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alpha chains of haptoglobin + H2O
?
alpha-globin + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because alpha-globin is not soluble at neutral pH
-
?
alpha-thrombin + H2O
beta-thrombin B-1 and B-2 chains
-
HRgpA and RgpB, cleavage of peptide bond R383-N394
-
?
alpha1-Antichymotrypsin + H2O
?
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
benzoyl-Arg 4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
benzoyl-Arg-4-nitroanilide + H2O
benzoyl-Arg + 4-nitroaniline
-
-
-
-
?
Benzoyl-Ile-Glu-(gamma-ornithyl)-Gly-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
benzoyl-Phe-Val-Arg-4-nitroanilide + H2O
benzoyl-Phe-Val-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Pro-Phe-Arg-4-nitroanilide + H2O
benzoyl-Pro-Phe-Arg + 4-nitroaniline
-
-
-
?
benzoyl-Val-Gly-Arg-4-nitroanilide + H2O
benzoyl-Val-Gly-Arg + 4-nitroaniline
-
-
-
?
beta-globin + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds, in presence of 4 M urea, because beta-globin is not soluble at neutral pH
-
?
beta-thrombin B-2 chain + H2O
?
-
HRgpA and RgpB, substrate inactivation and degradation
-
?
butoxy-carbonyl-O-benzyl-Ser-Gly-Arg-4-nitroanilide + H2O
butoxy-carbonyl-O-benzyl-Ser-Gly-Arg + 4-nitroaniline
-
best sythetic substrate
-
?
butoxy-carbonyl-Val-Leu-Gly-Arg-4-nitroanilide + H2O
butoxy-carbonyl-Val-Leu-Gly-Arg + 4-nitroaniline
-
-
-
?
Bz-L-Arg-4-nitroanilide + H2O
Bz-L-Arg + 4-nitroaniline
-
-
-
-
?
C3 protein + H2O
?
-
-
-
-
?
C4 protein + H2O
?
-
-
-
-
?
C5 protein + H2O
?
-
at higher enzyme concentrations
-
-
?
CBZ-Phe-Arg-4-methyl-coumaryl-7-amide + H2O
CBZ-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
CD27 protein + H2O
?
-
involved in reduction of T-cell function, effective even in the presence of 2.5 or 5% serum
-
-
?
cell adhesion molecule + H2O
?
-
involved in the detachment of endothelial cells
-
-
?
D-Ile-Pro-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
D-Phe-Pip-Arg 4-nitroanilide + H2O
?
-
-
-
-
?
denatured alpha1-proteinase inhibitor + H2O
?
-
-
?
denatured type I collagen + H2O
?
factor IX proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
factor X proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
fibrinogen A alpha-chain + H2O
28 kDa fragment + ?
-
major cleavage site at position 22, all isoforms
the 28 kDa fragment is the major product of isoform HRgpA
?
fibrinogen B beta-chain + H2O
?
-
high activity of isoform HRgpA, which performs cleavage at 2 positions: 42 and 44
-
?
Fibronectin + H2O
?
-
the enzyme isoforms HRgpA and RgpB effectively destroy the cell-binding domain of fibronectin
-
-
?
Glycophorin A + H2O
?
-
-
-
-
?
haemoglobin + H2O
?
-
complete digestion, enzyme form RGP-B shows high activity, not RGP-A, human substrate
-
?
haptoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
Hemoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
hemin + ?
human beta-defensin 3 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
human protease-activated receptor PAR-2 + H2O
?
Insulin B-chain + H2O
?
-
specific cleavage of Arg-+-
-
-
?
integrin subunit alpha2 + H2O
?
integrin subunit beta1 + H2O
?
integrin subunit beta3 + H2O
?
interleukin-1beta + H2O
?
Leu-Tyr-Arg-4-nitroanilide + H2O
Leu-Tyr-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Lysozyme + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
Mellitin + H2O
?
-
specific cleavage of Arg-+-
-
-
?
MeoSuc-Ala-Ala-Pro-Val-4-nitroanilide + H2O
?
-
-
-
?
N-alpha-benzoyl-D,L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-Arg-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Arg + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine 4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
N-alpha-benzoyl-DL-Lys-4-nitroanilide + H2O
N-alpha-benzoyl-DL-Lys + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-L-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
N-benzoyl-L-arginine-4-nitroanilide + H2O
N-benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
N-cadherin + H2O
?
-
in BCAEC cells, cleavage by HRgpA but not RgpB
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
Nalpha-benzoyl-D,L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-D,L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-D,L-arginine 4 nitroanilide + H2O
Nalpha-benzoyl-D,L-arginine + 4 nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-Arg-4-nitroanilide + H2O
Nalpha-benzoyl-L-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
oxyhaemoglobin + H2O
?
-
-
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
oxyhaemoglobin + H2O
methaemoglobin + ?
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
profibronectin + H2O
fibronectin + ?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
protein C + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
alpha-thrombin + 2 peptide fragments
-
major cleavage sites of HRgpA are R271-T272, R320-I321, and R155-S156, activation of human substrate, HRgpA possesses adhesion domains and is about 20fold more active than the single chain RgpB
high amount od alpha-thrombin
?
prothrombin + H2O
alpha-thrombin + prethrombin 1 + prethrombin 2 + 1 peptide fragments
-
major cleavage sites of RgpB are R155-S156 and R271-T272, while the peptide bond R320-I321 is not efficiently cleaved resulting in about 20fold slower reaction, activation of human substrate, less active than HRgpA
low amount of alpha-thrombin
?
prothrombin + H2O
thrombin + ?
-
HRgpA, involved in fibrinogen clotting
-
?
RgpA-HagA polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
ribonuclease A + H2O
?
-
absolutely specific cleavage of all Arg-Xaa peptides bonds
-
?
secretory leucocyte protease inhibitor + H2O
?
t-butyloxycarbonyl-L-leucylglycyl-L-arginine-4-metylcoumaryl-7-amide + H2O
?
-
-
-
-
?
thrombomodulin + H2O
?
-
Lys-gingipain and Arg-gingipain cleave thrombomodulin in vitro
-
-
?
toluenesulfonyl-glycyl-L-prolyl-L-arginine-4-nitroanilide + H2O
toluenesulfonyl-glycyl-L-prolyl-L-arginine + 4-nitroaniline
-
-
-
?
tosyl-Gly-L-Pro-L-Arg 4-nitroanilide + H2O
tosyl-Gly-L-Pro-L-Arg 4-nitroaniline
-
-
-
-
?
tosyl-GPR-4-nitroanilide + H2O
tosyl-GPR + 4-nitroaniline
other substrates with a Ps proline are very poor substrates, synthetic fluorogenic substrate
-
?
transferrin + H2O
?
-
degradation of host protein substrate
-
-
?
transferrin + H2O
hemin + ?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
VE-cadherin + H2O
?
-
in BCAEC cells, especially HRgpA
-
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
Z-Arg-Arg-4-nitroanilide + H2O
Z-Arg-Arg + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
additional information
?
-
alpha chains of haptoglobin + H2O
?
-
low activity, hemoglobin protects
-
?
alpha chains of haptoglobin + H2O
?
-
low activity, hemoglobin protects
-
?
alpha1-Antichymotrypsin + H2O
?
inactivation of the substrate
-
?
alpha1-Antichymotrypsin + H2O
?
inactivation of the substrate
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
-
-
-
-
?
AWTPTPTPLSTPSIIRTTGLRPYPSSVLI + H2O
AWTPTPTPLSTPSIIR + TTGLRPYPSSVLI
-
-
-
-
?
azocasein + H2O
?
-
-
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
azocasein + H2O
?
synthetic chromogenic substrate
-
?
Azocoll + H2O
?
-
-
-
-
?
Azocoll + H2O
?
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
benzoyl-L-arginine-4-nitroanilide + H2O
benzoyl-L-arginine + 4-nitroaniline
synthetic fluorogenic substrate
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
CXCL8 + H2O
?
-
-
-
-
?
denatured type I collagen + H2O
?
-
-
?
denatured type I collagen + H2O
?
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells) with RgpB being far more efficient than other gingipains. RgpB efficiently inactivates the inhibitory activity of elafin at subnanomolar concentrations through proteolysis limited to the Arg22-Cys23 peptide bond within the surface loop harboring the inhibitor active site
-
-
?
Gelatin + H2O
?
-
purified isozymes
-
?
Gelatin + H2O
?
-
purified isozymes
-
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 47 kDa, products of 23 kDa and 40 kDa in serum
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 47 kDa, products of 23 kDa and 40 kDa in serum
?
histatin 5 + H2O
?
-
-
-
-
?
histatin 5 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-2 + H2O
?
-
-
-
-
?
integrin subunit alpha2 + H2O
?
-
-
-
?
integrin subunit alpha2 + H2O
?
-
-
-
?
integrin subunit beta1 + H2O
?
-
-
-
?
integrin subunit beta1 + H2O
?
-
-
-
?
integrin subunit beta3 + H2O
?
-
-
-
?
integrin subunit beta3 + H2O
?
-
-
-
?
interferon gamma + H2O
?
-
degradation
-
-
?
interferon gamma + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin 12 + H2O
?
-
degradation
-
-
?
interleukin 12 + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin-1beta + H2O
?
-
low activity
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain, EC 3.4.22.47
-
-
?
interleukin-6 + H2O
?
-
-
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
-
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
Muc2 + H2O
?
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
-
?
N-alpha-benzoyl-DL-arginine-4-nitroanilide + H2O
N-alpha-benzoyl-DL-arginine + 4-nitroaniline
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
N-p-tosyl-Gly-Pro-Arg-4-nitroanilide + H2O
N-p-tosyl-Gly-Pro-Arg + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
Nalpha-benzoyl-L-arginine 4-nitroanilide + H2O
Nalpha-benzoyl-L-arginine + 4-nitroaniline
-
-
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin + ?
-
data indicate direct product formation without the occurrence of intermediates
-
-
?
oxyhaemoglobin + H2O
methaemoglobin + ?
-
data indicate direct product formation without the occurrence of intermediates
-
-
?
profibronectin + H2O
fibronectin + ?
-
-
-
?
profibronectin + H2O
fibronectin + ?
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp, Porphyromonas gingivalis-induced platelet aggregation in platelet-rich plasma depends on processed Hgp44 adhesin but not directly on Rgp proteinase, the adhesin is also processed by Lys-gingipain Kgp, EC 3.4.22.47
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
reduction of the protective effect of SLPIon neutrophil proteases and bacterial proinflammatory compounds
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
recombinant protein, reaction catalyzed by RgpA and RgpB
-
-
?
TNFalpha + H2O
?
-
degradation
-
-
?
TNFalpha + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
TNFalpha + H2O
?
-
inactivation by degradation of human TNFalpha on host cell surface and recombinant fibroblast cell surface, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
TNFalpha + H2O
?
-
degradation, high activity with HRgpA, moderate activity with RgpB
-
-
?
transferrin + H2O
hemin + ?
-
-
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
transferrin + H2O
hemin + ?
-
-
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Arg-7-amido-4-methylcoumarin + H2O
Z-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
Z-Phe-Arg-7-amido-4-methylcoumarin + H2O
Z-Phe-Arg + 7-amino-4-methylcoumarin
-
-
-
?
additional information
?
-
-
hydrolysis of synthetic chromogenic substrates with arginine in the P1 position
-
-
?
additional information
?
-
-
no activity of both enzyme forms with toluenesulfonyl-glycyl-L-prolyl-L-lysine-4-nitroanilide, Val-Leu-Lys-4-nitroanilide, benzoyl-Lys-4-nitroanilide, succinyl-Ala-Ala-Pro-Phe-4-nitroanilide, glutaryl-Phe-4-nitroanilide, benzoyl-Tyr-4-nitroanilide, and Lys-4-nitroanilide, activity with chromogenic synthetic substrates is limited to those with arginine in the P1-position
-
?
additional information
?
-
-
substrate specificity for the C-terminal position next to the cleavage site of the different enzyme forms, overview
-
?
additional information
?
-
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
-
the enzyme makes a significant contribution to the virulence of Porphyromonas gingivalis
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors
-
-
?
additional information
?
-
-
gingipains R mediate coaggregation of Porphyromonas gingivalis with other bacteria, overview
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases cleaving a broad range of in-host proteins
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme is specific for peptide substrate with Arg at P1 position, gingipain R performs autoprocessing and activation
-
-
?
additional information
?
-
-
implicated in a wide range of both pathological and physiological processes of Porphyromonas gingivalis, including destruction of periodontal tissue, disruption of host defense mechanisms, processing of bacterial cell surface and secretory proteins, and acquisition of heme and amino acids, involved in atherosclerotic processes
-
-
?
additional information
?
-
-
important for the provision of nutrients for the bacterium in the host organism, destruction of host tissue, modulation of host immune response
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, activation of the C1 complex in serum, degradation of multiple complement components, important factor for the resistance to the bacteriolytic activity of serum
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, involved in the perturbation of host defense and the destruction and invasion of host tissues, degradation of hosts proteins such as ICAM-1m VCAM-1, catenins, and cadherins, involved in the shedding of syndecan-1
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, probably involved in the reduction of T-cell function at periodontal lesion sites, induction of PAR-1 and PAR-2 receptor expression, up-regulation of PAR-4 expression, little effect on PAR-3 expression, increases expression of CD69 and CD25 on T-cells
-
-
?
additional information
?
-
-
involved in the deregulation of the hosts inflammatory response
-
-
?
additional information
?
-
-
involved in the induction of apoptosis in caspase dependent and caspase independent pathway
-
-
?
additional information
?
-
-
involved in the regulation of mRNA expression for the receptor activator of NF-kappaB ligand (RANKL) protein
-
-
?
additional information
?
-
-
no degradation of ICAM-3
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
-
-
?
additional information
?
-
-
gingipains are involved in bacterial adherence to host cells, RgpA binds to adhesin via its adhesin binding domain. Peptide A44 derived from the adhesin domain of RgpA plays a role in binding of Porphyromonas gingivalis to HEP-2 epithelial cells via cell surface receptors, e.g. clathrin, nocodazole and paclitaxel, which disrupt microtubule formation, block the interaction, while genistein does not
-
-
?
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
RgpA and RgpB cleave proteins after arginine residues
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases cleaving a broad range of in-host proteins
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
role of the Sn binding pocket, molecular basis for substrate specificity, overview
-
-
?
additional information
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
additional information
?
-
substrate specificity, no inactivation of native alpha1-proteinase inhibitor and native type I collagen
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
apoB-100 protein + H2O
?
-
apoB-100 degradation induces LDL-modification and contributes to the onset of atherosclerosis
-
-
?
C3 protein + H2O
?
-
-
-
-
?
C4 protein + H2O
?
-
-
-
-
?
C5 protein + H2O
?
-
at higher enzyme concentrations
-
-
?
CD27 protein + H2O
?
-
involved in reduction of T-cell function, effective even in the presence of 2.5 or 5% serum
-
-
?
cell adhesion molecule + H2O
?
-
involved in the detachment of endothelial cells
-
-
?
factor IX proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
factor X proenzyme + H2O
?
-
activation through limited proteolysis
-
-
?
Fibronectin + H2O
?
-
the enzyme isoforms HRgpA and RgpB effectively destroy the cell-binding domain of fibronectin
-
-
?
Glycophorin A + H2O
?
-
-
-
-
?
haptoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
Hemoglobin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
?
-
degradation of host protein substrate
-
-
?
hemopexin + H2O
hemin + ?
human protease-activated receptor PAR-1 + H2O
?
human protease-activated receptor PAR-2 + H2O
?
-
PAR-2 activation on epithelial cells
-
-
?
integrin subunit alpha2 + H2O
?
integrin subunit beta1 + H2O
?
integrin subunit beta3 + H2O
?
interferon gamma + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin 12 + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
interleukin-1beta + H2O
?
-
biological inactivation and degradation, low activity, cytokine degradation is mainly the result of Lys-gingipain, EC 3.4.22.47
-
-
?
interleukin-6 + H2O
?
-
biological inactivation and degradation
-
-
?
interleukin-8 + H2O
?
-
biological inactivation and degradation
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
prefimbrillin + H2O
fimbrilline + ?
-
-
mature form of the protein
-
?
profibronectin + H2O
fibronectin + ?
protease-activated receptor-1 + H2O
?
-
specific substrate for Arg-gingipain
-
-
?
protein C + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
?
-
activation through limited proteolysis
-
-
?
prothrombin + H2O
thrombin + ?
-
HRgpA, involved in fibrinogen clotting
-
?
RgpA-HagA polyprotein + H2O
?
-
processing of the precursor by Rgp
-
-
?
RgpA-Hgp polyprotein + H2O
?
-
processing of the precursor by Rgp, Porphyromonas gingivalis-induced platelet aggregation in platelet-rich plasma depends on processed Hgp44 adhesin but not directly on Rgp proteinase, the adhesin is also processed by Lys-gingipain Kgp, EC 3.4.22.47
-
-
?
secretory leucocyte protease inhibitor + H2O
?
-
reduction of the protective effect of SLPIon neutrophil proteases and bacterial proinflammatory compounds
-
-
?
transferrin + H2O
?
-
degradation of host protein substrate
-
-
?
transferrin + H2O
hemin + ?
transferring receptor + H2O
?
-
Rgp is responsible for transferring receptor degradation
-
-
?
additional information
?
-
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
Collagen type I + H2O
?
-
not the purified isoforms, enzyme probably needs to be attached to the cell surface
-
?
CXCL8 + H2O
?
-
-
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells)
-
-
?
elafin + H2O
?
all three gingipains have the ability to degrade elafin (endogenous inhibitor secreted by epithelial cells) with RgpB being far more efficient than other gingipains. RgpB efficiently inactivates the inhibitory activity of elafin at subnanomolar concentrations through proteolysis limited to the Arg22-Cys23 peptide bond within the surface loop harboring the inhibitor active site
-
-
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 40 kDa in serum
?
hemopexin + H2O
hemin + ?
-
-
products of 23 kDa and 40 kDa in serum
?
histatin 5 + H2O
?
-
-
-
-
?
histatin 5 + H2O
?
-
-
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
human protease-activated receptor PAR-1 + H2O
?
-
PAR-1 activation on epithelial cells
-
-
?
integrin subunit alpha2 + H2O
?
-
-
-
?
integrin subunit alpha2 + H2O
?
-
-
-
?
integrin subunit beta1 + H2O
?
-
-
-
?
integrin subunit beta1 + H2O
?
-
-
-
?
integrin subunit beta3 + H2O
?
-
-
-
?
integrin subunit beta3 + H2O
?
-
-
-
?
Muc2 + H2O
?
-
-
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
oxyhaemoglobin + H2O
methaemoglobin
-
data indicate direct product formation without the occurrence of intermediates, reaction required for the formation the the my-oxo heam dimer containing black pigment
-
-
?
profibronectin + H2O
fibronectin + ?
-
-
-
?
profibronectin + H2O
fibronectin + ?
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
protein + H2O
peptides
-
-
-
?
protein + H2O
peptides
-
-
?
TNFalpha + H2O
?
-
degradation leading to local cytokine paralysis impairing the inflammation-dependent host defense mechanisms
-
-
?
TNFalpha + H2O
?
-
inactivation by degradation of human TNFalpha on host cell surface and recombinant fibroblast cell surface, leading to inhibition of biological functions of TNFalpha, overview
-
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
transferrin + H2O
hemin + ?
-
slight truncation of the polypeptide chain in serum
-
?
additional information
?
-
-
the enzyme makes a significant contribution to the virulence of Porphyromonas gingivalis
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
additional information
?
-
-
a combination of both arginine- and lysine-specific gingipain activity is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin, interaction with oxyhemoglobin, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains R are potent permeability enhancement factors by prekallikrein activation and bradykinin induction, the enzyme degrades proteins of connective tissue, cell surface proteins and receptors, cytokines and plasma proteins, including components of the coagulation and complement cascades, heme- and iron-binding proteins, immunoglobulins and proteinase inhibitors
-
-
?
additional information
?
-
-
gingipains R mediate coaggregation of Porphyromonas gingivalis with other bacteria, overview
-
-
?
additional information
?
-
-
the enzyme degrades host iron- and heme-containing proteins, regulation of enzyme expression, overview, inhibition of gingipain increases the hmuR gene expression encoding the heme/hemoglobin receptor HmuR, and decreases the cell growth in the early and middle stages, but not in the late stages
-
-
?
additional information
?
-
-
the enzyme inactivates a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling involving CD25, but has no effect on TLR2-and TLR4-dependent signaling, overview
-
-
?
additional information
?
-
-
implicated in a wide range of both pathological and physiological processes of Porphyromonas gingivalis, including destruction of periodontal tissue, disruption of host defense mechanisms, processing of bacterial cell surface and secretory proteins, and acquisition of heme and amino acids, involved in atherosclerotic processes
-
-
?
additional information
?
-
-
important for the provision of nutrients for the bacterium in the host organism, destruction of host tissue, modulation of host immune response
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, activation of the C1 complex in serum, degradation of multiple complement components, important factor for the resistance to the bacteriolytic activity of serum
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, involved in the perturbation of host defense and the destruction and invasion of host tissues, degradation of hosts proteins such as ICAM-1m VCAM-1, catenins, and cadherins, involved in the shedding of syndecan-1
-
-
?
additional information
?
-
-
important virulence factors in periodontitis, probably involved in the reduction of T-cell function at periodontal lesion sites, induction of PAR-1 and PAR-2 receptor expression, up-regulation of PAR-4 expression, little effect on PAR-3 expression, increases expression of CD69 and CD25 on T-cells
-
-
?
additional information
?
-
-
involved in the deregulation of the hosts inflammatory response
-
-
?
additional information
?
-
-
involved in the induction of apoptosis in caspase dependent and caspase independent pathway
-
-
?
additional information
?
-
-
involved in the regulation of mRNA expression for the receptor activator of NF-kappaB ligand (RANKL) protein
-
-
?
additional information
?
-
-
no degradation of ICAM-3
-
-
?
additional information
?
-
-
extracellular gingipain protease activities cause a lack of secondary cytokine response in human cells after challenge with live Porphyromonas gingivalis
-
-
?
additional information
?
-
-
gingipains are cysteine proteinases and virulence factors of Porphyromonas gingivalis, the major causative bacterium of periodontal disease. Gingipains stimulate interleukin-8 secretion from human THP-1 cells, which is completely inhibited by proteinase inhibitors of gingipain and is increased in the presence of pathogen-associated molecular patterns, PAMPs, overview
-
-
?
additional information
?
-
-
gingipains are involved in bacterial adherence to host cells, RgpA binds to adhesin via its adhesin binding domain. Peptide A44 derived from the adhesin domain of RgpA plays a role in binding of Porphyromonas gingivalis to HEP-2 epithelial cells via cell surface receptors, e.g. clathrin, nocodazole and paclitaxel, which disrupt microtubule formation, block the interaction, while genistein does not
-
-
?
additional information
?
-
-
gingipains are key virulence determinants of Porphyromonas gingivalis and play a crucial role in pathogenicity
-
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
additional information
?
-
-
enzyme disrupts interaction between fibronectin and integrin in human fibroblasts, leading to cell death of detached fibroblasts, which contributes to the tissue damage in periodontal disease caused by Porphyromonas gingivalis
-
?
additional information
?
-
-
gingipains reduce cyclin expression and cause early G1 arrest, leading to the inhibition of cellular proliferation in murine ST2 osteoblastic/stromal cells, overview
-
-
?
additional information
?
-
-
gingipains cleave a broad range of in-host proteins and are key virulence factors in the onset and development of human adult periodontitis, the enzyme stimulates production of hepatocyte growth factor, i.e. scatter factor, through protease-activated receptors in human gingival fibroblasts in culture, overview
-
-
?
additional information
?
-
-
gingipains are essential for bacterial virulence and survival
-
-
?
additional information
?
-
-
HRgpA-mediated downregulation and RgpB-mediated upregulation of production of interleukin-8, occurs through protease-activated receptors, PAR-1 and PAR-2, signalling, RgpB-mediated upregulation of IL-8 production occurs through nuclear factor-kappa B, which does not affect HRgpA-mediated downregulation, overview. Gingipains preferentially suppress IL-8, resulting in attenuation of the cellular recognition of bacteria, and as a consequence, sustain chronic inflammation
-
-
?
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Kirszbaum, L.; Sotiropoulos, C.; Jackson, C.; Cleal, S.; Slakeski, N.; Reynolds, E.C.
Complete nucleotide sequence of a gene prtR of Porphyromonas gingivalis W50 encoding a 132 kDa protein that contains an arginine-specific thiol endopeptidase domain and a haemagglutinin domain
Biochem. Biophys. Res. Commun.
207
424-431
1995
Porphyromonas gingivalis, Porphyromonas gingivalis W50
brenda
Chen, Z.; Potempa, J.; Polanowski, A.; Wikstrom, M.; Travis, J.
Purification and characterization of a 50-kDa cysteine proteinase (gingipain) from Porphyromonas gingivalis
J. Biol. Chem.
267
18896-18901
1992
Porphyromonas gingivalis
brenda
Pavloff, N.; Potempa, J.; Pike, R.N.; Prochazka, V.; Kiefer, M.C.; Travis, J.; Barr, P.J.
Molecular cloning and structural characterization of the Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein
J. Biol. Chem.
270
1007-1010
1995
Porphyromonas gingivalis
brenda
Nakayama, K.; Kadowaki, T.; Okamoto, K.; Yamamoto, K.
Construction and characterization of arginine-specific cysteine proteinase (Arg-gingipain)-deficient mutants of Porphyromonas gingivalis. Evidence for significant contribution of Arg-gingipain to virulence
J. Biol. Chem.
270
23619-23626
1995
Porphyromonas gingivalis
brenda
Potempa, J.; Pike, R.; Travis, J.
The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain
Infect. Immun.
63
1176-1182
1995
Porphyromonas gingivalis, Porphyromonas gingivalis H66
brenda
Bedi, G.S.
Purification and characterization of lysine- and arginine-specific gingivain proteases from Porphyromonas gingivalis
Prep. Biochem.
24
251-261
1994
Porphyromonas gingivalis
brenda
Fujimura, S.; Hirai, K.; Shibata, Y.; Nakayama, K.; Nakamura, T.
Comparative properties of envelope-associated arginine-gingipains and lysine-gingipain of Porphyromonas gingivalis
FEMS Microbiol. Lett.
163
173-179
1998
Porphyromonas gingivalis
brenda
Sroka, A.; Sztukowska, M.; Potempa, J.; Travis, J.; Genco, C.A.
Degradation of host heme proteins by lysine- and arginine-specific cysteine proteinases (gingipains) of Porphyromonas gingivalis
J. Bacteriol.
183
5609-5616
2001
Porphyromonas gingivalis, Porphyromonas gingivalis A7436
brenda
Ally, N.; Whisstock, J.C.; Sieprawska-Lupa, M.; Potempa, J.; Le Bonniec, B.F.; Travis, J.; Pike, R.N.
Characterization of the specificity of arginine-specific gingipains from Porphyromonas gingivalis reveals active site differences between different forms of the enzymes
Biochemistry
42
11693-11700
2003
Porphyromonas gingivalis
brenda
Banbula, A.; Mak, P.; Smoluch, M.; Travis, J.; Potempa, J.
Arginine-specific cysteine proteinase from Porphyromonas gingivalis as a convenient tool in protein chemistry
Biol. Chem.
382
1399-1404
2001
Porphyromonas gingivalis
brenda
Baba, A.; Abe, N.; Kadowaki, T.; Nakanishi, H.; Ohishi, M.; Asao, T.; Yamamoto, K.
Arg-gingipain is responsible for the degradation of cell adhesion molecules of human gingival fibroblasts and their death induced by Porphyromonas gingivalis
Biol. Chem.
382
817-824
2001
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Krauser, A.; Potempa, J.; Travis, J.; Powers, J.C.
Inhibition f arginie gingipains (RgpB and HRgpA) with benzamidine inhibitors: zinc increases inhibitory potency
Biol. Chem.
383
1193-1198
2002
Porphyromonas gingivalis
brenda
Eichinger, A.; Beisel, H.G.; Jacob, U.; Huber, R.; Medrano, F.J.; Banbula, A.; Potempa, J.; Travis, J.; Bode, W.
Crystal structure of gingipain R: an Arg-specific bacterial cysteine proteinase with caspase-like fold
EMBO J.
18
5453-5462
1999
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
Houle, M.A.; Grenier, D.; Plamodon, P.; Nakayama, K.
The collagenase activity of Porphyromonas gingivalis is due to Arg-gingipain
FEMS Microbiol. Lett.
221
181-185
2003
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Potempa, J.; Mikolajczyk-Pawlinska, J.; Brassell, D.; Nelson, D.; Thogersen, I.B.; Enghild, J.J.; Travis, J.
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
1998
Porphyromonas gingivalis, Porphyromonas gingivalis (B2RKU0), Porphyromonas gingivalis (Q51844), Porphyromonas gingivalis HG66, Porphyromonas gingivalis HG66 (Q51844), Porphyromonas gingivalis ATCC 33277 (B2RKU0)
brenda
Imamura, T.; Banbula, A.; Pereira, P.J.B.; TRavis, J.; Potempa, J.
Activation of human prothrombin by arginine-specific cysteine proteinases (gingipain R) from POrphyromonas gingivalis
J. Biol. Chem.
276
18984-18991
2001
Porphyromonas gingivalis
brenda
Banbula, A.; Potempa, J.; Travis, J.; Bode, W.; Medrano, F.J.
Crystallization and preliminary X-ray diffraction analysis of gingipain R2 from Porphyromonas gingivalis in complex with H-D-Phe-Phe-Arg-chloromethylketone
Protein Sci.
7
1259-1261
1998
Porphyromonas gingivalis
brenda
Smalley, J.W.; Thomas, M.F.; Birss, A.J.; Withnall, R.; Silver, J.
A combination of both arginine- and lysine-specific gingipain activity of Porphyromonas gingivalis is necessary for the generation of the micro-oxo bishaem-containing pigment from haemoglobin
Biochem. J.
379
833-840
2004
Porphyromonas gingivalis
brenda
Abe, N.; Baba, A.; Takii, R.; Nakayama, K.; Kamaguchi, A.; Shibata, Y.; Abiko, Y.; Okamoto, K.; Kadowaki, T.; Yamamoto, K.
Roles of Arg- and Lys-gingipains in coaggregation of Porphyromonas gingivalis: identification of its responsible molecules in translation products of rgpA, kgp, and hagA genes
Biol. Chem.
385
1041-1047
2004
Porphyromonas gingivalis
brenda
Liu, X.; Sroka, A.; Potempa, J.; Genco, C.A.
Coordinate expression of the Porphyromonas gingivalis lysine-specific gingipain proteinase, Kgp, arginine-specific gingipain proteinase, RgpA, and the heme/hemoglobin receptor, HmuR
Biol. Chem.
385
1049-1057
2004
Porphyromonas gingivalis
brenda
Imamura, T.; Potempa, J.; Travis, J.
Gingipain R
Handbook of Proteolytic Enzymes (Barrett, A. J. ; Rawlings, N. D. ; Woessner, J. F. ; eds. )
2
1319-1328
2004
Porphyromonas gingivalis
-
brenda
Veith, P.D.; Chen, Y.Y.; Reynolds, E.C.
Porphyromonas gingivalis RgpA and Kgp proteinases and adhesins are C terminally processed by the carboxypeptidase CPG70
Infect. Immun.
72
3655-3657
2004
Porphyromonas gingivalis, Porphyromonas gingivalis RgpA
brenda
Mezyk-Kopec, R.; Bzowska, M.; Potempa, J.; Bzowska, M.; Jura, N.; Sroka, A.; Black, R.A.; Bereta, J.
Inactivation of membrane tumor necrosis factor alpha by gingipains from Porphyromonas gingivalis
Infect. Immun.
73
1506-1514
2005
Porphyromonas gingivalis
brenda
Rangarajan, M.; Hashim, A.; Aduse-Opoku, J.; Paramonov, N.; Hounsell, E.F.; Curtis, M.A.
Expression of Arg-gingipain RgpB is required for correct glycosylation and stability of monomeric Arg-gingipain RgpA from Porphyromonas gingivalis W50
Infect. Immun.
73
4864-4878
2005
Porphyromonas gingivalis
brenda
Uehara, A.; Muramoto, K.; Imamura, T.; Nakayama, K.; Potempa, J.; Travis, J.; Sugawara, S.; Takada, H.
Arginine-specific gingipains from Porphyromonas gingivalis stimulate production of hepatocyte growth factor (scatter factor) through protease-activated receptors in human gingival fibroblasts in culture
J. Immunol.
175
6076-6084
2005
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
Bialas, A.; Grembecka, J.; Krowarsch, D.; Otlewski, J.; Potempa, J.; Mucha, A.
Exploring the Sn binding pockets in gingipains by newly developed inhibitors: structure-based design, chemistry, and activity
J. Med. Chem.
49
1744-1753
2006
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
Kishimoto, M.; Yoshimura, A.; Naito, M.; Okamoto, K.; Yamamoto, K.; Golenbock, D.T.; Hara, Y.; Nakayama, K.
Gingipains inactivate a cell surface ligand on Porphyromonas gingivalis that induces TLR2-and TLR4-independent signaling
Microbiol. Immunol.
50
315-325
2006
Porphyromonas gingivalis
brenda
Naito, M.; Sakai, E.; Shi, Y.; Ideguchi, H.; Shoji, M.; Ohara, N.; Yamamoto, K.; Nakayama, K.
Porphyromonas gingivalis-induced platelet aggregation in plasma depends on Hgp44 adhesin but not Rgp proteinase
Mol. Microbiol.
59
152-167
2006
Porphyromonas gingivalis
brenda
Cronan, C.A.; Potempa, J.; Travis, J.; Mayo, J.A.
Inhibition of Porphyromonas gingivalis proteinases (gingipains) by chlorhexidine: synergistic effect of Zn(II)
Oral Microbiol. Immunol.
21
212-217
2006
Porphyromonas gingivalis
brenda
Smalley, J.W.; Birss, A.J.; Szmigielski, B.; Potempa, J.
Sequential action of R- and K-specific gingipains of Porphyromonas gingivalis in the generation of the haem-containing pigment from oxyhemoglobin
Arch. Biochem. Biophys.
465
44-49
2007
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
Hashimoto, M.; Kadowaki, T.; Tsukuba, T.; Yamamoto, K.
Selective proteolysis of apolipoprotein B-100 by Arg-gingipain mediates atherosclerosis progression accelerated by bacterial exposure
J. Biochem.
140
713-723
2006
Porphyromonas gingivalis
brenda
Into, T.; Inomata, M.; Kanno, Y.; Matsuyama, T.; Machigashira, M.; Izumi, Y.; Imamura, T.; Nakashima, M.; Noguchi, T.; Matsushita, K.
Arginine-specific gingipains from Porphyromonas gingivalis deprive protective functions of secretory leucocyte protease inhibitor in periodontal tissue
Clin. Exp. Immunol.
145
545-554
2006
Porphyromonas gingivalis
brenda
Yun, L.W.; Decarlo, A.A.; Hunter, N.
Blockade of protease-activated receptors on T cells correlates with altered proteolysis of CD27 by gingipains of Porphyromonas gingivalis
Clin. Exp. Immunol.
150
217-229
2007
Porphyromonas gingivalis
brenda
Yasaki-Inagaki, Y.; Inagaki, S.; Yamada, S.; Okuda, K.; Ishihara, K.
Production of protective antibodies against Porphyromonas gingivalis strains by immunization with recombinant gingipain domains
FEMS Immunol. Med. Microbiol.
47
287-295
2006
Porphyromonas gingivalis
brenda
Kato, T.; Tsuda, T.; Omori, H.; Kato, T.; Yoshimori, T.; Amano, A.
Maturation of fimbria precursor protein by exogenous gingipains in Porphyromonas gingivalis gingipain-null mutant
FEMS Microbiol. Lett.
273
96-102
2007
Porphyromonas gingivalis
brenda
Sheets, S.M.; Potempa, J.; Travis, J.; Fletcher, H.M.; Casiano, C.A.
Gingipains from Porphyromonas gingivalis W83 synergistically disrupt endothelial cell adhesion and can induce caspase-independent apoptosis
Infect. Immun.
74
5667-5678
2006
Porphyromonas gingivalis
brenda
Seers, C.A.; Slakeski, N.; Veith, P.D.; Nikolof, T.; Chen, Y.Y.; Dashper, S.G.; Reynolds, E.C.
The RgpB C-terminal domain has a role in attachment of RgpB to the outer membrane and belongs to a novel C-terminal-domain family found in Porphyromonas gingivalis
J. Bacteriol.
188
6376-6386
2006
Porphyromonas gingivalis
brenda
Popadiak, K.; Potempa, J.; Riesbeck, K.; Blom, A.M.
Biphasic effect of gingipains from Porphyromonas gingivalis on the human complement system
J. Immunol.
178
7242-7250
2007
Porphyromonas gingivalis
brenda
Belibasakis, G.N.; Bostanci, N.; Hashim, A.; Johansson, A.; Aduse-Opoku, J.; Curtis, M.A.; Hughes, F.J.
Regulation of RANKL and OPG gene expression in human gingival fibroblasts and periodontal ligament cells by Porphyromonas gingivalis: a putative role of the Arg-gingipains
Microb. Pathog.
43
46-53
2007
Porphyromonas gingivalis
brenda
Saiki, K.; Konishi, K.
Identification of a Porphyromonas gingivalis novel protein sov required for the secretion of gingipains
Microbiol. Immunol.
51
483-491
2007
Porphyromonas gingivalis
brenda
Roy, F.; Vanterpool, E.; Fletcher, H.M.
HtrA in Porphyromonas gingivalis can regulate growth and gingipain activity under stressful environmental conditions
Microbiology
152
3391-3398
2006
Porphyromonas gingivalis
brenda
Andrian, E.; Grenier, D.; Rouabhia, M.
Porphyromonas gingivalis gingipains mediate the shedding of syndecan-1 from the surface of gingival epithelial cells
Oral Microbiol. Immunol.
21
123-128
2006
Porphyromonas gingivalis
brenda
Uehara, A.; Imamura, T.; Potempa, J.; Travis, J.; Takada, H.
Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease-activated receptors with Toll-like receptor and NOD1/2 ligands in human monocytic cells
Cell. Microbiol.
10
1181-1189
2008
Porphyromonas gingivalis
brenda
Boisvert, H.; Duncan, M.J.
Clathrin-dependent entry of a gingipain adhesin peptide and Porphyromonas gingivalis into host cells
Cell. Microbiol.
10
2538-2552
2008
Porphyromonas gingivalis
brenda
Uehara, A.; Naito, M.; Imamura, T.; Potempa, J.; Travis, J.; Nakayama, K.; Takada, H.
Dual regulation of interleukin-8 production in human oral epithelial cells upon stimulation with gingipains from Porphyromonas gingivalis
J. Med. Microbiol.
57
500-507
2008
Porphyromonas gingivalis
brenda
Bania, J.; Kubiak, A.; Wojtachnio, K.; Polanowski, A.
Pancreatic secretory trypsin inhibitor acts as an effective inhibitor of cysteine proteinases gingipains from Porphyromonas gingivalis
J. Periodont. Res.
43
232-236
2008
Porphyromonas gingivalis
brenda
Kato, T.; Tsuda, T.; Inaba, H.; Kawai, S.; Okahashi, N.; Shibata, Y.; Abiko, Y.; Amano, A.
Porphyromonas gingivalis gingipains cause G(1) arrest in osteoblastic/stromal cells
Oral Microbiol. Immunol.
23
158-164
2008
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Stathopoulou, P.G.; Benakanakere, M.R.; Galicia, J.C.; Kinane, D.F.
The host cytokine response to Porphyromonas gingivalis is modified by gingipains
Oral Microbiol. Immunol.
24
11-17
2009
Porphyromonas gingivalis
brenda
Taiyoji, M.; Shitomi, Y.; Taniguchi, M.; Saitoh, E.; Ohtsubo, S.
Identification of proteinaceous inhibitors of a cysteine proteinase (an Arg-specific gingipain) from Porphyromonas gingivalis in rice grain, using targeted-proteomics approaches
J. Proteome Res.
8
5165-5174
2009
Porphyromonas gingivalis
brenda
Kantyka, T.; Latendorf, T.; Wiedow, O.; Bartels, J.; Glaeser, R.; Dubin, G.; Schroeder, J.M.; Potempa, J.; Meyer-Hoffert, U.
Elafin is specifically inactivated by RgpB from Porphyromonas gingivalis by distinct proteolytic cleavage
Biol. Chem.
390
1313-1320
2009
Porphyromonas gingivalis (P28784), Porphyromonas gingivalis (P95493)
brenda
Stathopoulou, P.; Galicia, J.; Benakanakere, M.; Garcia, C.; Potempa, J.; Kinane, D.
Porphyromonas gingivalis induce apoptosis in human gingival epithelial cells through a gingipain-dependent mechanism
BMC Microbiol.
9
107
2009
Porphyromonas gingivalis
brenda
Kuboniwa, M.; Amano, A.; Hashino, E.; Yamamoto, Y.; Inaba, H.; Hamada, N.; Nakayama, K.; Tribble, G.D.; Lamont, R.J.; Shizukuishi, S.
Distinct roles of long/short fimbriae and gingipains in homotypic biofilm development by Porphyromonas gingivalis
BMC Microbiol.
9
105
2009
Porphyromonas gingivalis
brenda
Saiki, K.; Konishi, K.
The role of Sov protein in the secretion of gingipain protease virulence factors of Porphyromonas gingivalis
FEMS Microbiol. Lett.
302
166-174
2010
Porphyromonas gingivalis
brenda
Haruyama, K.; Yoshimura, A.; Naito, M.; Kishimoto, M.; Shoji, M.; Abiko, Y.; Hara, Y.; Nakayama, K.
Identification of a gingipain-sensitive surface ligand of Porphyromonas gingivalis that induces Toll-like receptor 2- and 4-independent NF-kappaB activation in CHO cells
Infect. Immun.
77
4414-4420
2009
Porphyromonas gingivalis
brenda
Furuta, N.; Takeuchi, H.; Amano, A.
Entry of Porphyromonas gingivalis outer membrane vesicles into epithelial cells causes cellular functional impairment
Infect. Immun.
77
4761-4770
2009
Porphyromonas gingivalis
brenda
Monteiro, A.C.; Scovino, A.; Raposo, S.; Gaze, V.M.; Cruz, C.; Svensjoe, E.; Narciso, M.S.; Colombo, A.P.; Pesquero, J.B.; Feres-Filho, E.; Nguyen, K.A.; Sroka, A.; Potempa, J.; Scharfstein, J.
Kinin danger signals proteolytically released by gingipain induce Fimbriae-specific IFN-gamma- and IL-17-producing T cells in mice infected intramucosally with Porphyromonas gingivalis
J. Immunol.
183
3700-3711
2009
Porphyromonas gingivalis
brenda
Fitzpatrick, R.E.; Aprico, A.; Wijeyewickrema, L.C.; Pagel, C.N.; Wong, D.M.; Potempa, J.; Mackie, E.J.; Pike, R.N.
High molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism
J. Innate Immun.
1
109-117
2009
Porphyromonas gingivalis
brenda
Inomata, M.; Ishihara, Y.; Matsuyama, T.; Imamura, T.; Maruyama, I.; Noguchi, T.; Matsushita, K.
Degradation of vascular endothelial thrombomodulin by arginine- and lysine-specific cysteine proteases from Porphyromonas gingivalis
J. Periodontol.
80
1511-1517
2009
Porphyromonas gingivalis
brenda
Giacaman, R.A.; Asrani, A.C.; Ross, K.F.; Herzberg, M.C.
Cleavage of protease-activated receptors on an immortalized oral epithelial cell line by Porphyromonas gingivalis gingipains
Microbiology
155
3238-3246
2009
Porphyromonas gingivalis
brenda
Li, N.; Yun, P.; Nadkarni, M.; Ghadikolaee, N.; Nguyen, K.; Lee, M.; Hunter, N.; Collyer, C.
Structure determination and analysis of a haemolytic gingipain adhesin domain from Porphyromonas gingivalis
Mol. Microbiol.
76
861-873
2010
Porphyromonas gingivalis
brenda
Skottrup, P.D.; Leonard, P.; Kaczmarek, J.Z.; Veillard, F.; Enghild, J.J.; OKennedy, R.; Sroka, A.; Clausen, R.P.; Potempa, J.; Riise, E.
Diagnostic evaluation of a nanobody with picomolar affinity toward the protease RgpB from Porphyromonas gingivalis
Anal. Biochem.
415
158-167
2011
Porphyromonas gingivalis
brenda
Toh, E.C.; Dashper, S.G.; Huq, N.L.; Attard, T.J.; OBrien-Simpson, N.M.; Chen, Y.Y.; Cross, K.J.; Stanton, D.P.; Paolini, R.A.; Reynolds, E.C.
Porphyromonas gingivalis cysteine proteinase inhibition by kappa-casein peptides
Antimicrob. Agents Chemother.
55
1155-1161
2011
Porphyromonas gingivalis
brenda
Dashper, S.G.; Pan, Y.; Veith, P.D.; Chen, Y.Y.; Toh, E.C.; Liu, S.W.; Cross, K.J.; Reynolds, E.C.
Lactoferrin inhibits Porphyromonas gingivalis proteinases and has sustained biofilm inhibitory activity
Antimicrob. Agents Chemother.
56
1548-1556
2012
Porphyromonas gingivalis
brenda
Maisetta, G.; Brancatisano, F.; Esin, S.; Campa, M.; Batoni, G.
Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-beta-defensin 3 and affect peptides antibacterial activity in vitro
Peptides
32
1073-1077
2011
Porphyromonas gingivalis
brenda
Smalley, J.; Byrne, D.; Birss, A.; Wojtowicz, H.; Sroka, A.; Potempa, J.; Olczak, T.
HmuY haemophore and gingipain proteases constitute a unique syntrophic system of haem acquisition by Porphyromonas gingivalis
PLoS ONE
6
e17182
2011
Porphyromonas gingivalis
brenda
Veillard, F.; Sztukowska, M.; Mizgalska, D.; Ksiazek, M.; Houston, J.; Potempa, B.; Enghild, J.J.; Thogersen, I.B.; Gomis-Rueth, F.X.; Nguyen, K.A.; Potempa, J.
Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases
Biochim. Biophys. Acta
1830
4218-4228
2013
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
Ruggiero, S.; Cosgarea, R.; Potempa, J.; Potempa, B.; Eick, S.; Chiquet, M.
Cleavage of extracellular matrix in periodontitis: gingipains differentially affect cell adhesion activities of fibronectin and tenascin-C
Biochim. Biophys. Acta
1832
517-526
2013
Porphyromonas gingivalis
brenda
Veillard, F.; Potempa, B.; Guo, Y.; Ksiazek, M.; Sztukowska, M.N.; Houston, J.A.; Koneru, L.; Nguyen, K.A.; Potempa, J.
Purification and characterisation of recombinant His-tagged RgpB gingipain from Porphymonas gingivalis
Biol. Chem.
396
377-384
2015
Porphyromonas gingivalis
brenda
Taniguchi, M.; Matsuhashi, Y.; Abe, T.K.; Ishiyama, Y.; Saitoh, E.; Kato, T.; Ochiai, A.; Tanaka, T.
Contribution of cationic amino acids toward the inhibition of Arg-specific cysteine proteinase (Arg-gingipain) by the antimicrobial dodecapeptide, CL(14-25), from rice protein
Biopolymers
102
379-389
2014
Porphyromonas gingivalis (B2RKK0), Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277 (B2RKK0)
brenda
Taiyoji, M.; Yamanaka, T.; Tsuno, T.; Ohtsubo, S.
Potential value of a rice protein extract, containing proteinaceous inhibitors against cysteine proteinases from Porphyromonas gingivalis, for managing periodontal diseases
Biosci. Biotechnol. Biochem.
77
80-86
2013
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Jayaprakash, K.; Khalaf, H.; Bengtsson, T.
Gingipains from Porphyromonas gingivalis play a significant role in induction and regulation of CXCL8 in THP-1 cells
BMC Microbiol.
14
193
2014
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Bao, K.; Belibasakis, G.N.; Thurnheer, T.; Aduse-Opoku, J.; Curtis, M.A.; Bostanci, N.
Role of Porphyromonas gingivalis gingipains in multi-species biofilm formation
BMC Microbiol.
14
258
2014
Porphyromonas gingivalis, Porphyromonas gingivalis K1A
brenda
Jung, Y.J.; Jun, H.K.; Choi, B.K.
Contradictory roles of Porphyromonas gingivalis gingipains in caspase-1 activation
Cell. Microbiol.
17
1304-1319
2015
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Kataoka, S.; Baba, A.; Suda, Y.; Takii, R.; Hashimoto, M.; Kawakubo, T.; Asao, T.; Kadowaki, T.; Yamamoto, K.
A novel, potent dual inhibitor of Arg-gingipains and Lys-gingipain as a promising agent for periodontal disease therapy
FASEB J.
28
3564-3578
2014
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Chen, Y.Y.; Seers, C.A.; Slakeski, N.; Moore, C.; Zhang, L.; Reynolds, E.C.
Reversible redox regulation of specificity of Arg-gingipain B in Porphyromonas gingivalis
FEBS Lett.
587
1275-1280
2013
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
de Diego, I.; Veillard, F.T.; Guevara, T.; Potempa, B.; Sztukowska, M.; Potempa, J.; Gomis-Rueth, F.X.
Porphyromonas gingivalis virulence factor gingipain RgpB shows a unique zymogenic mechanism for cysteine peptidases
J. Biol. Chem.
288
14287-14296
2013
Porphyromonas gingivalis (P95493), Porphyromonas gingivalis, Porphyromonas gingivalis W83 (P95493)
brenda
van der Post, S.; Subramani, D.B.; Baeckstroem, M.; Johansson, M.E.; Vester-Christensen, M.B.; Mandel, U.; Bennett, E.P.; Clausen, H.; Dahlen, G.; Sroka, A.; Potempa, J.; Hansson, G.C.
Site-specific O-glycosylation on the MUC2 mucin protein inhibits cleavage by the Porphyromonas gingivalis secreted cysteine protease (RgpB)
J. Biol. Chem.
288
14636-14646
2013
Porphyromonas gingivalis, Porphyromonas gingivalis HG66
brenda
Nakayama, M.; Inoue, T.; Naito, M.; Nakayama, K.; Ohara, N.
Attenuation of the phosphatidylinositol 3-kinase/Akt signaling pathway by Porphyromonas gingivalis gingipains RgpA, RgpB, and Kgp
J. Biol. Chem.
290
5190-5202
2015
Porphyromonas gingivalis
brenda
Froehlich, E.; Kantyka, T.; Plaza, K.; Schmidt, K.H.; Pfister, W.; Potempa, J.; Eick, S.
Benzamidine derivatives inhibit the virulence of Porphyromonas gingivalis
Mol. Oral Microbiol.
28
192-203
2013
Porphyromonas gingivalis (P28784), Porphyromonas gingivalis (P95493), Porphyromonas gingivalis, Porphyromonas gingivalis W83 (P95493), Porphyromonas gingivalis ATCC 33277 (P28784)
brenda
Haraguchi, A.; Miura, M.; Fujise, O.; Hamachi, T.; Nishimura, F.
Porphyromonas gingivalis gingipain is involved in the detachment and aggregation of Aggregatibacter actinomycetemcomitans biofilm
Mol. Oral Microbiol.
29
131-143
2014
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Palm, E.; Khalaf, H.; Bengtsson, T.
Suppression of inflammatory responses of human gingival fibroblasts by gingipains from Porphyromonas gingivalis
Mol. Oral Microbiol.
30
74-85
2015
Porphyromonas gingivalis, Porphyromonas gingivalis ATCC 33277
brenda
Cherian, C.; Jannet Vennila, J.; Sharan, L.
Marine bromophenols as an effective inhibitor of virulent proteins (peptidyl arginine deiminase, gingipain R and hemagglutinin A) in Porphyromas gingivalis
Arch. Oral Biol.
100
119-128
2019
Porphyromonas gingivalis
brenda
Dou, Y.; Robles, A.; Roy, F.; Aruni, A.; Sandberg, L.; Nothnagel, E.; Fletcher, H.
The roles of RgpB and Kgp in late onset gingipain activity in the vimA-defective mutant of Porphyromonas gingivalis W83
Mol. Oral Microbiol.
30
347-360
2015
Porphyromonas gingivalis, Porphyromonas gingivalis (P95493), Porphyromonas gingivalis W83, Porphyromonas gingivalis W83 (P95493)
brenda
Pourhajibagher, M.; Bahador, A.
In silico identification of a therapeutic target for photo-activated disinfection with indocyanine green Modeling and virtual screening analysis of Arg-gingipain from Porphyromonas gingivalis
Photodiagnosis Photodyn. Ther.
18
149-154
2017
Porphyromonas gingivalis (P72197), Porphyromonas gingivalis
brenda