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3-aminobenzoyl-Ala-Ala-Ile-Lys-Ala-Gly-Ala-Arg + H2O
?
3-aminobenzoyl-Ala-Glu-Ile-Lys-Gln-Pro-Val-Val + H2O
?
-
-
-
-
?
3-aminobenzoyl-Asp-Lys-Val-Asn-Leu-Gly-Gly-Glu + H2O
?
3-aminobenzoyl-Glu-Gln-Ile-Lys-Glu-Asn-Lys-Lys + H2O
?
3-aminobenzoyl-Thr-Thr-Thr-Ala-Gly-Thr-Ala-Glu + H2O
?
acetyl-Ala-Ile-Arg-7-amino-4-methylcoumarin + H2O
?
alpha1-antitrypsin + H2O
?
-
-
-
-
?
azocasein + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Ala + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Glu-p-nitrophenyl ester + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Glu-Phe + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-Gly-p-nitrophenyl ester + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
benzyloxycarbonyl-Gly + p-nitrophenol
-
-
-
-
?
benzyloxycarbonyl-Nle-p-nitrophenyl ester + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Nle-Phe + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide + H2O
?
Bovine serum albumin + H2O
?
C5a peptidase + H2O
?
-
cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
-
-
?
cinnamoyl-Gly-p-nitrophenyl ester + H2O
cinnamoyl-Gly + 4-nitrophenol
-
-
-
-
?
complement component C3 + H2O
?
-
-
-
-
?
complement factor C3b + H2O
?
-
cleavage sites are RTL-D, NHK-L, LAR-S, and VEL-I
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
?
-
-
-
-
?
decorin + H2O
?
-
-
-
-
?
E-cadherin + H2O
?
-
-
-
-
?
EndoS + H2O
?
-
cleavage site is VML-K
-
-
?
FAAIKAGARY + H2O
FAAIK + AGARY
-
-
-
?
Fba protein + H2O
?
-
-
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
H-kininogen + H2O
?
-
cleavage sites are LMK-R and PFR-S
-
-
?
H-kininogen + H2O
biologically active kinins
-
-
-
?
human CXCL10 + H2O
?
-
-
-
-
?
human interleukin 1beta precursor + H2O
human interleukin 1beta + human interleukin 1beta signal peptide
-
-
-
-
?
IgD + H2O
?
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgE + H2O
?
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgG + H2O
Fab fragment + Gc fragments
-
the enzyme cleaves IgG in the flexible hinge region of the IgG heavy chain, generating two Fab fragments and Fc fragment. SpeB cleaves the heavy chain at a defined site between glycine residues 236 and 237
-
?
immunoglobulin A + H2O
?
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin D + H2O
?
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin E + H2O
?
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin G + H2O
?
-
cleavage site is LLG-G in gamma-chain
-
-
?
immunoglobulin G + H2O
F(ab')2 + 1/2Fc
-
non-immune binding of IgG to the bacterial surface is followed by the proteolytic cleavage of the antibody by the IgG-endopeptidase IdeS. IdeS generated 1/2Fc fragments do not compete efficiently with intact IgG in binding to the bacterial surface and rapid dissociation of 1/2Fc allows binding of new IgG. A correlated binding and proteolytic cleavage of IgG increases the probability that the bacteria can resist specific IgG, despite the presence of a large excess of non-specific IgG in the circulation. As a consequence of IdeS activity, circulating 1/2Fc fragments are generated. These 1/2Fc fragments are shown to be biological active by acting as priming agents for polymorphonuclear leucocytes
-
-
?
immunoglobulin G + H2O
F(ab')2 fragment + 1/2 Fc fragments
-
IdeS cleaves IgG by hydrolyzing the peptide bond between two glycine residues in the hinge region of IgG, generating one F(ab')2 fragment and two 1/2 Fc fragments
-
-
?
immunoglobulin M + H2O
?
-
cleavage sites are the heavy chains
-
-
?
insulin + H2O
?
-
reduced carboxymethylated phenylalanine chain, one of the most rapidly hydrolyzed Phe-Tyr linkages is in the Phe-Phe-Tyr sequence
-
-
?
insulin beta chain + H2O
?
-
reduced and carboxylated substrate, cleavage of the linkage Phe25-Tyr26
-
-
?
interleukin-1beta precursor + H2O
interleukin-1beta + interleukin-1beta propeptide
Laminin + H2O
?
-
-
-
-
?
M protein + H2O
?
-
-
-
-
?
mouse CXCL-2 + H2O
?
-
the cleavage site is between lysine residues K65 and K66
-
-
?
N-benzoyl-Gly-p-nitrophenyl ester + H2O
N-benzoyl-Gly + 4-nitrophenol
-
-
-
-
?
N-benzyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
-
?
N-benzyloxycarbonyl-Gly + H2O
?
-
-
-
-
?
N-benzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
N-benzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Lys-Phe + H2O
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Lys-phenyl ester + H2O
Nalpha-benzyloxycarbonyl-Lys + phenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Nepsilon-t-butyloxycarbonyl-Lys-Phe + H2O
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Nepsilon-tosyl-Lys-p-nitrophenyl ester + H2O
Nalpha-benzyloxycarbonyl-Nepsilon-tosyl-Lys + p-nitrophenol
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Phe-Phe + H2O
?
-
-
-
-
?
Nalpha-benzyloxycarbonyl-Phe-Tyr + H2O
?
-
-
-
-
?
Nepsilon-benzyloxycarbonyl-Lys-p-nitrophenyl ester + H2O
Nepsilon-benzyloxycarbonyl-Lys + 4-nitrophenol
-
-
-
-
?
occludin + H2O
?
-
-
-
-
?
p-nitrobenzyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
p-nitrobenzyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
-
?
p-nitrophenyl-benzyloxycarbonyl-L-Ala + H2O
?
-
-
-
-
?
plasminogen + H2O
?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
cleavage site is YVH-D
-
-
?
proSPE B C47S + H2O
?
-
the proSPE B C47S mutant is also be used as the substrate for activity assay because it does not exhibit any enzyme activity and exists as a 42 kDa zymogen
-
-
?
protein H + H2O
?
-
-
-
-
?
resorufin-labeled casein + H2O
?
-
-
-
-
?
SpeBz + H2O
mature SpeB + ?
-
auto-cleavage sites are AIK-A, KVN-L, QIK-E, TYA-G, and EIK-Q
-
-
?
streptococcal mitogenic exotoxin SmeZ + H2O
?
-
cleaves between glutamate and glycine residues
-
-
?
streptococcal mitogenic exotoxin SpeG + H2O
?
-
partial degradation, SpeB cleaves between glutamate and glycine residues
-
-
?
streptococcal mitogenic exotoxin Z + H2O
?
-
-
-
-
?
streptokinase + H2O
?
-
-
-
-
?
streptolysin O + H2O
?
-
-
-
-
?
t-butyloxycarbonyl-Gly-p-nitrophenyl ester + H2O
t-butyloxycarbonyl-Gly + 4-nitrophenol
-
-
-
-
?
tert-butyloxycarbonyl-Ala-p-nitrophenyl ester + H2O
tert-butyloxycarbonyl-Ala + 4-nitrophenol
-
-
-
-
?
urokinase receptor + H2O
?
-
cleavage site is close to the GPI anchor
-
-
?
Vitronectin + H2O
?
-
-
-
-
?
additional information
?
-
3-aminobenzoyl-Ala-Ala-Ile-Lys-Ala-Gly-Ala-Arg + H2O
?
-
-
-
-
?
3-aminobenzoyl-Ala-Ala-Ile-Lys-Ala-Gly-Ala-Arg + H2O
?
-
-
-
-
?
3-aminobenzoyl-Asp-Lys-Val-Asn-Leu-Gly-Gly-Glu + H2O
?
-
-
-
-
?
3-aminobenzoyl-Asp-Lys-Val-Asn-Leu-Gly-Gly-Glu + H2O
?
-
-
-
-
?
3-aminobenzoyl-Glu-Gln-Ile-Lys-Glu-Asn-Lys-Lys + H2O
?
-
-
-
-
?
3-aminobenzoyl-Glu-Gln-Ile-Lys-Glu-Asn-Lys-Lys + H2O
?
-
-
-
-
?
3-aminobenzoyl-Thr-Thr-Thr-Ala-Gly-Thr-Ala-Glu + H2O
?
-
-
-
-
?
3-aminobenzoyl-Thr-Thr-Thr-Ala-Gly-Thr-Ala-Glu + H2O
?
-
-
-
-
?
acetyl-Ala-Ile-Arg-7-amino-4-methylcoumarin + H2O
?
-
-
-
-
?
acetyl-Ala-Ile-Arg-7-amino-4-methylcoumarin + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide + H2O
?
-
-
-
-
?
benzyloxycarbonyl-Val-Arg-4-methylcoumarinyl-7-amide + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
Bovine serum albumin + H2O
?
-
-
-
-
?
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
bovine
-
-
?
Fba + H2O
?
-
a cell surface factor H- and factor H-like protein 1-binding protein of epithelial human cells, the enzyme inhibits complement regulatory protein factor H- and factor H-like protein 1 binding by proteolysis of the Fba protein, overview
-
-
?
Fba + H2O
?
-
a cell surface factor H- and factor H-like protein 1-binding protein of epithelial human cells
-
-
?
Fibrinogen + H2O
?
-
human fibrinogen
-
-
?
Fibrinogen + H2O
?
-
cleavage sites are C-terminally in Aalpha chains
-
-
?
human CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-2 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-2 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-6 + H2O
?
-
-
-
-
?
human CXCL-6 + H2O
?
-
-
-
-
?
human CXCL-8 + H2O
?
-
-
-
-
?
human CXCL-8 + H2O
?
-
-
-
-
?
Human fibrinogen + H2O
?
-
processing
-
-
?
Human fibrinogen + H2O
?
-
release and processing, the enzyme abolishes the binding of Streptococcus pyogenes to full-length or 30 kDa fragment of human fibrinogen Fn, kinetics overview
-
-
?
IgA + H2O
?
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgA + H2O
?
-
efficiently cleaved under reducing conditions but not under nonreducing conditions
-
-
?
IgG + H2O
?
-
efficiently cleaved under reducing conditions but not under nonreducing conditions
-
-
?
IgG + H2O
?
-
cleaves off the Fc part of antigen-bound IgG, the cleavage of IgG is not species restricted
-
?
IgG + H2O
?
-
the ability to cleave off the Fc part of antigen-bound IgG contributes to the escape of group A streptococci from opsonophygocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding
-
?
IgG + H2O
?
-
cleaves off the Fc part of antigen-bound IgG, the cleavage of IgG is not species restricted
-
?
IgG + H2O
?
-
the ability to cleave off the Fc part of antigen-bound IgG contributes to the escape of group A streptococci from opsonophygocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding
-
?
IgM + H2O
?
-
degradation of the carboxy-terminal part of the heavy chain
-
?
IgM + H2O
?
-
efficiently cleaved under reducing conditions but not under nonreducing conditions
-
-
?
interleukin-1beta precursor + H2O
interleukin-1beta + interleukin-1beta propeptide
-
-
-
?
interleukin-1beta precursor + H2O
interleukin-1beta + interleukin-1beta propeptide
-
-
-
?
mouse CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K65 and K66
-
-
?
mouse CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K65 and K66
-
-
?
properdin + H2O
?
-
-
-
-
?
properdin + H2O
?
-
cleavage of properdin leads to inhibition of complement-mediated opsonophagocytosis and bacterial killing by neutrophils, alternative complement pathway overview
-
-
?
proSpeB + H2O
SpeB + ?
autoactivation
-
-
?
proSpeB + H2O
SpeB + ?
autoactivation
-
-
?
protein F1 + H2O
?
-
-
-
-
?
protein F1 + H2O
?
-
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1, e.g. in human pharyngeal epithelial cells Detroit 562, while proteins H and M1 are protected by plasma proteins, overview
-
-
?
protein F1 + H2O
?
-
cell-wall-anchored protein F1
-
-
?
additional information
?
-
-
an unprotonated imidazole ring and the protonated form of the single sulfhydryl group are essential for activity
-
-
?
additional information
?
-
-
the enzyme also at low concentrations efficiently removes M1 protein and protein H from the streptococcal surface
-
-
?
additional information
?
-
-
the enzyme activates a 66000 Da matrix metalloprotease produced by human endothelial cells, a process that may contribute to endothelial cell damage, tissue destruction, and hemodynamic derangement
-
-
?
additional information
?
-
-
by removal of M1 protein and protein H from the streptococcal surface the enzyme regulates the bacterial cell-cell interactions, and perhaps also interactions with epithelial cells. Through expression of streptopain the enzyme can modify the composition of the surface proteins in response to environmental conditions. Such a mechanism will facilitate the adaption of the bacterium to its host
-
-
?
additional information
?
-
-
the enzyme can enhance the invasion ability of group A streptococci in human respiratory epithelial cells
-
-
?
additional information
?
-
-
the expression of the enzyme contributes to soft tissue pathology, including necrosis, and is required for efficient systemic dissemination of the organism from the initial site of skin inoculation
-
-
?
additional information
?
-
-
release of biological active kinins from kininogens present in human plasma
-
-
?
additional information
?
-
-
the enzyme is an important virulence factor
-
-
?
additional information
?
-
-
the enzyme is secreted under conditions of starvation and may be involved in nutrient acquisition
-
-
?
additional information
?
-
-
thus, although IgG might by a substrate for SpeB under certain environmental conditions, it seems unlikely that SpeB is part of the first line of defense against specific antibodies. Even though SpeB might not be directly involved in the attenuation of the adaptive immune response, its proteolytic activity towards streptococcal surface proteins, including IgG-binding proteins and the streptococcal C5a peptidase, could certainly be important for the modulation of the complement system
-
?
additional information
?
-
-
streptopain shows strepadhesin activity, independent of protease activity, mediated by a cell surface adhesin and controlled by the multiple gene regulator Mga
-
-
?
additional information
?
-
-
the enzyme can induce apoptosis in A549 cells, the induction of apoptosis in cells requires the protease activity and the propper enzyme size of 28 kDa, cell binding activity of processed and unprocessed wild-type and mutant enzymes, the induction can be prevented by inhibition of caspase-8, induction cascade, overview
-
-
?
additional information
?
-
-
the enzyme inactivates the metabolic activity of polymorphonuclear cells, the enzyme causes mitochondria damage to polymorphonuclear cells preventing phagocytosis of group A Streptococcus, it is essential for bacterial survival in blood, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is a virulence factor of Streptococcus pyogenes inducing the release of histamine in mast cells, basophils, and mononuclear cells, and increasing capillary permeability and histamine release in skin of guinea pigs, the recombinant enzyme shows mitogenic activity with human T-cells
-
-
?
additional information
?
-
-
cleavage site specificity, overview, the enzyme prefers cleavage of Phe-Tyr bonds, the enzyme shows poor activity with trypsin substrates fibrin, casein, and gelatin from human and rabbit
-
-
?
additional information
?
-
-
Spi and the Spe B pro-peptide both bind to mature Spe B, but are no substrates
-
-
?
additional information
?
-
-
the enzyme performs autolytic activity and also cleaves the inactive mutant C192S
-
-
?
additional information
?
-
-
the enzyme performs autolytic processing to the mature protein, interaction overview
-
-
?
additional information
?
-
-
does not cleave streptococcal mitogenic exotoxins SpeA and SpeJ
-
-
?
additional information
?
-
-
SPE B is able to autoactivate
-
-
?
additional information
?
-
-
the three-dimensional structure and backbone dynamics of the 28 kDa mature SPE B (mSPE B) is determined: Interactions between the C-terminal loop and the active site residues in mSPE B are observed. The structural differences between mSPE B and zymogen proSPE B are the conformation of the C-terminal loop and the orientation of the catalytic His-195 residue. Dynamics analysis of mSPEB and the mSPEB/inhibitor complexes show that the catalytic and C-terminal loops are the most flexible regions, suggesting that the flexible C-terminal loop of SPE B may play an important role in controlling the substrate binding, resulting in its broad substrate specificity
-
-
?
additional information
?
-
-
CXCL9 is quite resistant to hydrolysis by SpeB
-
-
?
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
-
-
?
additional information
?
-
-
SpeB has no immunoglobulin-degrading activity in human plasma or blood
-
-
?
additional information
?
-
streptopain can cleave a wide range of human proteins, including immunoglobulins, the complement activation system, chemokines, and structural proteins
-
-
?
additional information
?
-
-
streptopain can cleave a wide range of human proteins, including immunoglobulins, the complement activation system, chemokines, and structural proteins
-
-
?
additional information
?
-
-
the enzyme can induce apoptosis in A549 cells, the induction of apoptosis in cells requires the protease activity and the propper enzyme size of 28 kDa, cell binding activity of processed and unprocessed wild-type and mutant enzymes, the induction can be prevented by inhibition of caspase-8, induction cascade, overview
-
-
?
additional information
?
-
-
the enzyme performs autolytic activity and also cleaves the inactive mutant C192S
-
-
?
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
-
-
?
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
-
-
?
additional information
?
-
-
Spi and the Spe B pro-peptide both bind to mature Spe B, but are no substrates
-
-
?
additional information
?
-
-
the enzyme is not critical for the development of tissue necrosis, bacteremia and lethal infection in a murine model of human necrotizing fascilitis
-
-
?
additional information
?
-
-
critical virulence factor for invasive disease episode. Binds host cell integrins alphaVbeta3 and alphaIIbbeta3 through an RGD motif
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha1-antitrypsin + H2O
?
-
-
-
-
?
C5a peptidase + H2O
?
-
cleavage sites are APA-K, AVI-D, SGTS, and C-terminally
-
-
?
complement factor C3b + H2O
?
-
cleavage sites are RTL-D, NHK-L, LAR-S, and VEL-I
-
-
?
decorin + H2O
?
-
-
-
-
?
EndoS + H2O
?
-
cleavage site is VML-K
-
-
?
Fba + H2O
?
-
a cell surface factor H- and factor H-like protein 1-binding protein of epithelial human cells, the enzyme inhibits complement regulatory protein factor H- and factor H-like protein 1 binding by proteolysis of the Fba protein, overview
-
-
?
Fba protein + H2O
?
-
-
-
-
?
Fibrinogen + H2O
?
-
cleavage sites are C-terminally in Aalpha chains
-
-
?
Fibronectin + H2O
?
-
-
-
-
?
H-kininogen + H2O
?
-
cleavage sites are LMK-R and PFR-S
-
-
?
human CXCL10 + H2O
?
-
-
-
-
?
Human fibrinogen + H2O
?
-
release and processing, the enzyme abolishes the binding of Streptococcus pyogenes to full-length or 30 kDa fragment of human fibrinogen Fn, kinetics overview
-
-
?
immunoglobulin A + H2O
?
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin D + H2O
?
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin E + H2O
?
-
cleavage sites are the heavy chains
-
-
?
immunoglobulin G + H2O
?
-
cleavage site is LLG-G in gamma-chain
-
-
?
immunoglobulin M + H2O
?
-
cleavage sites are the heavy chains
-
-
?
Laminin + H2O
?
-
-
-
-
?
M protein + H2O
?
-
-
-
-
?
mouse CXCL-2 + H2O
?
-
the cleavage site is between lysine residues K65 and K66
-
-
?
plasminogen + H2O
?
-
-
-
-
?
pro-interleukin-1beta + H2O
interleukin-1beta + ?
-
cleavage site is YVH-D
-
-
?
protein H + H2O
?
-
-
-
-
?
SpeBz + H2O
mature SpeB + ?
-
auto-cleavage sites are AIK-A, KVN-L, QIK-E, TYA-G, and EIK-Q
-
-
?
streptococcal mitogenic exotoxin Z + H2O
?
-
-
-
-
?
streptokinase + H2O
?
-
-
-
-
?
streptolysin O + H2O
?
-
-
-
-
?
urokinase receptor + H2O
?
-
cleavage site is close to the GPI anchor
-
-
?
Vitronectin + H2O
?
-
-
-
-
?
additional information
?
-
human CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-2 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-2 + H2O
?
-
the cleavage site is between lysine residues K60 and K61
-
-
?
human CXCL-6 + H2O
?
-
-
-
-
?
human CXCL-6 + H2O
?
-
-
-
-
?
human CXCL-8 + H2O
?
-
-
-
-
?
human CXCL-8 + H2O
?
-
-
-
-
?
IgG + H2O
?
-
the ability to cleave off the Fc part of antigen-bound IgG contributes to the escape of group A streptococci from opsonophygocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding
-
?
IgG + H2O
?
-
the ability to cleave off the Fc part of antigen-bound IgG contributes to the escape of group A streptococci from opsonophygocytosis while not interfering with the formation of a host-like coat by unspecific IgG binding
-
?
mouse CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K65 and K66
-
-
?
mouse CXCL-1 + H2O
?
-
the cleavage site is between lysine residues K65 and K66
-
-
?
properdin + H2O
?
-
-
-
-
?
properdin + H2O
?
-
cleavage of properdin leads to inhibition of complement-mediated opsonophagocytosis and bacterial killing by neutrophils, alternative complement pathway overview
-
-
?
protein F1 + H2O
?
-
-
-
-
?
protein F1 + H2O
?
-
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1, e.g. in human pharyngeal epithelial cells Detroit 562, while proteins H and M1 are protected by plasma proteins, overview
-
-
?
additional information
?
-
-
the enzyme activates a 66000 Da matrix metalloprotease produced by human endothelial cells, a process that may contribute to endothelial cell damage, tissue destruction, and hemodynamic derangement
-
-
?
additional information
?
-
-
by removal of M1 protein and protein H from the streptococcal surface the enzyme regulates the bacterial cell-cell interactions, and perhaps also interactions with epithelial cells. Through expression of streptopain the enzyme can modify the composition of the surface proteins in response to environmental conditions. Such a mechanism will facilitate the adaption of the bacterium to its host
-
-
?
additional information
?
-
-
the enzyme can enhance the invasion ability of group A streptococci in human respiratory epithelial cells
-
-
?
additional information
?
-
-
the expression of the enzyme contributes to soft tissue pathology, including necrosis, and is required for efficient systemic dissemination of the organism from the initial site of skin inoculation
-
-
?
additional information
?
-
-
release of biological active kinins from kininogens present in human plasma
-
-
?
additional information
?
-
-
the enzyme is an important virulence factor
-
-
?
additional information
?
-
-
the enzyme is secreted under conditions of starvation and may be involved in nutrient acquisition
-
-
?
additional information
?
-
-
thus, although IgG might by a substrate for SpeB under certain environmental conditions, it seems unlikely that SpeB is part of the first line of defense against specific antibodies. Even though SpeB might not be directly involved in the attenuation of the adaptive immune response, its proteolytic activity towards streptococcal surface proteins, including IgG-binding proteins and the streptococcal C5a peptidase, could certainly be important for the modulation of the complement system
-
?
additional information
?
-
-
streptopain shows strepadhesin activity, independent of protease activity, mediated by a cell surface adhesin and controlled by the multiple gene regulator Mga
-
-
?
additional information
?
-
-
the enzyme can induce apoptosis in A549 cells, the induction of apoptosis in cells requires the protease activity and the propper enzyme size of 28 kDa, cell binding activity of processed and unprocessed wild-type and mutant enzymes, the induction can be prevented by inhibition of caspase-8, induction cascade, overview
-
-
?
additional information
?
-
-
the enzyme inactivates the metabolic activity of polymorphonuclear cells, the enzyme causes mitochondria damage to polymorphonuclear cells preventing phagocytosis of group A Streptococcus, it is essential for bacterial survival in blood, mechanism, overview
-
-
?
additional information
?
-
-
the enzyme is a virulence factor of Streptococcus pyogenes inducing the release of histamine in mast cells, basophils, and mononuclear cells, and increasing capillary permeability and histamine release in skin of guinea pigs, the recombinant enzyme shows mitogenic activity with human T-cells
-
-
?
additional information
?
-
-
CXCL9 is quite resistant to hydrolysis by SpeB
-
-
?
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
-
-
?
additional information
?
-
-
SpeB has no immunoglobulin-degrading activity in human plasma or blood
-
-
?
additional information
?
-
-
the enzyme can induce apoptosis in A549 cells, the induction of apoptosis in cells requires the protease activity and the propper enzyme size of 28 kDa, cell binding activity of processed and unprocessed wild-type and mutant enzymes, the induction can be prevented by inhibition of caspase-8, induction cascade, overview
-
-
?
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
-
-
?
additional information
?
-
-
incubation of mature SpeB in 20% (v/v) plasma for 24 h at 37°C does not cause degradation of the protein
-
-
?
additional information
?
-
-
the enzyme is not critical for the development of tissue necrosis, bacteremia and lethal infection in a murine model of human necrotizing fascilitis
-
-
?
additional information
?
-
-
critical virulence factor for invasive disease episode. Binds host cell integrins alphaVbeta3 and alphaIIbbeta3 through an RGD motif
-
-
?
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(S)-1-azido-2-tosylamino-hexane
-
moderate inhibitor of IdeS
(S)-1-azido-3-methyl-2-tosylamino-butane
-
moderate inhibitor of IdeS
(S)-1-azido-3-phenyl-2-tosylamino-propane
-
moderate inhibitor of IdeS
(S)-3-tosylamino-1-heptanal
-
strong inhibitory activity
(S)-3-tosylamino-heptane-1-nitrile
-
the compound shows some inhibition of IdeS
(S)-4-methyl-3-tosylamino-1-pentanal
-
strong inhibitory activity
(S)-4-phenyl-3-tosylamino-1-butanal
-
strong inhibitory activity
(S)-7-tert-butoxycarbonylamino-3-tosylamino-1-heptanal
-
strong inhibitory activity
1,3-Dibromoacetone
-
rapid and complete loss of activity
2,4-dinitrofluorobenzene
-
-
acetonitrile
-
mixed type
acetyl-Ala-Gln-Ile-(S)-2,6-diaminohexanal
-
-
benzyloxycarbonyl-Ala-Ala-CHN2
-
-
benzyloxycarbonyl-Ala-Ala-Pro-CHN2
-
-
benzyloxycarbonyl-Ala-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Asn-Val-Gly-CHN2
-
inhibition of protease activity, no influence on the superantigenic properties of the enzyme
Benzyloxycarbonyl-Gly-Phe
-
competitive against benzyloxycarbonyl-Phe-Tyr
benzyloxycarbonyl-Leu-Val-Gly-CHN2
-
inhibits kininogen degradation
Benzyloxycarbonyl-Phe-Ala-CHN2
-
-
benzyloxycarbonyl-Phe-Gly-CHN2
-
-
benzyloxycarbonyl-Phe-Gly-Phe-CHN2
-
-
Cu2+
-
Cu2+ inhibits the proteolytic activity of mature SpeB
dimethyl sulfoxide
-
competitive
E64
-
i.e. trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
iodoacetate
-
irreversible inhibitor
L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane
-
-
N-(N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl)-agmatine
-
-
N-[N-(L-3-transcarboxyirane-2-carbonyl)-L-leucyl]agmatine
-
Nalpha-benzyloxycarbonyl-Phe-Phe
-
strong inhibition of hydrolysis of Nalpha-benzyloxycarbonyl-Phe-Tyr
Spe B pro-peptide
-
specific inhibition of the mature enzyme, secondary structure and SpeB binding analysis, inhibition modeling and mechanism, overview
-
Spi
-
specific enzyme pro-peptide analogue inhibitor, purification from Streptococcus pyogenes, secondary structure and SpeB binding analysis, inhibition modeling and mechanism, overview
-
tosyl-L-lysine chloromethyl ketone
-
irreversible inhibitor
tosyl-L-phenylalanine chloromethyl ketone
-
irreversible inhibitor
Tosyl-norleucine-Phe
-
competitive against benzyloxycarbonyl-norleucine-Phe
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane
-
-
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
Z-LVG-CHN2
-
irreversible inhibitor
Zn2+
-
Zinc inhibits the proteolytic activity of mature SpeB
E-64
-
0.028 mM
E-64
-
i.e. L-trans-epoxysuccinyl-leucylamido(4-guanidino)butane, irreversible inhibition
HgCl2
-
prevents the conversion to the mature 28 kDa form
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64, inhibits the capillary permeability increasing effect of the enzyme
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64, complete inhibition at 0.016 mM
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
i.e. E64
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane
-
-
additional information
-
IdeS is not inhibited by E-64, (S)-3-phenyl-2-tosylamino-1-propanol, (S)-2-tosylamino-1-hexanol, (S)-3-methyl-2-tosylamino-1-butanol, (S)-6-tert-butoxycarbonylamino-2-tosylamino-1-hexanol, (S)-6-amino-2-tosylamino-1-hexanol trifluoroacetic acid, (S)-3-phenyl-2-tosylamino-propyl-1-toluenesulfonate, (S)-2-tosylamino-hexyl-1-toluenesulfonate, (S)-3-methyl-2-tosylamino-butyl-1-toluenesulfonate, and (S)-6-tert-butoxycarbonylamino-2-tosylamino-hexyl-1-toluenesulfonate
-
additional information
-
antibodies produced against the r28-kDa truncated form of the C192 mutant enzyme effectively inhibit digestion of casein or fibrinogen by cysteine protease wheras antibodies generated against the r40-kDA form of the mutant have no significant effect on proteolysis
-
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Anti-Glomerular Basement Membrane Disease
The IgG-degrading enzyme of Streptococcus pyogenes causes rapid clearance of anti-glomerular basement membrane antibodies in patients with refractory anti-glomerular basement membrane disease.
Arthritis
Blocking of experimental arthritis by cleavage of IgG antibodies in vivo.
Arthritis, Infectious
Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes.
Bacteremia
Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes.
Bacteremia
Histopathologic changes in kidney and liver correlate with streptococcal pyrogenic exotoxin B production in the mouse model of group A streptococcal infection.
Cellulitis
Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes.
Exanthema
The production of pyrogenic exotoxins by group A streptococci.
Fasciitis, Necrotizing
Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: an integrin-binding cysteine protease.
Fasciitis, Necrotizing
Diagnosis of group A streptococcal necrotizing fasciitis by using PCR to amplify the streptococcal pyrogenic exotoxin B gene.
Foodborne Diseases
Time course of virulence factors produced by group A streptococcus during a food-borne epidemic.
Glomerulonephritis
Acute poststreptococcal glomerulonephritis with acute interstitial nephritis related to streptococcal pyrogenic exotoxin B.
Glomerulonephritis
Bacterial infection-related glomerulonephritis in adults.
Glomerulonephritis
Immunohistochemical and serological evidence for the role of streptococcal proteinase in acute post-streptococcal glomerulonephritis.
Glomerulonephritis
Is the nephritogenic antigen in post-streptococcal glomerulonephritis pyrogenic exotoxin B (SPE B) or GAPDH?
Glomerulonephritis
Role of streptococcal proteinase in acute post-streptococcal glomerulonephritis.
Glomerulonephritis
Streptococcal pyrogenic exotoxin B antibodies in a mouse model of glomerulonephritis.
Infections
An amino-terminal signal peptide of Vfr protein negatively influences RopB-dependent SpeB expression and attenuates virulence in Streptococcus pyogenes.
Infections
Antibody to streptococcal cysteine proteinase as a seromarker of group A Streptococcal (Streptococcus pyogenes) infections.
Infections
Application of the c3-binding motif of streptococcal pyrogenic exotoxin B to protect mice from invasive group a streptococcal infection.
Infections
Clinical and microbiological characteristics of severe group A streptococcus infections and streptococcal toxic shock syndrome.
Infections
Degradation of complement 3 by streptococcal pyrogenic exotoxin B inhibits complement activation and neutrophil opsonophagocytosis.
Infections
Determining antibody-binding site of streptococcal pyrogenic exotoxin B to protect mice from group a streptococcus infection.
Infections
Histopathologic changes in kidney and liver correlate with streptococcal pyrogenic exotoxin B production in the mouse model of group A streptococcal infection.
Infections
Leaderless secreted peptide signaling molecule alters global gene expression and increases virulence of a human bacterial pathogen.
Infections
Metal-mediated modulation of streptococcal cysteine protease activity and its biological implications.
Infections
Molecular analysis of the role of the group A streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection.
Infections
Streptococcal mitogenic exotoxin, SmeZ, is the most susceptible M1T1 streptococcal superantigen to degradation by the streptococcal cysteine protease, SpeB.
Infections
Streptococcal pyrogenic exotoxin B cleaves properdin and inhibits complement-mediated opsonophagocytosis.
Infections
Streptococcal pyrogenic exotoxin B inhibits apoptotic cell clearance by macrophages through protein S cleavage.
Infections
Structure of the mature streptococcal cysteine protease exotoxin mSpeB in its active dimeric form.
Infections
Substrate specificity of the streptococcal cysteine protease.
Infections
Synergistic effects of streptolysin S and streptococcal pyrogenic exotoxin B on the mouse model of group A streptococcal infection.
Lung Injury
Streptococcal cysteine protease augments lung injury induced by products of group A streptococci.
Melanoma
Cleavage of interleukin 1 beta (IL-1 beta) precursor to produce active IL-1 beta by a conserved extracellular cysteine protease from Streptococcus pyogenes.
Nephritis, Interstitial
A possible rare cause of renal failure in streptococcal infection.
Nephritis, Interstitial
Acute poststreptococcal glomerulonephritis with acute interstitial nephritis related to streptococcal pyrogenic exotoxin B.
Pharyngitis
Detection of invasive protein profile of Streptococcus pyogenes M1 isolates from pharyngitis patients.
Pharyngitis
The production of pyrogenic exotoxins by group A streptococci.
Pneumonia
Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes.
Shock, Septic
Cysteine protease activity and histamine release from the human mast cell line HMC-1 stimulated by recombinant streptococcal pyrogenic exotoxin B/streptococcal cysteine protease.
Shock, Septic
Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes.
Shock, Septic
Molecular structure of staphylococcus and streptococcus superantigens.
Shock, Septic
Nucleotide sequence of the streptococcal pyrogenic exotoxin type B gene and relationship between the toxin and the streptococcal proteinase precursor.
Shock, Septic
The potential role of bacterial superantigens in the pathogenesis of Kawasaki syndrome.
Starvation
Life in protein-rich environments: the relA-independent response of Streptococcus pyogenes to amino acid starvation.
Starvation
Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion.
Streptococcal Infections
Abrogation of streptococcal pyrogenic exotoxin B-mediated suppression of phagocytosis in U937 cells by Cordyceps sinensis mycelium via production of cytokines.
Streptococcal Infections
Application of the c3-binding motif of streptococcal pyrogenic exotoxin B to protect mice from invasive group a streptococcal infection.
Streptococcal Infections
Cysteine protease activity and histamine release from the human mast cell line HMC-1 stimulated by recombinant streptococcal pyrogenic exotoxin B/streptococcal cysteine protease.
Streptococcal Infections
Histopathologic changes in kidney and liver correlate with streptococcal pyrogenic exotoxin B production in the mouse model of group A streptococcal infection.
Streptococcal Infections
Identification and characterization of bicistronic speB and prsA gene expression in the group A Streptococcus.
Streptococcal Infections
Inverse relation between disease severity and expression of the streptococcal cysteine protease, SpeB, among clonal M1T1 isolates recovered from invasive group A streptococcal infection cases.
Streptococcal Infections
Role of streptococcal pyrogenic exotoxin B in the mouse model of group A streptococcal infection.
Streptococcal Infections
Studies of recombinant streptococcal pyrogenic exotoxin B/cysteine protease (rSPE B/SCP) in the skin of guinea pigs & the release of histamine from cultured mast cells & basophilic leukocytes.
Streptococcal Infections
Synergistic effects of streptolysin S and streptococcal pyrogenic exotoxin B on the mouse model of group A streptococcal infection.
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Liu, T.Y.; Elliott, S.D.
Streptococcal proteinase
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
609-647
1971
Streptococcus sp.
-
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Molecular analysis of the role of the group A streptococcal cysteine protease, hyaluronic acid capsule, and M protein in a murine model of human invasive soft-tissue infection
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1998
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Autocatalytic processing of the streptococcal cysteine protease zymogen: processing mechanism and characterization of the autoproteolytic cleavage sites
Eur. J. Biochem.
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1999
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brenda
Green, G.D.J.; Shaw, E.
Peptidyl diazomethyl ketones are specific inactivators of thiol proteinases
J. Biol. Chem.
256
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1981
Streptococcus sp.
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Kortt, A.A.; Wysocki, J.R.; Liu, T.Y.
Primary structure of streptococcal proteinase. I Isolation, composition, and amino acid sequences of the tryptic and chymotryptic peptides of cyanogen bromide fragments 1 to 4
J. Biol. Chem.
251
1941-1947
1976
Streptococcus sp.
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Berge, A.; Bjrck, L.
Streptococcal cysteine proteinase releases biologically active fragments of streptococcal surface proteins
J. Biol. Chem.
270
9862-9867
1995
Streptococcus pyogenes
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Tai, J.Y.; Kortt, A.A.; Liu, T.Y.; Elliott, S.D.
Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: complete covalent structure of the polypeptide chain
J. Biol. Chem.
251
1955-1959
1976
Streptococcus sp.
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Kortt, A.A.; Liu, T.Y.
On the mechanism of action of streptococcal proteinase. I. Active-site titration
Biochemistry
12
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1973
Streptococcus sp.
brenda
Kortt, A.A.; Liu, T.Y.
On the mechanism of action of streptococcal proteinase. II. Comparison of the kinetics of proteinase- and papain-catalyzed hydrolysis of N-acylamino acid esters
Biochemistry
12
328-337
1973
Streptococcus sp.
brenda
Kortt, A.A.; Liu, T.Y.
On the mechanism of action of streptococcal proteinase. 3. The effect of pH, organic solvents, and deuterium oxide on the proteinase-catalyzed hydrolysis of N-acylamino acid esters
Biochemistry
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1973
Streptococcus sp.
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Elliott, S.D.; Liu, T.Y.
Streptococcal proteinase
Methods Enzymol.
19
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1970
Streptococcus sp.
-
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Stockbauer, K.E.; Magoun, L.; Liu, M.; Burns, E.H.; Gubba, S.; Renish, S.; Pan, X.; Bodary, S.C.; Baker, E.; Coburn, J.; Leong, J.M.; Musser, J.M.
A natural variant of the cysteine protease virulence factor of group A Streptococcus with an arginine-glycine-aspartic acid (RGD) motif preferentially binds human integrins alphavbeta3 and alphaIIbbeta3
Proc. Natl. Acad. Sci. USA
96
242-247
1999
Streptococcus sp.
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Burns, E.H.; Marciel, A.; Musser, J.M.
Structure-function and pathogenesis studies of Streptococcus pyogenes extracellular cysteine protease
Adv. Exp. Med. Biol.
418
589-592
1997
Streptococcus pyogenes
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Liu, T.Y.; Elliott, S.D.
Streptococcal proteinase: the zymogen to enzyme transformation
J. Biol. Chem.
240
1138-1142
1965
Streptococcus pyogenes
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Gerwin, B.I.; Stein, W.H.; Moore, S.
On the specificity of streptococcal proteinase
J. Biol. Chem.
241
3331-3339
1966
Streptococcus sp.
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Burns, E.H.; Marciel, A.M.; Musser, J.M.
Activation of a 66-kilodalton human endothelial cell matrix metalloprotease by Streptococcus pyogenes extracellular cysteine protease
Infect. Immun.
64
4744-4750
1996
Streptococcus pyogenes
brenda
Herwald, H.; Collin, M.; Muller-Esterl, W.; Bjrck, L.
Streptococcal cysteine proteinase releases kinins: a virulence mechanism
J. Exp. Med.
184
665-673
1996
Streptococcus pyogenes
brenda
Chaussee, M.S.; Phillips, E.R.; Ferretti, J.J.
Temporal production of streptococcal erythrogenic toxin B (streptococcal cysteine proteinase) in response to nutrient depletion
Infect. Immun.
65
1956-1959
1997
Streptococcus pyogenes
brenda
Tsai, P.J.; Kuo, C.F.; Lin, K.Y.; Lin, Y.; Lei, H.Y.; Chen, F.F.; Wang, J.R.; Wu, J.J.
Effect of group A streptococcal cysteine protease on invasion of epithelial cells
Infect. Immun.
66
1460-1466
1998
Streptococcus pyogenes
brenda
Matsuka, Y.V.; Pillai, S.; Gubba, S.; Musser, J.M.; Olmstedt, S.B.
Fibrinogen cleavage by the Streptococcus pyogenes extracellular cysteine protease and generation of antibodies that inhibit enzyme proteolytic activity
Infect. Immun.
67
4326-4333
1999
Streptococcus pyogenes
brenda
Lukomski, S.; Montgomery, C.A.; Rurangirwa, J.; Geske, R.S.; Barrish, J.P.; Adams, G.J.; Musser, J.M.
Extracellular cysteine protease produced by Streptococcus pyogenes participates in the pathogenesis of invasive skin infection and dissemination in mice
Infect. Immun.
67
1779-1788
1999
Streptococcus pyogenes
brenda
Eriksson, A.; Norgren, M.
The superantigenic activity of streptococcal pyrogenic exotoxin B is independent of the protease activity
FEMS Immunol. Med. Microbiol.
25
355-363
1999
Streptococcus sp., Streptococcus sp. T10BW
brenda
von Pawel-Rammingen, U.; Johansson, B.P.; Bjorck, L.
IdeS, a novel streptococcal cysteine proteinase with unique specificity for immunoglobulin G
EMBO J.
21
1607-1615
2002
Streptococcus pyogenes
brenda
Eriksson, A.; Norgren, M.
Cleavage of antigen-bound immunoglobulin G by SpeB contributes to streptococcal persistence in opsonizing blood
Infect. Immun.
71
211-217
2003
Streptococcus sp., Streptococcus sp. T1BRB
brenda
Kagawa, T.F.; Cooney, J.C.; Baker, H.M.; McSweeney, S.; Liu, M.; Gubba, S.; Musser, J.M.; Baker, E.N.
Crystal structure of the zymogen form of the group A Streptococcus virulence factor SpeB: an integrin-binding cysteine protease
Proc. Natl. Acad. Sci. USA
97
2235-2240
2000
Streptococcus pyogenes (P0C0J0), Streptococcus pyogenes
brenda
Anderson, E.T.; Winter, L.A.; Fernsten, P.; Olmsted, S.B.; Matsuka, Y.V.
The pro-sequence domain of streptopain directs the folding of the mature enzyme
Arch. Biochem. Biophys.
436
297-306
2005
Streptococcus pyogenes
brenda
Tsao, N.; Tsai, W.H.; Lin, Y.S.; Chuang, W.J.; Wang, C.H.; Kuo, C.F.
Streptococcal pyrogenic exotoxin B cleaves properdin and inhibits complement-mediated opsonophagocytosis
Biochem. Biophys. Res. Commun.
339
779-784
2006
Streptococcus pyogenes
brenda
Watts, A.B.; Brocklehurst, K.
Streptopain
Handbook of Proteolytic Enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. )Academic Press
2
1245-1249
2004
Streptococcus pyogenes
-
brenda
Ohkuni, H.; Todome, Y.; Watanabe, Y.; Ishikaw, T.; Takahashi, H.; Kannari, Y.; Kato, H.; Uchiyama, T.; Saito, H.; Fischetti, V.A.; Zabriskie, J.B.
Studies of recombinant streptococcal pyrogenic exotoxin B/cysteine protease (rSPE B/SCP) in the skin of guinea pigs & the release of histamine from cultured mast cells & basophilic leukocytes
Indian J. Med. Res.
119 Suppl
33-36
2004
Streptococcus pyogenes
brenda
Tsai, W.H.; Chang, C.W.; Chuang, W.J.; Lin, Y.S.; Wu, J.J.; Liu, C.C.; Chang, W.T.; Lin, M.T.
Streptococcal pyrogenic exotoxin B-induced apoptosis in a549 cells is mediated by a receptor- and mitochondrion-dependent pathway
Infect. Immun.
72
7055-7062
2004
Streptococcus pyogenes, Streptococcus pyogenes A-20
brenda
Wei, L.; Pandiripally, V.; Gregory, E.; Clymer, M.; Cue, D.
Impact of the SpeB protease on binding of the complement regulatory proteins factor H and factor H-like protein 1 by Streptococcus pyogenes
Infect. Immun.
73
2040-2050
2005
Streptococcus pyogenes
brenda
Chiang-Ni, C.; Wang, C.H.; Tsai, P.J.; Chuang, W.J.; Lin, Y.S.; Lin, M.T.; Liu, C.C.; Wu, J.J.
Streptococcal pyrogenic exotoxin B causes mitochondria damage to polymorphonuclear cells preventing phagocytosis of group A streptococcus
Med. Microbiol. Immunol.
195
55-63
2006
Streptococcus pyogenes
brenda
Nyberg, P.; Rasmussen, M.; Von Pawel-Rammingen, U.; Bjoerck, L.
SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1
Microbiology
150
1559-1569
2004
Streptococcus pyogenes
brenda
Kagawa, T.F.; Otoole, P.W.; Cooney, J.C.
SpeB-Spi: a novel protease-inhibitor pair from Streptococcus pyogenes
Mol. Microbiol.
57
650-666
2005
Streptococcus pyogenes, Streptococcus pyogenes B220
brenda
Kuo, C.F.; Chen, C.C.; Lin, C.F.; Jan, M.S.; Huang, R.Y.; Luo, Y.H.; Chuang, W.J.; Sheu, C.C.; Lin, Y.S.
Abrogation of streptococcal pyrogenic exotoxin B-mediated suppression of phagocytosis in U937 cells by Cordyceps sinensis mycelium via production of cytokines
Food Chem. Toxicol.
45
278-285
2007
Streptococcus pyogenes
brenda
Kuo, C.F.; Lin, Y.S.; Chuang, W.J.; Wu, J.J.; Tsao, N.
Degradation of complement 3 by streptococcal pyrogenic exotoxin B inhibits complement activation and neutrophil opsonophagocytosis
Infect. Immun.
76
1163-1169
2008
Streptococcus pyogenes
brenda
Tsai, W.H.; Chang, C.W.; Lin, Y.S.; Chuang, W.J.; Wu, J.J.; Liu, C.C.; Tsai, P.J.; Lin, M.T.
Streptococcal pyrogenic exotoxin B-induced apoptosis in A549 cells is mediated through alpha(v)beta(3) integrin and Fas
Infect. Immun.
76
1349-1357
2008
Streptococcus pyogenes
brenda
Nooh, M.M.; Aziz, R.K.; Kotb, M.; Eroshkin, A.; Chuang, W.J.; Proft, T.; Kansal, R.
Streptococcal mitogenic exotoxin, SmeZ, is the most susceptible M1T1 streptococcal superantigen to degradation by the streptococcal cysteine protease, SpeB
J. Biol. Chem.
281
35281-35288
2006
Streptococcus pyogenes
brenda
Luo, Y.H.; Kuo, C.F.; Huang, K.J.; Wu, J.J.; Lei, H.Y.; Lin, M.T.; Chuang, W.J.; Liu, C.C.; Lin, C.F.; Lin, Y.S.
Streptococcal pyrogenic exotoxin B antibodies in a mouse model of glomerulonephritis
Kidney Int.
72
716-724
2007
Streptococcus pyogenes (P0C0J0)
brenda
Cole, J.N.; Aquilina, J.A.; Hains, P.G.; Henningham, A.; Sriprakash, K.S.; Caparon, M.G.; Nizet, V.; Kotb, M.; Cordwell, S.J.; Djordjevic, S.P.; Walker, M.J.
Role of group A Streptococcus HtrA in the maturation of SpeB protease
Proteomics
7
4488-4498
2007
Streptococcus pyogenes M1 GAS (P0C0J1), Streptococcus pyogenes M1 GAS HSC5 (P0C0J1)
brenda
Wang, C.C.; Houng, H.C.; Chen, C.L.; Wang, P.J.; Kuo, C.F.; Lin, Y.S.; Wu, J.J.; Lin, M.T.; Liu, C.C.; Huang, W.; Chuang, W.J.
Solution structure and backbone dynamics of Streptopain
J. Biol. Chem.
284
10957-10967
2009
Streptococcus pyogenes
brenda
Soederberg, J.J.; von Pawel-Rammingen, U.
The streptococcal protease IdeS modulates bacterial IgGFc binding and generates 1/2Fc fragments with the ability to prime polymorphonuclear leucocytes
Mol. Immunol.
45
3347-3353
2008
Streptococcus pyogenes
brenda
Berggren, K.; Johansson, B.; Fex, T.; Kihlberg, J.; Bjoerck, L.; Luthman, K.
Synthesis and biological evaluation of reversible inhibitors of IdeS, a bacterial cysteine protease and virulence determinant
Bioorg. Med. Chem.
17
3463-3470
2009
Streptococcus pyogenes
brenda
Meinert Niclasen, L.; Olsen, J.G.; Dagil, R.; Qing, Z.; Sorensen, O.E.; Kragelund, B.B.
Streptococcal pyogenic exotoxin B (SpeB) boosts the contact system via binding of alpha-1 antitrypsin
Biochem. J.
434
123-132
2011
Streptococcus pyogenes, Streptococcus pyogenes Alab49, Streptococcus pyogenes AP1
brenda
Nelson, D.C.; Garbe, J.; Collin, M.
Cysteine proteinase SpeB from Streptococcus pyogenes - a potent modifier of immunologically important host and bacterial proteins
Biol. Chem.
392
1077-1088
2011
Streptococcus pyogenes
brenda
Kurupati, P.; Turner, C.E.; Tziona, I.; Lawrenson, R.A.; Alam, F.M.; Nohadani, M.; Stamp, G.W.; Zinkernagel, A.S.; Nizet, V.; Edwards, R.J.; Sriskandan, S.
Chemokine-cleaving Streptococcus pyogenes protease SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues and the respiratory tract
Mol. Microbiol.
76
1387-1397
2010
Streptococcus pyogenes, Streptococcus pyogenes H292
brenda
Connolly, K.L.; Braden, A.K.; Holder, R.C.; Reid, S.D.
Srv mediated dispersal of streptococcal biofilms through SpeB is observed in CovRS+ strains
PLoS ONE
6
e28640
2011
Streptococcus sp., Streptococcus sp. RGAS053, Streptococcus sp. MGAS315
brenda
Persson, H.; Vindebro, R.; von Pawel-Rammingen, U.
The streptococcal cysteine protease SpeB is not a natural immunoglobulin-cleaving enzyme
Infect. Immun.
81
2236-2241
2013
Streptococcus pyogenes
brenda
Chella Krishnan, K.; Mukundan, S.; Landero Figueroa, J.A.; Caruso, J.A.; Kotb, M.
Metal-mediated modulation of streptococcal cysteine protease activity and its biological implications
Infect. Immun.
82
2992-3001
2014
Streptococcus pyogenes
brenda
Gonzalez-Paez, G.E.; Wolan, D.W.
Ultrahigh and high resolution structures and mutational analysis of monomeric Streptococcus pyogenes SpeB reveal a functional role for the glycine-rich C-terminal loop
J. Biol. Chem.
287
24412-24426
2012
Streptococcus pyogenes, Streptococcus pyogenes ATCC 10782
brenda
Sumitomo, T.; Nakata, M.; Higashino, M.; Terao, Y.; Kawabata, S.
Group A streptococcal cysteine protease cleaves epithelial junctions and contributes to bacterial translocation
J. Biol. Chem.
288
13317-13324
2013
Streptococcus pyogenes
brenda
Brouwer, S.; Cork, A.J.; Ong, C.Y.; Barnett, T.C.; West, N.P.; McIver, K.S.; Walker, M.J.
Endopeptidase PepO regulates the SpeB cysteine protease and is essential for the virulence of invasive M1T1 Streptococcus pyogenes
J. Bacteriol.
200
e00654-17
2018
Streptococcus pyogenes (P0C0J0), Streptococcus pyogenes 5448 (P0C0J0)
brenda
Lane, M.D.; Seelig, B.
Highly efficient recombinant production and purification of streptococcal cysteine protease streptopain with increased enzymatic activity
Protein Expr. Purif.
121
66-72
2016
Streptococcus pyogenes (P0C0J0), Streptococcus pyogenes
brenda