addition, the qpo null mutant exhibits reduced production of leukotoxin (LtxA), a secreted bacterial toxin that is known to target human leukocytes and erythrocytes. Screening identified ascofuranone as a highly potent inhibitor of QPO (K i = 9.6 nM). This inhibitor also induced a dose-dependent decrease in the secretion of LtxA, with an associated reduction in the pathogenicity of A. actinomycetemcomitans for HL-60 cells. Thus, inhibitors of QPO are promising candidates as drugs for the treatment and prevention of LAP.
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Konishi, K. (2014). Physiological Roles of a Periodontopathic Bacterial Membrane-Bound Quinol Peroxidase. In: Ekuni, D., Battino, M., Tomofuji, T., Putnins, E. (eds) Studies on Periodontal Disease. Oxidative Stress in Applied Basic Research and Clinical Practice. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4614-9557-4_8
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DOI: https://doi.org/10.1007/978-1-4614-9557-4_8
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