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Information on EC 3.4.24.29 - aureolysin and Organism(s) Staphylococcus aureus and UniProt Accession Q2FZL2
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3.4.24.29 aureolysinSpecify your search results
Word Map
- 3.4.24.29
- c3b
- plasminogen
-
thrombolytic
- plasmin
-
hemolytic
- clot
- fibrin
-
fibrinolytic
- streptokinase
-
staphylococcal
- properdin
-
complement-mediated
- fibrinogen
-
nephritic
-
decay-accelerating
- glomerulonephritis
-
fibrin-specific
-
cell-bound
-
c3nefs
-
fluid-phase
-
membranoproliferative
- cobra
-
mbl-associated
- masp-2
-
2-antiplasmin
- glomerulopathy
-
kringle
-
mannan-binding
-
plasminogen-activating
- alpha2-antiplasmin
-
reocclusion
- ficolins
- glu-plasminogen
- reteplase
-
amidolytic
- coagulase
-
opsonin
-
leukocidin
- hemoglobinuria
-
profibrinolytic
- medicine
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Cleavage of insulin B chain with specificity similar to that of thermolysin, preferring hydrophobic P1' residue. Activates the glutamyl endopeptidase (EC 3.4.21.19) of Staphylococcus aureus
Synonyms
c3 convertase, staphylokinase, aureolysin, aurwm, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Proteinase, Staphylococcus aureus neutral
-
-
-
-
Staphylococcus aureus neutral protease
-
-
-
-
Staphylococcus aureus neutral proteinase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
39335-13-2
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
-
?
Collagen + H2O
?
the enzyme cleaves collagen into peptide fragments that can support Staphylococcus aureus growth under nutrient-limited conditions
-
-
?
GWTLNSAGYLLGPHAIDNHRSFHDKYGLA-NH2 + H2O
Gly-Trp-Thr + Leu-Asn-Ser + Ala-Gly + Tyr + Leu + LGPHAIDNHRS + FHDKYG + Leu-Ala-NH2
-
i.e. galanin
-
-
?
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
-
-
?
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
-
-
?
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
-
?
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
-
-
?
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
-
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
-
?
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Zn2+
additional information
Co2+
-
slight stimulation of protease I, protease II inactive in presence of
Co2+
-
reactivates 1,10-phenanthroline inactivated enzyme with 160% of the activity of the native enzyme
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha2-Macroglobulin
-
a regulatory serpin, 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
-
Co2+
-
protease II inactive in presence of, protease I slightly stimulated
DFP
-
1.0 mM, 30 min, 20°C, activity of protease I is reduced by 10%, activity of protease II by 30%
NaCl
-
50% reduction of activity at 0.3 M for protease I and 0.5 M for protease II
plasminogen activator inhibitor-1
-
PAI-1, a regulatory serpin, interaction analysis with aureolysin, overview, 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
additional information
-
protease I is not significantly affected by SH-reducing, SH-inactivating or metal-complexing agents
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Reducing agents
-
protease II active only in presence of reducing agents such as cysteine, 2-mercaptoethanol or sodium thioglycollate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
the enzyme is expressed and secreted in the course of human and mouse infection, overview
additional information
-
the enzyme is expressed and secreted in the course of human and mouse infection, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
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 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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
mutation T85R/L86Y at the site of autocatalytic activation in the propeptide results in secretion of an intact N-terminal propeptide with degradation of the M4 metalloprotease domain. The fungalysin-thermolysin-propeptide domain promotes intracellular processing of proaureolysin while bestowing a chaperone function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
inhibitor-free form, cristall from sitting-drop vapour-diffusion method, refinement by molecular replacement
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T85R/L86Y
-
mutation at the site of autocatalytic activation in the propeptide. Mutation results in secretion of an intact N-terminal propeptide with degradation of the M4 metalloprotease domain. The segment of the fungalysin-thermolysin-propeptide domain promotes intracellular processing of proaureolysin while bestowing a chaperone function
additional information
additional information
-
construction of aur- mutants lacking aureolysin activity
additional information
-
construction of diverse mutant strains using wild-type strain 8325-4, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Purified enzyme contains trace amounts of a serine proteinase which rapidly degrades the Staphylococcus aureus metalloproteinase when EDTA is present, no degradation occurs when Ca2+ is added
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by hydrophobic interaction and ion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene aur, DNA and amino acid sequence determination and analysis, expression analysis and genetic survey of the prevalence of extracellular protease-encoding genes in genomes of 167 commensal and pathogenic strains of Staphylococcus aureus, overview. Gene expression and secretion of the enzyme in the course of human and mouse infection, PDR-based expression analysis
gene aur, encoding the enzyme, is regulated by the genes sarA, rot, and agr, the latter encoding RNAIII, agr and mgr A stimulate enzyme expression, while rot and sar A suppress it, mutational analysis and expression analysis, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
disruption of a two-gene operon, yjbIH, results in decreased levels of pigmentation and aureolysin activity relative to the wild-type strain. Decreased levels of pigmentation and aureolysin activity in the yjbH mutant are dependent on the transcriptional regulator Spx
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
enzyme does not act as a virulence factor. Staphylococcus aureus strains lacking enzyme, or serine protease, or cysteine protease, show similar frequency or severity of joint disease as wild-type in a mouse model
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Drapeau, G.R.
Role of metalloprotease in activation of the precursor of staphylococcal protease
J. Bacteriol.
136
607-613
1978
Staphylococcus aureus
Potempa, J.; Porwit-Bobr, Z.; Travis, J.
Stabilization vs. degradation of Staphylococcus aureus metalloproteinase
Biochim. Biophys. Acta
993
301-304
1989
Staphylococcus aureus
Saheb, S.A.
Purification and properties of a metalloprotease from Staphylococcus aureus
Biochimie
60
429-435
1978
Staphylococcus aureus, Staphylococcus aureus A152
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
1185-1193
1998
Staphylococcus aureus, Staphylococcus aureus V8-BC 10
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
Antimicrob. Agents Chemother.
48
4673-4679
2004
Staphylococcus aureus
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
Microbes Infect.
6
202-206
2004
Staphylococcus aureus, Staphylococcus aureus NCTC 8325
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
Biochem. J.
410
157-165
2008
Staphylococcus aureus
Calander, A.M.; Dubin, G.; Potempa, J.; Tarkowski, A.
Staphylococcus aureus infection triggers production of neutralizing, V8 protease-specific antibodies
FEMS Immunol. Med. Microbiol.
52
267-272
2008
Staphylococcus aureus
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)
Int. J. Med. Microbiol.
296
365-380
2006
Staphylococcus aureus
Nickerson, N.N.; Prasad, L.; Jacob, L.; Delbaere, L.T.; McGavin, M.J.
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
J. Biol. Chem.
282
34129-34138
2007
Staphylococcus aureus, Staphylococcus aureus RN4220
Sabat, A.J.; Wladyka, B.; Kosowska-Shick, K.; Grundmann, H.; van Dijl, J.M.; Kowal, J.; Appelbaum, P.C.; Dubin, A.; Hryniewicz, W.
Polymorphism, genetic exchange and intragenic recombination of the aureolysin gene among Staphylococcus aureus strains
BMC Microbiol.
8
129
2008
Staphylococcus aureus
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
Mol. Microbiol.
69
1530-1543
2008
Staphylococcus aureus
Schmidtchen, A.; Pasupuleti, M.; Moergelin, M.; Davoudi, M.; Alenfall, J.; Chalupka, A.; Malmsten, M.
Boosting antimicrobial peptides by hydrophobic oligopeptide end tags
J. Biol. Chem.
284
17584-17594
2009
Staphylococcus aureus
Kwak, Y.K.; Hoegbom, M.; Colque-Navarro, P.; Moellby, R.; Vecsey-Semjen, B.
Biological relevance of natural alpha-toxin fragments from Staphylococcus aureus
J. Membr. Biol.
233
93-103
2010
Staphylococcus aureus
Laarman, A.J.; Ruyken, M.; Malone, C.L.; van Strijp, J.A.; Horswill, A.R.; Rooijakkers, S.H.
Staphylococcus aureus metalloprotease aureolysin cleaves complement C3 to mediate immune evasion
J. Immunol.
186
6445-6453
2011
Staphylococcus aureus, Staphylococcus aureus KV27
Marti, M.; Trotonda, M.; Tormo-Mas, M.; Vergara-Irigaray, M.; Cheung, A.; Lasa, I.; Penades, J.
Extracellular proteases inhibit protein-dependent biofilm formation in Staphylococcus aureus
Microbes Infect.
12
55-64
2010
Staphylococcus aureus
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
FEMS Immunol. Med. Microbiol.
66
220-229
2012
Staphylococcus aureus (Q2FUX4), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FUX4)
Kantyka, T.; Pyrc, K.; Gruca, M.; Smagur, J.; Plaza, K.; Guzik, K.; Zeglen, S.; Ochman, M.; Potempa, J.
Staphylococcus aureus proteases degrade lung surfactant protein a potentially impairing innate immunity of the lung
J. Innate Immun.
5
251-260
2013
Staphylococcus aureus
Jusko, M.; Potempa, J.; Kantyka, T.; Bielecka, E.; Miller, H.; Kalinska, M.; Dubin, G.; Garred, P.; Shaw, L.; Blom, A.
Staphylococcal proteases aid in evasion of the human complement system
J. Innate Immun.
6
31-46
2014
Staphylococcus aureus, Staphylococcus aureus V8-BC10
Elmwall, J.; Kwiecinski, J.; Na, M.; Ali, A.A.; Osla, V.; Shaw, L.N.; Wang, W.; Saevman, K.; Josefsson, E.; Bylund, J.; Jin, T.; Welin, A.; Karlsson, A.
Galectin-3 is a target for proteases involved in the virulence of Staphylococcus aureus
Infect. Immun.
85
e00177-17
2017
Staphylococcus aureus (Q2FZL2), Staphylococcus aureus, Staphylococcus aureus NCTC 8325 (Q2FZL2)
Austin, C.M.; Garabaglu, S.; Krute, C.N.; Ridder, M.J.; Seawell, N.A.; Markiewicz, M.A.; Boyd, J.M.; Bose, J.L.
Contribution of YjbIH to virulence factor expression and host colonization in Staphylococcus aureus
Infect. Immun.
87
e00155-19
2019
Staphylococcus aureus (P81177), Staphylococcus aureus
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