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Information on EC 3.4.21.110 - C5a peptidase
for references in articles please use BRENDA:EC3.4.21.110
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EC Tree 3 Hydrolases
3.4 Acting on peptide bonds (peptidases)
3.4.21 Serine endopeptidases
3.4.21.110 C5a peptidase
IUBMB Comments
This enzyme is a surface-associated subtilisin-like serine peptidase with very specific substrate specificity. Virulent strains of streptococci, including Streptococcus pyogenes, can evade human detection and phagocytosis by destroying the complement chemotaxin C5a. Cleavage of human C5a by this enzyme reduces the ability of C5a to bind receptors on the surface of polymorphonuclear neutrophil leukocytes (PMNLs) and thereby abolishes its chemotactic properties [1,4]. Belongs in peptidase family S8A.
The enzyme appears in viruses and cellular organisms
- 3.4.21.110
- streptococci
- pyogenes
-
serotype
- agalactiae
- pharyngitis
- medicine
-
streptolysin
- streptokinase
-
chemotaxins
-
antiphagocytic
- dysgalactiae
-
m-like
-
lancefield
- impetigo
- equisimilis
-
pyrogenic
-
spycep
-
laminin-binding
- fasciitis
Reaction Schemes
showthe primary cleavage site is at His67-/-Lys68 in human C5a with a minor secondary cleavage site at Ala58-/-Ser59
Synonyms
c5a peptidase, gbs c5a peptidase, surface-bound c5a peptidase, sez c5a peptidase, streptococcal chemotactic factor inactivator, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C5a peptidase
SCPA
ScpB
SCPZ
SEZ C5a peptidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the primary cleavage site is at His67-/-Lys68 in human C5a with a minor secondary cleavage site at Ala58-/-Ser59
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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CAS REGISTRY NUMBER
COMMENTARY
100179-39-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Ac-SQLRANISH-4-nitroanilide + H2O
?
-
Substrates: weak chromogenic substrate
Products: -
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?
complement component C3 + H2O
?
Substrates: -
Products: -
Products: -
?
complement component C3a + H2O
?
Substrates: -
Products: -
Products: -
?
Cys-Val-Val-Ala-Ser-Gln-Leu-Arg-Ala-Asn-Ile-His-Gln-Asp-Met-Gln-Leu-Gly-Arg
?
-
Substrates: substrate is cleaved into 2 fragments
Products: -
Products: -
?
Cys-Val-Val-Ala-Ser-Gln-Leu-Arg-Ala-Asn-Ile-Ser-His-Lys-Asp-Met-Gln-Leu-Gly-Arg
?
-
Substrates: -
Products: -
Products: -
?
glutathione S-transferase-chemotaxin C5a-GFP + H2O
?
-
Substrates: fusion protein
Products: -
Products: -
?
N-terminal His-tagged C5a fusion protein + H2O
?
-
Substrates: Matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis of cleaved HT-C5a indicate a loss of 830 Da, consistent with the removal of seven residues from the C-terminus
Products: -
Products: -
?
VVASQLRANISHKDMQLGR + H2O
VVASQLRANISH + KDMQLGR
-
Substrates: -
Products: -
Products: -
?
chemotaxin C5a
?
-
Substrates: -
Products: -
Products: -
?
chemotaxin C5a
?
-
Substrates: cleavage site is His-Lys rather than Lys-Asp, native protein is resistant to cleavage, suggesting that His-Lys bond is inaccessible prior to proteolytic cleavage by C5 convertase
Products: -
Products: -
?
chemotaxin C5a + H2O
?
-
Substrates: -
Products: -
Products: -
?
chemotaxin C5a + H2O
?
-
Substrates: cleaves between His67 and Lys68 or Ala58 and Ser59
Products: -
Products: -
?
chemotaxin C5a + H2O
?
-
Substrates: removes a six-amino-acid fragment and thereby inactivates this chemotaxin
Products: -
Products: -
?
chemotaxin C5a + H2O
?
-
Substrates: cleavage between histidine-67 and lysine-68 near the C-terminus
Products: -
Products: -
?
rGST-C5a-enhanced green fluorescent protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
rGST-C5a-enhanced green fluorescent protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrate: Cys-Val-Val-Ala-Ser-Gln-Leu-Arg-Ala-Asn-Ile-His-Pro-Lys-Asp-Met-Gln-Leu-Gly-Arg
Products: -
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?
additional information
?
-
-
Substrates: alters the normal host inflammatory response by delaying the accumulation of PMNLs at the foci of streptococcal infection
Products: -
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?
additional information
?
-
-
Substrates: binds directly to HEp2 and A549 cells, binds to the extracellular matrix protein fibronectin, role in cell invasion
Products: -
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?
additional information
?
-
-
Substrates: mediates adherence to fibronectin, role in immune evasion by attenuating recruitment of polymorphonuclear leukocytes to the site of infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: no cleavage of rGST-enhanced green fluorescent protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: no cleavage of rGST-enhanced green fluorescent protein
Products: -
Products: -
?
additional information
?
-
-
Substrates: native bovine serum albumin and other native proteins are highly resistant to proteolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: fibronectin adhesin activity. Affinity for fibronectin is very high for both full-length recombinant ScpB and the 110-amino-acid phage display fragment
Products: -
Products: -
?
additional information
?
-
-
Substrates: group B Streptococci do not bind to fibronectin in solution, but bind to fibronectin adsorbed onto a solid surface through ScpB, that binds to a motif created by the juxtaposition of multiple fibronectin molecules
Products: -
Products: -
?
additional information
?
-
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Substrates: fibronectin adhesin activity. Affinity for fibronectin is very high for both full-length recombinant ScpB and the 110-amino-acid phage display fragment
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
chemotaxin C5a
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: alters the normal host inflammatory response by delaying the accumulation of PMNLs at the foci of streptococcal infection
Products: -
Products: -
?
additional information
?
-
-
Substrates: binds directly to HEp2 and A549 cells, binds to the extracellular matrix protein fibronectin, role in cell invasion
Products: -
Products: -
?
additional information
?
-
-
Substrates: mediates adherence to fibronectin, role in immune evasion by attenuating recruitment of polymorphonuclear leukocytes to the site of infection
Products: -
Products: -
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
anti-SCPB antibody
-
also provides protection against group A streptococcal infection
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anti-ScpA antibody
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blocks internalization of streptococci and neutralizes the C5a peptidase acitvity, enabling recruitment of polymorphoneutrophil leukocytes to sites of infection
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anti-ScpA antibody
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rise in convalescent anti-SCPA antibody in all children aged 2-12 years, mean convalescent anti-SCPA antibody level is twice the level of mean actue anti-SCPA antibody, which is statistically significant
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anti-ScpA antibody
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reduces group A streptococci colonization of nasal mucosa-associated lymphoid tissue administered alone or with cholera toxin
-
additional information
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a high degree of group A streptococci colonization of nasal mucosa-associated lymphoid tissue in control mice immunized with phosphate-buffered saline only
-
additional information
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anti-SCPA antibodies can neutralize the activity of the enzyme in vitro and in vivo
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
at the lowest fibronectin coverages the probability of observing a ScpB-Fn binding event increases linearly with fibronectin surface coverage. As a fibronectin monolayer is reached the probability of a ScpB-fibronectin binding event occurring increases markedly (ca. 50fold), with a concomitant increase in the rupture force from 17 pN to 33 pN
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
COVID-19
Enzyme kinetic and binding studies identify determinants of specificity for the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease.
Fasciitis, Necrotizing
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Impetigo
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Infant, Newborn, Diseases
Prevalence, serotypes and virulence genes of Streptococcus agalactiae isolated from pregnant women with 35-37?weeks of gestation.
Infections
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Infections
Efficacy of polymeric encapsulated C5a peptidase-based group B streptococcus vaccines in a murine model.
Infections
Enzyme kinetic and binding studies identify determinants of specificity for the immunomodulatory enzyme ScpA, a C5a inactivating bacterial protease.
Infections
Immune response to group A streptococcal C5a peptidase in children: implications for vaccine development.
Infections
Immunization with C5a peptidase from either group A or B streptococci enhances clearance of group A streptococci from intranasally infected mice.
Infections
Impact of M49, Mrp, Enn, and C5a peptidase proteins on colonization of the mouse oral mucosa by Streptococcus pyogenes.
Infections
Multifunctional glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pyogenes is essential for evasion from neutrophils.
Infections
Protective immunization in mice against group B streptococci using encapsulated C5a peptidase.
Pharyngitis
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Pharyngitis
An Experimental Group A Streptococcus Vaccine That Reduces Pharyngitis and Tonsillitis in a Nonhuman Primate Model.
Rheumatic Fever
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Rheumatic Heart Disease
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Shock, Septic
Active and passive intranasal immunizations with streptococcal surface protein C5a peptidase prevent infection of murine nasal mucosa-associated lymphoid tissue, a functional homologue of human tonsils.
Streptococcal Infections
Human immunogenicity studies on group A streptococcal C5a peptidase (SCPA) as a potential vaccine against group A streptococcal infections.
Streptococcal Infections
In vivo Streptococcus pyogenes C5a peptidase activity: analysis using transposon- and nitrosoguanidine-induced mutants.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.6
-
activity against chromogenic substrate Ac-SQLRANISH-4-nitroanilide is 60% higher than at pH 7.4
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.6
-
activity against chromogenic substrate Ac-SQLRANISH-4-nitroanilide is 60% higher than at pH 7.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 43
-
increase of temperature from 5°C to 43°C results in 10fold increase in enzyme activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptococcus zooepidemicus, gene scpZ
UniProt
brenda
Streptococcus zooepidemicus, gene scpZ
UniProt
brenda
group A streptococcal serotype M1 strains 90-131, 90-226 and MGAS5005, serotype M49 strain CS101
-
-
brenda
group A Streptococcus strain 90 226 serotype M1, strain Xen-20 serotype M49
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
additional information
physiological function
the purified recombinant SEZ C5a peptidase adheres to Hep-2 cells and interferes with the invasion of SEZ into Hep-2 cells
physiological function
complement components C3 and C3a are substrates for peptidase C5a. Both are functionally inactivated as a result of cleavage 7 amino acids upstream of the natural C3 convertase. Cleavage of C3a by C5a results in disruption of human neutrophil activation, phagocytosis and chemotaxis, while cleavage of C3 generates abnormally-sized C3a and C3b moieties with impaired function, in particular reducing C3 deposition on the bacterial surface. Expression of C5a reduces clearance of group A streptococci in vivo in wild-type and C5 deficient mice, and promotes systemic bacterial dissemination in mice that lack both C3 and C5
physiological function
-
the purified recombinant SEZ C5a peptidase adheres to Hep-2 cells and interferes with the invasion of SEZ into Hep-2 cells
-
additional information
immunization of BALB/c mice with the recombinant enzyme can elicit a significant humoral antibody response and can confer significant protection against challenge with a lethal dose of Streptococcus zooepidemicus
additional information
-
immunization of BALB/c mice with the recombinant enzyme can elicit a significant humoral antibody response and can confer significant protection against challenge with a lethal dose of Streptococcus zooepidemicus
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
propeptide is cleaved either via an autocatalytic intramolecular cleavage or by exogenous protease streotopain
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
SCP mutant, by hanging drop method, to 2 A resolution, SCPB composed of five distinct domains, N-terminal subtilisin-like protease domain with a 134-residue protease-associated domain inserted into a loop between two beta-strands, and with one of two Arg-Gly-Asp sequences found in SCPB, at the C-terminus are three fibronectin type III domains, second Arg-Gly-Asp sequence is located between fibronectin type III (1) and fibronectin type III (2)
-
crystal structure of an active form of ScpA is solved to 1.9 A resolution. The ScpA structure reveals that access to the catalytic site is restricted by variable regions in the catalytic domain and by the presence of the inserted protease-associated domain and the second fibronectin type III domains (Fn2). Modeling of the ScpA-C5a complex indicates that the substrate binds with carboxyl-terminal residues (65-74) extended through the active site and core residues (1-64) forming exosite-type interactions with the Fn2 domain. Substrate binding is anticipated to be dominated by ionic interactions in two distinct regions of ScpA. On the prime side of the active site, salt bridges are predicted between P1', P2', and P7' residues, and residues in the catalytic and PA domains. Remote to the active site, a larger number of ionic interactions between residues in the C5a core and the Fn2 domain are observed in the model. Thus, both PA and Fn2 domains are expected to play significant roles in substrate recognition
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D130A
H193A
N295A
S512A
D130A
-
strain 90 226 SCPA-mutant, impaired capacity to infect nasal mucosa-associated lymphoid tissue
additional information
additional information
-
analysis of M-like protein (simA) and C5a peptidase, two gene homologues of Streptococcus iniae, through allelic replacement reveals that M-like protein plays a significant role in Streptococcus iniae virulence and C5a peptidase does not
additional information
-
isogenic M1-mutant, expressses SCPA on cell surface
additional information
-
mutant ScpBdelta, a common natural variant of ScpB, contains a 4-amino-acid deletion that eliminates peptidase activity. High affinity for fibronectin is maintained in ScpBdelta. ScpB and scpBdelta can complement the fibronectin-binding defect of the deletion mutant strain TOH97, that does not express scpB. Thus, the delta12 allele has no effect on the fibronectin binding of recombinant ScpB, recombinant ScpB-phage display fragment, or ScpB expressed by group B streptococci. High-affinity interaction between ScpB and immobilized fibronectin is responsible for the maintenance of the scpB gene in strains lacking C5a peptidase activity
additional information
-
mutant ScpBdelta, a common natural variant of ScpB, contains a 4-amino-acid deletion that eliminates peptidase activity. High affinity for fibronectin is maintained in ScpBdelta. ScpB and scpBdelta can complement the fibronectin-binding defect of the deletion mutant strain TOH97, that does not express scpB. Thus, the delta12 allele has no effect on the fibronectin binding of recombinant ScpB, recombinant ScpB-phage display fragment, or ScpB expressed by group B streptococci. High-affinity interaction between ScpB and immobilized fibronectin is responsible for the maintenance of the scpB gene in strains lacking C5a peptidase activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amino acid residues 31-1032 of the C5a peptidase gene are fused to GST and expressed in Escherichia coli. In addition expression as an N-terminal His-tagged C5a fusion protein in Escherichia coli
-
female ICR mice immunized with encapsulated C5a peptidase or free C5a peptidase
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gene scpZ, quantitative real-time PCR expression analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
culture in the presence of 1 to 50% human serum results in a dose-dependent induction of reporter gene activity for C5a peptidase
culture in the presence of 1 to 50% human serum results in a dose-dependent induction of reporter gene activity for C5a peptidase
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culture in the presence of 1 to 50% human serum results in a dose-dependent induction of reporter gene activity for C5a peptidase
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
additional information
medicine
-
acts as a potential invasin of group A streptococcus and promotes invasion independent of fibronectin
medicine
-
immunization with C5a peptidase protein from either group A or group B streptococci provides protection against group A streptococcus infections in mice, moreover, mice immunized with antibodies directed against protein from group B streptococci also cleared streptococci from their lungs more efficiently than those immunized with tetanus toxoid
medicine
-
inactivates recombinant chemotaxin C5a by destroying its capacity to interact with the C5a receptor on human polymorphonuclear leukocytes
medicine
-
intranasal immunization with SCPA prevents colonization and infection of human tonsils, thereby eliminating potential reservoirs that maintain endemic disease
medicine
-
SCPA is highly immunogenic in children infected with group A streptococcal pharyngitis
medicine
-
encapsulated C5a peptidase elicites significant immune responses and protection against group B streptococci challenge. C5a peptidase microsphere encapsulation has potential as a group B streptococci vaccine
medicine
-
increased anti-SCPA IgG levels in rheumatic fever, rheumatic heart disease and acute glomerulo nephritis cases. The rise of anti-SCPA IgG observed in patients is irrespective of different emm types of group A streptococci strains isolated from these patients. Indian females show higher concentration of anti-SCPA antibodies than male patients. Anti-SCPA IgG1 and anti-SCPA IgG3 are the predominant subclasses of anti-SCPA antibody and clearly distinguish individuals with acute rheumatic fever from those free of streptococcal disease
medicine
-
encapsulated C5a peptidase elicits significant immune responses and protection against a group B Streptococcus challenge. C5a peptidase poly(lactide-coglycolide) microsphere encapsulation has potential as a group B Streptococcus vaccine
medicine
-
the enzyme is used for vaccine development against group B Streptococcus
medicine
the enzyme can be useful for development of subunit vaccine against the pathogen Streptococcus zooepidemicus
medicine
inactive mutant H193A elicits high titers of antigen-specific IgG1 antibodies and robust T cell-mediated immunities in mice showing potential as a Streptococcus vaccine. Cconjugating the trisaccharide repeating unit of Streptococcus polysaccharide with mutant H193A converts the nonimmunogenic oligosaccharide into a highly active and T cell-dependent antigen
medicine
-
the enzyme can be useful for development of subunit vaccine against the pathogen Streptococcus zooepidemicus
-
additional information
-
greatly reduces ability to bind to receptors of polymorphonuclear leukocytes as compared with native C5a, inactivation is temperature dependent, mediates a small decrease in the molecular weight of C5adesArg and a six-residue peptide in inactivated C5a is lost
additional information
-
ScpA and the multifunctional protein streptococcal plasmin receptor/surface dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase are both necessary for the cleavage of C5a on the bacterial surface
additional information
-
streptococcal C5a peptidase binding to integrins by the Arg-Gly-Asp motifs may stabilize conformational changes required for substrate binding
additional information
-
ScpA and the multifunctional protein streptococcal plasmin receptor/surface dehydrogenase/glyceraldehyde-3-phosphate dehydrogenase are both necessary for the cleavage of C5a on the bacterial surface
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Anderson, E.T.; Wetherell, M.G.; Winter, L.A.; Olmsted, S.B.; Cleary, P.P.; Matsuka, Y.V.
Processing, stability, and kinetic parameters of C5a peptidase from Streptococcus pyogenes
Eur. J. Biochem.
269
4839-4851
2002
Streptococcus pyogenes
brenda
Cleary, P.P.; Prahbu, U.; Dale, J.B.; Wexler, D.E.; Handley, J.
Streptococcal C5a peptidase is a highly specific endopeptidase
Infect. Immun.
60
5219-5223
1992
Streptococcus pyogenes
brenda
Cheng, Q.; Stafslien, D.; Purushothaman, S.S.; Cleary, P.
The group B streptococcal C5a peptidase is both a specific protease and an invasin
Infect. Immun.
70
2408-2413
2002
Streptococcus pyogenes
brenda
Beckmann, C.; Waggoner, J.D.; Harris, T.O.; Tamura, G.S.; Rubens, C.E.
Identification of novel adhesins from Group B streptococci by use of phage display reveals that C5a peptidase mediates fibronectin binding
Infect. Immun.
70
2869-2876
2002
Streptococcus pyogenes
brenda
Stafslien, D.K.; Cleary, P.P.
Characterization of the streptococcal C5a peptidase using a C5a-green fluorescent protein fusion protein substrate
J. Bacteriol.
182
3254-3258
2000
Streptococcus pyogenes
brenda
O'Connor, S.P.; Cleary, P.P.
In vivo Streptococcus pyogenes C5a peptidase activity: analysis using transposon- and nitrosoguanidine-induced mutants
J. Infect. Dis.
156
495-504
1987
Streptococcus pyogenes
brenda
Bohnsack, J.F.; Mollison, K.W.; Buko, A.M.; Ashworth, J.C.; Hill, H.R.
Group B streptococci inactivate complement component C5a by enzymic cleavage at the C-terminus
Biochem. J.
273
635-640
1991
Streptococcus sp.
-
brenda
Purushothaman, S.S.; Park, H.; Cleary, P.P.
Promotion of fibronectin independent invasion by C5a peptidase into epithelial cells in group A Streptococcus
Indian J. Med. Res.
119
44-47
2004
Streptococcus sp.
-
brenda