Investigation of the potential regulator proteins associated with the expression of major surface protein and dentilisin in Treponema denticola

References

• Kinane DF, Stathopoulou PG, Papapanou PN. Periodontal diseases. Nat Rev Dis Primers. 2017;3:17038.
   PubMed Web of Science ®Google Scholar
• Lamont RJ, Koo H, Hajishengallis G. The oral microbiota: dynamic communities and host interactions. Nat Rev Microbiol. 2018;16(12):745–9.
   PubMed Web of Science ®Google Scholar
• Griffen AL, Beall CJ, Campbell JH, et al. Distinct and complex bacterial profiles in human periodontitis and health revealed by 16S pyrosequencing. Isme J. 2012;6(6):1176–1185.
   PubMed Web of Science ®Google Scholar
• Socransky SS, Haffajee AD, Cugini MA, et al. Microbial complexes in subgingival plaque. J Clin Periodontol. 1998;25(2):134–144.
   PubMed Web of Science ®Google Scholar
• Ellen RP, Galimanas VB. Spirochetes at the forefront of periodontal infections. Periodontol. 2005;38:13–32.
   Google Scholar
• Cogulu D, Oncag O, Kutukculer N, et al. The correlation between serum immunoglobulin A and immunoglobulin G levels and the presence of Treponema denticola in human periapical lesions. J Endod. 2007;33(12):1413–1416.
   Web of Science ®Google Scholar
• Ishihara K, Nabuchi A, Ito R, et al. Correlation between detection rates of periodontopathic bacterial DNA in carotid coronary stenotic artery plaque and in dental plaque samples. J Clin Microbiol. 2004;42(3):1313–1315.
   Web of Science ®Google Scholar
• Ishihara K. Virulence factors of Treponema denticola. Periodontol. 2010;54(1):117–135.
   Google Scholar
• Fenno JC, Hannam PM, Leung WK, et al. Cytopathic effects of the major surface protein and the chymotrypsinlike protease of Treponema denticola. Infect Immun. 1998;66(5):1869–1877.
   PubMed Web of Science ®Google Scholar
• Umemoto T, Namikawa I, Suido H, et al. A major antigen on the outer envelope of a human oral spirochete, Treponema denticola. Infect Immun. 1989;57(8):2470–2474.
   Web of Science ®Google Scholar
• Haapasalo M, Muller KH, Uitto VJ, et al. Characterization, cloning, and binding properties of the major 53-kilodalton Treponema denticola surface antigen. Infect Immun. 1992;60(5):2058–2065.
   PubMed Web of Science ®Google Scholar
• Godovikova V, Goetting-Minesky MP, Timm JC, et al. Immunotopological analysis of the Treponema denticola major surface protein (Msp). J Bacteriol. 2019;201(2):e00528–18.
   Web of Science ®Google Scholar
• Fenno JC, Muller KH, McBride BC. Sequence analysis, expression, and binding activity of recombinant major outer sheath protein (Msp) of Treponema denticola. J Bacteriol. 1996;178(9):2489–2497.
   PubMed Web of Science ®Google Scholar
• Ishihara K, Miura T, Kuramitsu HK, et al. Characterization of the Treponema denticola prtP gene encoding a prolyl-phenylalanine-specific protease (dentilisin). Infect Immun. 1996;64(12):5178–5186.
   Web of Science ®Google Scholar
• Godovikova V, Wang HT, Goetting-Minesky MP, et al. Treponema denticola PrcB is required for expression and activity of the PrcA-PrtP (dentilisin) complex. J Bacteriol. 2010;192(13):3337–3344.
   Web of Science ®Google Scholar
• Bamford CV, Fenno JC, Jenkinson HF, et al. The chymotrypsin-like protease complex of Treponema denticola ATCC 35405 mediates fibrinogen adherence and degradation. Infect Immun. 2007;75(9):4364–4372.
   PubMed Web of Science ®Google Scholar
• Yamazaki T, Miyamoto M, Yamada S, et al. Surface protease of Treponema denticola hydrolyzes C3 and influences function of polymorphonuclear leukocytes. Microbes Infect. 2006;8(7):1758–1763.
   Web of Science ®Google Scholar
• Sano Y, Okamoto-Shibayama K, Tanaka K, et al. Dentilisin involvement in coaggregation between Treponema denticola and Tannerella forsythia. Anaerobe. 2014;30:45–50.
   Web of Science ®Google Scholar
• Inagaki S, Kimizuka R, Kokubu E, et al. Treponema denticola invasion into human gingival epithelial cells. Microb Pathog. 2016;94:104–111.
   Web of Science ®Google Scholar
• Ishihara K, Kuramitsu HK, Miura T, et al. Dentilisin activity affects the organization of the outer sheath of Treponema denticola. J Bacteriol. 1998;180(15):3837–3844.
   Web of Science ®Google Scholar
• Bian XL, Wang HT, Ning Y, et al. Mutagenesis of a novel gene in the prcA-prtP protease locus affects expression of Treponema denticola membrane complexes. Infect Immun. 2005;73(2):1252–1255.
   Web of Science ®Google Scholar
• Chan EC, Siboo R, Keng T, et al. Treponema denticola (ex Brumpt 1925) sp. nov., nom. rev., and identification of new spirochete isolates from periodontal pockets. Int J Syst Bacteriol. 1993;43(2):196–203.
   Google Scholar
• Ohta K, Makinen KK, Loesche WJ. Purification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates. Infect Immun. 1986;53(1):213–220.
   Web of Science ®Google Scholar
• Tanaka-Kumazawa K, Kikuchi Y, Sano-Kokubun Y, et al. Characterization of a potential ABC-type bacteriocin exporter protein from Treponema denticola. BMC Oral Health. 2016;17(1):18.
   Google Scholar
• Edgar R, Domrachev M, Lash AE. Gene Expression Omnibus: NCBI gene expression and hybridization array data repository. Nucleic Acids Res. 2002;30(1):207–210.
   PubMed Web of Science ®Google Scholar
• Rosen G, Naor R, Rahamim E, et al. Proteases of Treponema denticola outer sheath and extracellular vesicles. Infect Immun. 1995;63(10):3973–3979.
   Web of Science ®Google Scholar
• Veith PD, Glew MD, Gorasia DG, et al. Localization of outer membrane proteins in Treponema denticola by quantitative proteome analyses of outer membrane vesicles and cellular fractions. J Proteome Res. 2019;18(4):1567–1581.
   Web of Science ®Google Scholar
• Browning DF, Busby SJ. Local and global regulation of transcription initiation in bacteria. Nat Rev Microbiol. 2016;14(10):638–650.
   PubMed Web of Science ®Google Scholar
• Cuthbertson L, Nodwell JR. The TetR family of regulators. Microbiol Mol Biol Rev. 2013;77(3):440–475.
   PubMed Web of Science ®Google Scholar
• Galperin MY. Structural classification of bacterial response regulators: diversity of output domains and domain combinations. J Bacteriol. 2006;188(12):4169–4182.
   PubMed Web of Science ®Google Scholar
• Frederick JR, Sarkar J, McDowell JV, et al. Molecular signaling mechanisms of the periopathogen, Treponema denticola. J Dent Res. 2011;90(10):1155–1163.
   Web of Science ®Google Scholar
• Miller DP, Frederick JR, Sarkar J, et al. The Treponema denticola AtcR LytTR domain-containing response regulator interacts with three architecturally distinct promoter elements: implications for understanding the molecular signaling mechanisms that drive the progression of periodontal disease. Mol Oral Microbiol. 2014;29(5):219–232.
   PubMed Web of Science ®Google Scholar
• Sarkar J, Miller DP, Oliver LD Jr., et al. The Treponema denticola PAS domain-containing histidine kinase Hpk2 is a heme binding sensor of oxygen levels. J Bacteriol. 2018;200(18):e00116–00118.
   Web of Science ®Google Scholar
• Brett PJ, Burtnick MN, Fenno JC, et al. Treponema denticola TroR is a manganese- and iron-dependent transcriptional repressor. Mol Microbiol. 2008;70(2):396–409.
   Web of Science ®Google Scholar
• Saraithong P, Goetting-Minesky MP, Durbin PM, et al. Roles of TroA and TroR in metalloregulated growth and gene expression in Treponema denticola. J Bacteriol. 2020;202(7):e00770–00719.
   Web of Science ®Google Scholar
• McHardy I, Keegan C, Sim JH, et al. Transcriptional profiles of Treponema denticola in response to environmental conditions. PLoS One. 2010;5(10):e13655.
   Web of Science ®Google Scholar
• Ikegami A, Honma K, Sharma A, et al. Multiple functions of the leucine-rich repeat protein LrrA of Treponema denticola. Infect Immun. 2004;72(8):4619–4627.
   Web of Science ®Google Scholar
• Frederick JR, Rogers EA, Marconi RT. Analysis of a growth-phase-regulated two-component regulatory system in the periodontal pathogen Treponema denticola. J Bacteriol. 2008;190(18):6162–6169.
   Web of Science ®Google Scholar
• Strauch MA. Regulation of Bacillus subtilis gene expression during the transition from exponential growth to stationary phase. Prog Nucleic Acid Res Mol Biol. 1993;46:121–153.
   Google Scholar
• Strauch MA, Hoch JA. Transition-state regulators: sentinels of Bacillus subtilis post-exponential gene expression. Mol Microbiol. 1993;7(3):337–342.
   Web of Science ®Google Scholar
• Godovikova V, Goetting-Minesky MP, Fenno JC. Composition and localization of Treponema denticola outer membrane complexes. Infect Immun. 2011;79(12):4868–4875.
   Web of Science ®Google Scholar
• Yurimoto H, Hirai R, Matsuno N, et al. HxlR, a member of the DUF24 protein family, is a DNA-binding protein that acts as a positive regulator of the formaldehyde-inducible hxlAB operon in Bacillus subtilis. Mol Microbiol. 2005;57(2):511–519.
   Web of Science ®Google Scholar
• McClure JM, Wierman MB, Maqani N, et al. Isonicotinamide enhances Sir2 protein-mediated silencing and longevity in yeast by raising intracellular NAD+ concentration. J Biol Chem. 2012;287(25):20957–20966.
   Web of Science ®Google Scholar