Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis

References

Chen, Z.X., Potempa, J., Polanowski, A., Renvert, S., Wikstrom, M., and Travis, J. (1991). Stimulation of proteinase and amidase activities in Porphyromonas (Bacteroides) gingivalis by amino acids and dipeptides. Infect. Immun. 59, 2846–2850.10.1128/iai.59.8.2846-2850.1991Search in Google Scholar PubMed PubMed Central

Chiu, J., March, P.E., Lee, R., and Tillett, D. (2004). Site-directed, ligase-independent mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h. Nucleic Acids Res. 32, e174.10.1093/nar/gnh172Search in Google Scholar PubMed PubMed Central

de Diego, I., Veillard, F.T., Guevara, T., Potempa, B., Sztukowska, M., Potempa, J., and Gomis-Ruth, F.X. (2013). Porphyromonas gingivalis virulence factor gingipain RgpB shows a unique zymogenic mechanism for cysteine peptidases. J. Biol. Chem. 288, 14287–14296.10.1074/jbc.M112.444927Search in Google Scholar PubMed PubMed Central

Eichinger, A., Beisel, H.G., Jacob, U., Huber, R., Medrano, F.J., Banbula, A., Potempa, J., Travis, J., and Bode, W. (1999). Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with a caspase-like fold. EMBO J. 18, 5453–5462.10.1093/emboj/18.20.5453Search in Google Scholar PubMed PubMed Central

Glew, M.D., Veith, P.D., Peng, B., Chen, Y.Y., Gorasia, D.G., Yang, Q., Slakeski, N., Chen, D., Moore, C., Crawford, S., et al. (2012). PG0026 is the C-terminal signal peptidase of a novel secretion system of Porphyromonas gingivalis. J. Biol. Chem. 287, 24605–24617.10.1074/jbc.M112.369223Search in Google Scholar PubMed PubMed Central

Godat, E., Herve-Grvepinet, V., Veillard, F., Lecaille, F., Belghazi, M., Bromme, D., and Lalmanach, G. (2008). Regulation of cathepsin K activity by hydrogen peroxide. Biol. Chem. 389, 1123–1126.10.1515/BC.2008.109Search in Google Scholar PubMed

Guo, Y., Nguyen, K.A., and Potempa, J. (2010). Dichotomy of gingipains action as virulence factors: from cleaving substrates with the precision of a surgeon’s knife to a meat chopper-like brutal degradation of proteins. Periodontol. 54, 15–44.10.1111/j.1600-0757.2010.00377.xSearch in Google Scholar PubMed PubMed Central

Imamura, T. (2003). The role of gingipains in the pathogenesis of periodontal disease. J. Periodontol. 74, 111–118.10.1902/jop.2003.74.1.111Search in Google Scholar PubMed

Mikolajczyk, J., Boatright, K.M., Stennicke, H.R., Nazif, T., Potempa, J., Bogyo, M., and Salvesen, G.S. (2003). Sequential autolytic processing activates the zymogen of Arg-gingipain. J. Biol. Chem. 278, 10458–10464.10.1074/jbc.M210564200Search in Google Scholar PubMed

Nguyen, K.A., Travis, J., and Potempa, J. (2007). Does the importance of the C-terminal residues in the maturation of RgpB from Porphyromonas gingivalis reveal a novel mechanism for protein export in a subgroup of Gram-negative bacteria? J. Bacteriol. 189, 833–843.10.1128/JB.01530-06Search in Google Scholar PubMed PubMed Central

O’Brien-Simpson, N.M., Pathirana, R.D., Walker, G.D., and Reynolds, E.C. (2009). Porphyromonas gingivalis RgpA-Kgp proteinase-adhesin complexes penetrate gingival tissue and induce proinflammatory cytokines or apoptosis in a concentration-dependent manner. Infect. Immun. 77, 1246–1261.10.1128/IAI.01038-08Search in Google Scholar PubMed PubMed Central

Paramonov, N., Rangarajan, M., Hashim, A., Gallagher, A., Aduse-Opoku, J., Slaney, J.M., Hounsell, E., and Curtis, M.A. (2005). Structural analysis of a novel anionic polysaccharide from Porphyromonas gingivalis strain W50 related to Arg-gingipain glycans. Mol. Microbiol. 58, 847–863.10.1111/j.1365-2958.2005.04871.xSearch in Google Scholar PubMed

Potempa, J. and Nguyen, K.A. (2007). Purification and characterization of gingipains. Curr. Protoc. Protein. Sci. 21, Unit 21.20.10.1002/0471140864.ps2120s49Search in Google Scholar PubMed

Potempa, J., Pike, R., and Travis, J. (1997). Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes. Biol. Chem. 378, 223–230.10.1515/bchm.1997.378.3-4.223Search in Google Scholar PubMed

Potempa, J., Mikolajczyk-Pawlinska, J., Brassell, D., Nelson, D., Thogersen, I.B., Enghild, J.J., and Travis, J. (1998). Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis. J. Biol. Chem. 273, 21648–21657.10.1074/jbc.273.34.21648Search in Google Scholar PubMed

Sato, K., Kido, N., Murakami, Y., Hoover, C.I., Nakayama, K., and Yoshimura, F. (2009). Lipopolysaccharide biosynthesis-related genes are required for colony pigmentation of Porphyromonas gingivalis. Microbiology 155, 1282–1293.10.1099/mic.0.025163-0Search in Google Scholar PubMed

Shoji, M., Sato, K., Yukitake, H., Kondo, Y., Narita, Y., Kadowaki, T., Naito, M., and Nakayama, K. (2011). Por secretion system-dependent secretion and glycosylation of Porphyromonas gingivalis hemin-binding protein 35. PLoS One 6, e21372.10.1371/journal.pone.0021372Search in Google Scholar PubMed PubMed Central

Shoji, M., Sato, K., Yukitake, H., Naito, M., and Nakayama, K. (2014). Involvement of the Wbp pathway in the biosynthesis of Porphyromonas gingivalis lipopolysaccharide with anionic polysaccharide. Sci. Rep. 4, 5056.10.1038/srep05056Search in Google Scholar PubMed PubMed Central

Sztukowska, M., Veillard, F., Potempa, B., Bogyo, M., Enghild, J.J., Thogersen, I.B., Nguyen, K.A., and Potempa, J. (2012). Disruption of gingipain oligomerization into non-covalent cell-surface attached complexes. Biol. Chem. 393, 971–977.10.1515/hsz-2012-0175Search in Google Scholar PubMed PubMed Central

Veillard, F., Potempa, B., Poreba, M., Drag, M., and Potempa, J. (2012). Gingipain aminopeptidase activities in Porphyromonas gingivalis. Biol. Chem. 393, 1471–1476.10.1515/hsz-2012-0222Search in Google Scholar PubMed PubMed Central

Veillard, F., Sztukowska, M., Mizgalska, D., Ksiazek, M., Houston, J., Potempa, B., Enghild, J.J., Thogersen, I.B., Gomis-Ruth, F.X., Nguyen, K.A., et al. (2013). Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases. Biochim. Biophys. Acta 1830, 4218–4228.10.1016/j.bbagen.2013.04.005Search in Google Scholar PubMed PubMed Central

Veith, P.D., Nor Muhammad, N.A., Dashper, S.G., Likic, V.A., Gorasia, D.G., Chen, D., Byrne, S.J., Catmull, D.V., and Reynolds, E.C. (2013). Protein substrates of a novel secretion system are numerous in the Bacteroidetes phylum and have in common a cleavable C-terminal secretion signal, extensive post-translational modification, and cell-surface attachment. J. Proteome Res. 12, 4449–4461.10.1021/pr400487bSearch in Google Scholar PubMed

Veith, P.D., Chen, Y.Y., Gorasia, D.G., Chen, D., Glew, M.D., O’Brien-Simpson, N.M., Cecil, J.D., Holden, J.A., and Reynolds, E.C. (2014). Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors. J. Proteome Res. 13, 2420–2432.10.1021/pr401227eSearch in Google Scholar PubMed

Zhou, X.Y., Gao, J.L., Hunter, N., Potempa, J., and Nguyen, K.A. (2013). Sequence-independent processing site of the C-terminal domain (CTD) influences maturation of the RgpB protease from Porphyromonas gingivalis. Mol. Microbiol. 89, 903–917.10.1111/mmi.12319Search in Google Scholar PubMed PubMed Central