RgpB belongs to a group of cysteine endoproteases, the gingipains, that are unique to the periodontal pathogen Porphyromonas gingivalis. There are three members to the gingipain family: RgpA and RgpB hydrolyse Arg-Xaa and which Kgp cleaves Lys-Xaa peptide bonds. The cysteine proteinases of the gingipain family are responsible for 85% of the general proteolytic activity generated by this bacterium. The gingipains are potent virulence factors which are able to degrade a broad range of host proteins including extracellular matrix, plasma and immunological proteins. The gingipains are not only responsible for degradation of host proteins, but also possess the potential for the activation of some of them. RgpB have been shown to activate prothrombin to thrombin; prekallikrein – leading to the formation of bradykinin; PAR-1,-2 and -4 receptors located on various cell types including platelets, neutrophils and epithelial cells – leading to platelets aggregation, neutrophils activation, release of pro-inflammatory cytokies.
Arginine-specific protease Rgp from Porphyromonas gingivalis
Veillard F, Potempa B, Guo Y, Ksiazek M, Sztukowska MN, Houston JA, Koneru L, Nguyen KA, Potempa J. (2015) Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis. Biol. Chem. 396:377-384. PMID: 25720118
Growth medium of genetically modified P. gingivalis W83 carrying the rgpB gene with an insertion of the hexahistidine coding sequence in the front of the sequence encoding the C-terminal domain.
Aceton precipitation, DE-52 cellulose ion-exchange chromatography, Ni-Sepharose affinity chromatography
~ 48.5 kDa
50 μg or 100 μg
batch specific (≥80% estimated by SDS-PAGE)
20 mM Bis-Tris, 150 mM, NaCl 0.02% NaN3, pH 6.5
– 80°C. Avoid freeze/thaw cycles by aliquoting protein
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