ABSTRACT
The aims of this study were to assess the diagnostic accuracy of swept-source optical coherence tomography (SS-OCT) for detection of caries beneath composite restorations and to compare the results with those obtained by radiography. Flat dentin surfaces with and without natural caries were bonded with 1- or 2-mm thick composite restorations. SS-OCT scanning was performed over the composite restorations to construct three-dimensional (3D) images of the resin-dentin interface. Images were chosen from the 3D constructions to detect caries beneath the restorations. The sensitivity, specificity, false positive and negative predictive values for caries detection, and Az values from receiver-operating characteristic analysis were calculated and compared with those of digital dental radiography at a significance level of α=0.05. Intraexaminer and interexaminer reproducibility was compared between SSOCT and radiography. SS-OCT could detect caries, which appeared as a bright zone beneath composite up to 2-mm thick. SS-OCT provided greater diagnostic accuracy than radiography.
Subject(s)
Dental Caries/diagnostic imaging , Imaging, Three-Dimensional/methods , Tomography, Optical Coherence/methods , Composite Resins/therapeutic use , Dental Caries/therapy , Dental Restoration, Permanent/methods , Humans , In Vitro Techniques , Molar , Predictive Value of Tests , Radiography, Dental, Digital , Sensitivity and Specificity , Surface PropertiesABSTRACT
The oxidation of guanine (G) to 7,8-dihydro-8-oxoguanine (GO) forms one of the major DNA lesions generated by reactive oxygen species (ROS). The GO can be corrected by GO DNA glycosylases (Ogg), enzymes involved in base excision repair (BER). Unrepaired GO induces mismatched base pairing with adenine (A); as a result, the mismatch causes a point mutation, from G paired with cytosine (C) to thymine (T) paired with adenine (A), during DNA replication. Here, we report the characterization of a putative Ogg from the thermoacidophilic archaeon Thermoplasma volcanium. The 204-amino acid sequence of the putative Ogg (TVG_RS00315) shares significant sequence homology with the DNA glycosylases of Methanocaldococcus jannaschii (MjaOgg) and Sulfolobus solfataricus (SsoOgg). The six histidine-tagged recombinant TVG_RS00315 protein gene was expressed in Escherichia coli and purified. The Ogg protein is thermostable, with optimal activity near a pH of 7.5 and a temperature of 60°C. The enzyme displays DNA glycosylase, and apurinic/apyrimidinic (AP) lyase activities on GO/N (where N is A, T, G, or C) mismatch; yet it cannot eliminate U from U/G or T from T/G, as mismatch glycosylase (MIG) can. These results indicate that TvoOgg-encoding TVG_RS00315 is a member of the Ogg2 family of T. volcanium.
