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alpha2-macroglobulin + H2O
?
-
processing of the inhibitor, the initial N-terminal hydrolysis of alpha2-macroglobulin by aureolysin does not affect the serpin inhibitory activity, cleavage within its exposed reactive loop is associated with a decreased inhibitory activity, down to 23% of the control inhibitor
-
-
?
Bap + H2O
?
-
a surface-anchored protein
-
-
?
casein + H2O
hydrolyzed casein
cathelicidin LL-37 + H2O
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
Gelatin + H2O
?
-
-
-
-
?
GWTLNSAGYLLGPHAIDNHRSFHDKYGLA-NH2 + H2O
Gly-Trp-Thr + Leu-Asn-Ser + Ala-Gly + Tyr + Leu + LGPHAIDNHRS + FHDKYG + Leu-Ala-NH2
-
i.e. galanin
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
Nalpha-furylacryloyl-Gly-Ala-NH2 + H2O
?
-
very poor substrate
-
-
?
Nalpha-Furylacryloyl-Gly-Leu amide + H2O
?
-
-
-
-
?
Nalpha-furylacryloyl-Gly-Leu-NH2
?
-
Nalpha-furylacryloyl-Gly-Phe-NH2 is a better substrate than Fa-Gly-Leu-NH2
-
-
?
Nalpha-furylacryloyl-Gly-Phe-NH2
?
-
Nalpha-furylacryloyl-Gly-Phe-NH2 is a better substrate than Fa-Gly-Leu-NH2
-
-
?
Nalpha-furylacryloyl-Gly-Val-NH2 + H2O
?
-
very poor substrate
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
plasminogen + H2O
angiostatin + mini-plasminogen
-
-
-
-
?
plasminogen activator inhibitor-1 + H2O
?
-
processing of the inhibitor, the proteolytic degradation of PAI-1 by aureolysin is associated with a drastic decrease in its capacity to inhibit uPA, down to 7% of the inhibitory activity of the control PAI-1
-
-
?
pro-urokinase-type plasmin activator + H2O
2 chains of urokinase-type plasmin activator
-
human substrate, activation by cleavage into two enzyme chains, activity by wild-type strains 8325-4 and Newman, and clinical isolates, overview, no activity with N-terminal enzyme substrate mutants, overview
-
-
?
additional information
?
-
alpha-toxin + H2O
?
-
-
-
-
?
alpha-toxin + H2O
?
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
casein + H2O
hydrolyzed casein
-
-
-
-
?
cathelicidin LL-37 + H2O
?
-
human antimicrobial peptide. Enzyme production by Staphylococcus aureus contributes to its resistance to the innate immune system of humans mediated by LL-37
-
-
?
cathelicidin LL-37 + H2O
?
-
human antimicrobial peptide, cleavage by enzyme at R19-I20, R23-I24, L31-V32
-
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b
both products are active
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Hemoglobin + H2O
Hydrolyzed hemoglobin
-
-
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
-
hydrolysis of bonds in which the NH2-group of hydrophobic amino acids is involved, no hydrolysis of Phe24-Phe25
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
-
cleaves at His5-Leu6, His10-Leu11, Ala14-Leu15, Tyr16-Leu17, Gly23-Phe24, Phe25-Tyr26
-
-
?
Oxidized insulin B-chain + H2O
Hydrolyzed oxidized insulin
-
hydrolysis of bonds in which the NH2-group of hydrophobic amino acids is involved, no hydrolysis of Phe24-Phe25
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
SspA zymogen + H2O
?
-
SspA is a serine protease secreted by Staphylococcus aureus as inactive zymogen, aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
SspA zymogen + H2O
?
-
SspA is a serine protease secreted by Staphylococcus aureus as inactive zymogen, aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65
-
-
?
additional information
?
-
-
specificity for peptide bonds on the N-terminal side of large hydrophobic residues
-
-
?
additional information
?
-
-
protease II exhibits esterase activity, using N-benzoyl-L-Tyr ethyl ester as substrate, no activity of protease I
-
-
?
additional information
?
-
-
activates the precursor of another protease secreted by the same organism, staphylococcal protease
-
-
?
additional information
?
-
-
the aur null mutant strain causes the same immune reaction in mice as the wild-type strain, overview
-
-
?
additional information
?
-
-
aureolysin does not hydrolyze GKHKNKGKKNGKHNGWK and HKHGHGHGKHKNKGKKN
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
additional information
?
-
-
pulmonary surfactant protein-A from human host lung is no substrate for aureolysin from Staphylococcus aureus, but for staphylopain A, EC 3.4.22.48
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
additional information
?
-
-
protease II exhibits esterase activity, using N-benzoyl-L-Tyr ethyl ester as substrate, no activity of protease I
-
-
?
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Bap + H2O
?
-
a surface-anchored protein
-
-
?
cathelicidin LL-37 + H2O
?
-
human antimicrobial peptide. Enzyme production by Staphylococcus aureus contributes to its resistance to the innate immune system of humans mediated by LL-37
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
additional information
?
-
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
complement component C3 + H2O
C3a+SN + C3b2SN
-
aureolysin cleaves purified C3 specifically in the alpha-chain, close to the C3 convertase cleavage site, yielding active C3a and C3b. In serum, the aureolysin-generated C3b is further degraded by host factors
both products are active
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
Galectin-3 + H2O
?
the enzyme has galectin-3-processing capacity. It cleaves human galectin-3 (a beta-galactoside-binding lectin involved in immune regulation and antimicrobial defense) into mostly higher-molecular-mass fragments, suggesting that it primarily digested the more distant parts of the N-terminal collagen-like domain
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
SspA zymogen + H2O
?
-
aureolysin is essential for activation of SspA zymogen, but the first step in processing of the N-terminal propeptide requires autocatalytic intramolecular cleavage at glutamine, aureolysin then processes at Leu58 and then Val69 to produce the first active molecules of mature SspA, which then feed back to promote efficient autocatalytic intermolecular processing of remaining zSspA at Glu65, mechanism, overview
-
-
?
additional information
?
-
-
activates the precursor of another protease secreted by the same organism, staphylococcal protease
-
-
?
additional information
?
-
-
the aur null mutant strain causes the same immune reaction in mice as the wild-type strain, overview
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
additional information
?
-
-
Aureolysin collaborates with host factors to inactivate C3b
-
-
?
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malfunction
-
the sigB mutant strain overexpresses the surface-anchored protein Bap, that is essential for biofilm formation in the model strain. Staphylococcus aureus completely inhibits the biofilm formation of the mutant strain via Aur and SspA, two proteases that are overexpressed in the sigB mutant strain and are capable of degrading Bap
metabolism
-
four major extracellular proteases of Staphylococcus aureus are potent complement inhibitors: cysteine proteases staphopain A and staphopain B, the serine protease V8, and the metalloproteinase aureolysin cause a drastic decrease in the haemolytic activity of serum, whereas two serine-protease like enzymes, SplD and SplE, have no effect. The four enzymes inhibit all pathways of complement due to the efficient degradation of several crucial components
metabolism
-
four major extracellular proteases of Staphylococcus aureus are potent complement inhibitors: cysteine proteases staphopain A and staphopain B, the serine protease V8, and the metalloproteinase aureolysin cause a drastic decrease in the haemolytic activity of serum, whereas two serine-protease like enzymes, SplD and SplE, have no effect. The four enzymes inhibit all pathways of complement due to the efficient degradation of several crucial components
-
physiological function
-
extracellular proteases Aur and SspA inhibit protein-dependent biofilm formation by Staphylococcus aureus, detailed overview
physiological function
-
Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion and is a potent complement inhibitor dependent on its proteolytic activity. Aureolysin effectively inhibits phagocytosis and killing of bacteria by neutrophils in the human host, e.g. in U937 cells, aureolysin inhibits C3b deposition and C5a generation, overview. Aureolysin is essential and sufficient for C3 cleavage by bacterial supernatant, but acts in synergy with host regulators to inactivate C3 thereby effectively dampening the host immune response. Aureolysin acts as a C3 convertase
physiological function
-
the enzyme acts as host complement inhibitor
physiological function
-
the enzyme interacts with the host tissue components in vitro to modulate host defense mechanisms and likely increase bacterial survival, but is not involved in the breakdown of first line of innate immune defense agent, pulmonary surfactant protein-A, of human host lung cells
physiological function
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
physiological function
the enzyme is probably associated with efficient processing of the PROM protease (homolog of V8/SspA serine protease). Additionally, AurWM appeares to affect biofilm formation in an uncertain suppressive way
physiological function
-
Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion and is a potent complement inhibitor dependent on its proteolytic activity. Aureolysin effectively inhibits phagocytosis and killing of bacteria by neutrophils in the human host, e.g. in U937 cells, aureolysin inhibits C3b deposition and C5a generation, overview. Aureolysin is essential and sufficient for C3 cleavage by bacterial supernatant, but acts in synergy with host regulators to inactivate C3 thereby effectively dampening the host immune response. Aureolysin acts as a C3 convertase
-
physiological function
-
the enzyme is probably associated with efficient processing of the PROM protease (homolog of V8/SspA serine protease). Additionally, AurWM appeares to affect biofilm formation in an uncertain suppressive way
-
physiological function
-
the enzyme acts as host complement inhibitor
-
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Arvidson, S.; Holme, T.; Lindholm, B.
Studies on extracellular proteolytic enzymes from Staphylococcus aureus. I. Purification and characterization of one neutral and one alkaline protease
Biochim. Biophys. Acta
302
135-148
1973
Staphylococcus aureus, Staphylococcus aureus V8
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Drapeau, G.R.
Role of metalloprotease in activation of the precursor of staphylococcal protease
J. Bacteriol.
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607-613
1978
Staphylococcus aureus
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Potempa, J.; Porwit-Bobr, Z.; Travis, J.
Stabilization vs. degradation of Staphylococcus aureus metalloproteinase
Biochim. Biophys. Acta
993
301-304
1989
Staphylococcus aureus
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Saheb, S.A.
Purification and properties of a metalloprotease from Staphylococcus aureus
Biochimie
60
429-435
1978
Staphylococcus aureus, Staphylococcus aureus A152
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Banbula, A.; Potempa, J.; Travis, J.; Fernandez-Catalan, C.; Mann, K.; Huber, R.; Bode, W.; Medrano, F.
Amino-acid sequence and three-dimensional structure of the Staphylococcus aureus metalloproteinase at 1.72 A resolution
Structure
6
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1998
Staphylococcus aureus, Staphylococcus aureus V8-BC 10
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Sieprawska-Lupa, M.; Mydel, P.; Krawczyk, K.; Wojcik, K.; Puklo, M.; Lupa, B.; Suder, P.; Silberring, J.; Reed, M.; Pohl, J.; Shafer, W.; McAleese, F.; Foster, T.; Travis, J.; Potempa, J.
Degradation of human antimicrobial peptide LL-37 by Staphylococcus aureus-derived proteinases
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48
4673-4679
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Staphylococcus aureus
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Calander, A.M.; Jonsson, I.M.; Kanth, A.; Arvidsson, S.; Shaw, L.; Foster, S.J.; Tarkowski, A.
Impact of staphylococcal protease expression on the outcome of infectious arthritis
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6
202-206
2004
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
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Beaufort, N.; Wojciechowski, P.; Sommerhoff, C.P.; Szmyd, G.; Dubin, G.; Eick, S.; Kellermann, J.; Schmitt, M.; Potempa, J.; Magdolen, V.
The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin
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410
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Staphylococcus aureus
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Calander, A.M.; Dubin, G.; Potempa, J.; Tarkowski, A.
Staphylococcus aureus infection triggers production of neutralizing, V8 protease-specific antibodies
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52
267-272
2008
Staphylococcus aureus
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Oscarsson, J.; Tegmark-Wisell, K.; Arvidson, S.
Coordinated and differential control of aureolysin (aur) and serine protease (sspA) transcription in Staphylococcus aureus by sarA, rot and agr (RNAIII)
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296
365-380
2006
Staphylococcus aureus
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Activation of the SspA serine protease zymogen of Staphylococcus aureus proceeds through unique variations of a trypsinogen-like mechanism and is dependent on both autocatalytic and metalloprotease-specific processing
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282
34129-34138
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Staphylococcus aureus, Staphylococcus aureus RN4220
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Polymorphism, genetic exchange and intragenic recombination of the aureolysin gene among Staphylococcus aureus strains
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8
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Staphylococcus aureus
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Nickerson, N.N.; Joag, V.; McGavin, M.J.
Rapid autocatalytic activation of the M4 metalloprotease aureolysin is controlled by a conserved N-terminal fungalysin-thermolysin-propeptide domain
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69
1530-1543
2008
Staphylococcus aureus
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Schmidtchen, A.; Pasupuleti, M.; Moergelin, M.; Davoudi, M.; Alenfall, J.; Chalupka, A.; Malmsten, M.
Boosting antimicrobial peptides by hydrophobic oligopeptide end tags
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284
17584-17594
2009
Staphylococcus aureus
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Biological relevance of natural alpha-toxin fragments from Staphylococcus aureus
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233
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2010
Staphylococcus aureus
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Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion
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186
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Staphylococcus aureus, Staphylococcus aureus KV27
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Extracellular proteases inhibit protein-dependent biofilm formation in Staphylococcus aureus
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12
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2010
Staphylococcus aureus
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Zdzalik, M.; Karim, A.; Wolski, K.; Buda, P.; Wojcik, K.; Brueggemann, S.; Wojciechowski, P.; Eick, S.; Calander, A.; Jonsson, I.; Kubica, M.; Polakowska, K.; Miedzobrodzki, J.; Wladyka, B.; Potempa, J.; Dubin, G.
Prevalence of genes encoding extracellular proteases in Staphylococcus aureus - important targets triggering immune response in vivo
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66
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Staphylococcus aureus proteases degrade lung surfactant protein a potentially impairing innate immunity of the lung
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Staphylococcus aureus
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Staphylococcal proteases aid in evasion of the human complement system
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6
31-46
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Staphylococcus aureus, Staphylococcus aureus V8-BC10
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Aureolysin of Staphylococcus warneri M accelerates its proteolytic cascade, and participates in biofilm formation
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80
1238-1242
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brenda
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Galectin-3 is a target for proteases involved in the virulence of Staphylococcus aureus
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85
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Contribution of YjbIH to virulence factor expression and host colonization in Staphylococcus aureus
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87
e00155-19
2019
Staphylococcus aureus (P81177), Staphylococcus aureus
brenda
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Protease-mediated growth of Staphylococcus aureus on host proteins is opp3 dependent
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10
e02553-18
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Staphylococcus aureus (P81177), Staphylococcus aureus
brenda