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Information on EC 3.4.21.72 - IgA-specific serine endopeptidase and Organism(s) Haemophilus influenzae and UniProt Accession P44969
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3.4.21.72 IgA-specific serine endopeptidaseSpecify your search results
Word Map
- 3.4.21.72
- neisseria
- haemophilus
- streptococcus
- influenzae
- gonorrhoeae
- hinge
- meningitidis
- sanguis
-
autotransporter
- pneumococcal
-
gonococcal
-
serogroups
-
meningococci
- oralis
- medicine
-
protease-producing
- lactamica
-
nontypeable
-
paraproteins
- ramosum
-
enzyme-neutralizing
- urealyticum
- pharmacology
- agriculture
- drug development
- analysis
The taxonomic range for the selected organisms is: Haemophilus influenzae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
iga1 protease, iga protease, immunoglobulin a1 protease, type 2 iga1 protease, iga1p, iga1-protease, immunoglobulin a protease, iga proteinase, igaa1, iga1-specific protease, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IgA protease
IgA proteinase
-
-
-
-
IgA-specific proteinase
-
-
-
-
IgA1 protease
Immunoglobulin A protease
-
-
-
-
Immunoglobulin A proteinase
-
-
-
-
Proteinase, immunoglobulin A
-
-
-
-
IgA protease
-
-
-
-
IgA1 protease
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
55127-02-1
-
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
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated and degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
desialylated IgA1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate
-
-
?
desialylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate
-
-
?
desialylated/degalactosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
artificial substrate, high activity
-
-
?
human IgA1 + H2O
?
culture supernatants from all strains tested cause degradation of human IgA1
-
-
?
human IgA1 + H2O
?
the enzyme specifically cleaves the hinge region of human IgA1, the predominant class of immunoglobulin present on mucosal membranes
-
-
?
human IgA1 + H2O
?
unique cleavage specificity of the NTHI IgA1 protease
-
-
?
human IgA1 + H2O
?
deglycosylated human IgA1, the IgA1 protease cleaves two peptide bonds within the human IgA1 hinge region at replicate sequences, cleavage of human IgA1 produces two different sized Fc fragments with N-terminal sequence Thr-Pro-Ser-Pro-Ser
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
pathogenic human aberrantly glycosylated IgA1
-
-
?
aberrantly glycosylated immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
pathogenic human aberrantly glycosylated immunglobulin A1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
human IgA1 + H2O
?
-
human IgA1 possesses a unique hinge region composed of a repeated sequence rich in proline, serine and threonine, which are the specific cleavage sites of IgA1 protease
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 24% of the substrate is cleaved after 24 h incubation
-
-
?
IgA2-IgA1 half hinge + H2O
?
-
a hybrid comprised of human IgA2 bearing half of the human IgA1 hinge region, pH 7.2, 37°C, 27% of the substrate is cleaved after 24 h incubation
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma IgA1
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human myeloma immunglobulin A1
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
all bacterial IgA1 proteases cleave the heavy chain of IgA1, both serum and secretory IgA2 proteins are IgA1 protease-resistant
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Streptococcus sanguis, Streptococcus pneumoniae and Neisseria gonorrhoeae all release IgA1 proteases each cleaving a single peptide bond, Neisseria meningitidis and Haemophilus influenzae release multiple enzyme types differing in the specific peptide bonds hydrolyzed, e.g. random clinical isolates of Neisseria meningitidis release either type 1 and type 2 protease, type 1 cleaving peptide 237-238 and type 2 cleaving 235-236 in the IgA hinge
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Haemophilus influenzae type 1 enzyme cleaves Pro231-Ser232, type 2 enzyme cleaves Pro235-Thr236, type 3 enzyme cleaves peptide bond 237-238
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
peptide analogs of human IgA as protease substrates
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
Haemophilus influenzae enzyme has at least 2 cleavage types. Serogroups, type 1 in serotypes a, b, d, f. Type 2 in c and e
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
human myeloma immunoglobulin
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 36% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhP227S + H2O
?
-
pH 7.2, 37°C, 54% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 17% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224/230P + H2O
?
-
pH 7.2, 37°C, 35% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 19% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS224P + H2O
?
-
pH 7.2, 37°C, 67% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 13% of the substrate is cleaved after 24 h incubation
-
-
?
mutant hhS230P + H2O
?
-
pH 7.2, 37°C, 14% of the substrate is cleaved after 24 h incubation
-
-
?
additional information
?
-
-
in vitro studies show that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes
-
-
?
additional information
?
-
-
the type 2 IgA1 protease is a potential virulence factor in Haemophilus influenzae, the igaB encoded enzyme is the primary mediator of IgA1 protease activity in strain 11P6H, not the type 1 IgA1 protease encoded by igaA, IgA1 proteases are classified as type 1 or type 2 based on the specific site of enzymatic cleavage in the hinge region of the IgA1 molecule
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
additional information
?
-
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated IgA1 and desialylated/degalactosylated IgA1, as compared to the wild-type IgA1 substrate, while the activity with artificial desialylated IgA1 is reduced
-
-
?
additional information
?
-
-
the enzyme activity is several fold higher with artificial substrates, degalactosylated immunglobulin A1 and desialylated/degalactosylated immunglobulin A1, as compared to the wild-type immunglobulin A1 substrate, while the activity with artificial desialylated immunglobulin A1 is reduced
-
-
?
additional information
?
-
-
the enzyme performs autocatalysis at its autocleavage site
-
-
?
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
immunoglobulin A1 + H2O
oligopeptides derived from immunoglobulin A1
IgA proteases only cleave the proline, serine and threonine rich hinge peptide unique to immunoglobulin A1
-
-
?
human IgA1 + H2O
?
-
IgA1 protease is a proteolytic enzyme with strict substrate specificity for human IgA1
-
-
?
Immunoglobulin A + H2O
immunoglobulin Fabalpha + immunoglobulin Fc
-
-
-
-
?
human IgA1 + H2O
?
culture supernatants from all strains tested cause degradation of human IgA1
-
-
?
human IgA1 + H2O
?
the enzyme specifically cleaves the hinge region of human IgA1, the predominant class of immunoglobulin present on mucosal membranes
-
-
?
human IgA1 + H2O
?
unique cleavage specificity of the NTHI IgA1 protease
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
-
-
-
?
immunglobulin A1 + H2O
immunglobulin Fc + immunglobulin Fd
-
human IgA1, cleavage at the hinge region
-
-
?
immunoglobulin A + H2O
?
-
IgA 1 proteases are a family of bacterial enzymes specifically cleaving human IgA, the immunoglobulin for antibody defense of mucosal surfaces
-
-
?
immunoglobulin A + H2O
?
-
IgA hydrolysis may allow the microbes to circumvent immunity, or possibly even recruit antibodies or their fragments as a step in the infectious process
-
-
?
additional information
?
-
-
the type 2 IgA1 protease is a potential virulence factor in Haemophilus influenzae, the igaB encoded enzyme is the primary mediator of IgA1 protease activity in strain 11P6H, not the type 1 IgA1 protease encoded by igaA, IgA1 proteases are classified as type 1 or type 2 based on the specific site of enzymatic cleavage in the hinge region of the IgA1 molecule
-
-
?
additional information
?
-
-
IgA1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agIgA1 also exists as circulating IgA1-IgG immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
immunglobulin A1 exists in forms of monomer, dimer, and oligomer (or polymer) in the physiological conditions and agimmunglobulin A1 also exists as circulating immunglobulin A1-immunglobulin G immune complexes in patients with IgAN
-
-
?
additional information
?
-
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
no inhibition by natural protease inhibitors SLPI, alpha-1-antitrypsin, cathepsin G and cystatin C, and by synthetic protease inhibitors Tos-Lys-chloromethylketone, and ZD0892
-
additional information
-
no inhibition by natural protease inhibitors SLPI, alpha-1-antitrypsin, cathepsin G and cystatin C, and by synthetic protease inhibitors Tos-Lys-chloromethylketone, and ZD0892
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the alpha-protein domain has a pI-value of higher than 10
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora
additional information
-
NTHI is a Gram-negative coccobacillus, which colonizes the human upper respiratory tract as part of the normal flora
additional information
-
distribution of igaB among clinical isolates of nontypeable Haemophilus influenzae, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
Haemophilus influenzae utilizes IgA proteases to aid in defeating the host immune response facilitating disease
evolution
physiological function
evolution
-
Haemophilus influenzae has likely acquired igaB from Neisseria meningitidis, the acquisition is accompanied by a about 20 kb genomic inversion that is present only in strains that have igaB, overview
evolution
-
Haemophilus influenzae 49247 IgA protease shows unique DNA and amino acid sequence but with typical endopeptidase domain and beta transporter domain compared to known IgA proteases from the same species
physiological function
-
the clonally related group of strains of nontypeable Haemophilus influenzae that has two IgA1 protease genes, iga and igaB, is adapted for colonization and infection in chronic obstructive pulmonary disease, COPD
physiological function
-
IgA1 protease treatment reverses mesangial deposits and hematuria in a model of IgA nephropathy, overview
physiological function
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agIgA1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated IgA1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
physiological function
-
the bacteria-derived IgA protease is capable of degrading the pathogenic human agimmunglobulin A1 and derived immune complexes in vitro and in vivo. Mesangial deposition of aberrantly glycosylated immunglobulin A1 (agIgA1) and its immune complexes is a key pathogenic mechanism of IgA nephropathy (IgAN) in humans. The bacteria-derived IgA protease also can efficiently degrade the deposited IgA1-IgG immune complexes in a passive mouse model of IgAN
physiological function
-
the IgA protease from Haemophilus influenzae strain ATCC 49247 has a high activity and the ability to degrade human in vivo deposited aberrantly glycosylated IgA1-containing immune complex. In addition to be a pathogenic factor, IgA protease is also proven to serve as a potential therapeutic agent in the treatment of IgA nephropathy (IgAN)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
-
recombinant extracellular His6-tagged IgA protease, gel filtration
additional information
-
characterization of the Neisseria IgAbeta-core, the essential unit for outer membrane targeting and extracellular protein secretion
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
the enzyme performs autocatalysis at its autocleavage site
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M sodium acetate, pH 5.0, 0.1 M potassium dihydrogen phosphate and 10% (w/v) PEG 20000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
construction of igaB mutants and igaA/igaB double mutants of strain 11P6H
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged IgA1 protease by nickel affinity chromatography, anion exchange chromatography, and gel filtration
native enzyme by hydrophobic interaction chromatography, ultrafiltration, anion exchange chromatography, dialysis, gel filtration, and again ultrafiltration
-
recombinant extracellular His6-tagged IgA protease from Escherichia coli culture medium by nickel affinity chromatography, dialysis, and ultrafiltration, to over 95% purity
-
recombinant refolded enzyme solubilized from Escherichia coli inclusion bodies by ion exchange and hydrophobic interaction chromatography, followed by ultrafiltration and diafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged IgA1 protease in Escherichia coli strain C41(DE3), method development and optimization by evaluation of expression of recombinant Haemophilus influenzae IgA1 protease by combining various expression plasmids, IgA1 protease constructs, and Escherichia coli strains under multiple conditions, overview
gene iga, DNA and amino acid sequence determination and analysis
gene igaA, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, constitutive recombinant expression of codon-optimized gene encoding His6-tagged IgA protease in Escherichia coli and secretion of the enzyme to the culture medium
-
gene igaB, DNA and amino acid sequence determination and analysis, genetic organization of the igaB locus, overview
-
igaB, COPD strains, DNA sequence determination and analysis, sequence comparisons and relation to strain 11P6H, clonal relationship among the strains, overview
-
recombinant intracellular expression of the enzyme in inclusion bodies in Escherichia coli in fed-batch fermentation
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli inclusion bodies by urea solubilization and refolding
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
the IgA1 proteases may have the potential to cleave IgA1 complexes in the human host kidney and be a therapeutic agent for IgA1 nephropathy, a disease characterized by deposition of the IgA1 antibody in the glomerulus
agriculture
-
the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil
drug development
-
a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells
medicine
pharmacology
-
systemically administered IgA protease is able to reduce the quantity of glomerular IgA immune complexes, both the antigen and antibody components, in a passive mouse model of IgA nephropathy
medicine
-
inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces
medicine
-
IgA1 protease may be an effective therapeutic candidate for IgAN by removing the mesangial deposited IgA1 in glomerular mesangium leading to immunoglobulin A nephropathy. The removal of IgA1 by IgA1 protease may separate the IgA1-containing immune complexes thereby eliminating its other components at the same time
medicine
-
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bachovchin, W.W.; Plaut, A.G.; Flentke, G.R.; Lynch, M.; Kettner, C.A.
Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids
J. Biol. Chem.
265
3738-3743
1990
Haemophilus influenzae, Neisseria gonorrhoeae
Plaut, A.G.
The IgA1 proteases of pathogenic bacteria
Annu. Rev. Microbiol.
37
603-622
1983
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Streptococcus sanguinis
Plaut, A.G.; Bachovchin, W.W.
IgA-specific prolyl endopeptidases: serine type
Methods Enzymol.
244
137-151
1994
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Ureaplasma urealyticum
Grundy, F.J.; Plaut, A.; Wright, A.
Haemophilus influenzae immunoglobulin A1 protease genes: cloning by plasmid integration-excision, comparative analyses, and localization of secretion determinants
J. Bacteriol.
169
4442-4450
1987
Haemophilus influenzae
Klauser, T.; Krmer, J.; Otzelberger, K.; Pohlner, J.; Meyer, T.F.
Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion
J. Mol. Biol.
234
579-593
1993
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
Bleeg, H.S.; Reinholdt, J.; Kilian, M.
Bacterial immunoglobulin A proteases monitored by continuous spectrophotometry
FEBS Lett.
188
357-362
1985
Haemophilus influenzae, Haemophilus influenzae HK 393
Parsons, H.K.; Vitovski, S.; Sayers, J.R.
Immunoglobulin A1 proteases: a structure-function update
Biochem. Soc. Trans.
32
1130-1132
2004
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
McGillivary, G.; Smoot, L.M.; Actis, L.A.
Characterization of the IgA1 protease from the Brazilian purpuric fever strain F3031 of Haemophilus influenzae biogroup aegyptius
FEMS Microbiol. Lett.
250
229-236
2005
Haemophilus influenzae (Q93T34), Haemophilus influenzae
Senior, B.W.; Woof, J.M.
Effect of mutations in the human immunoglobulin A1 (IgA1) hinge on its susceptibility to cleavage by diverse bacterial IgA1 proteases
Infect. Immun.
73
1515-1522
2005
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Neisseria meningitidis (Q9K0B4), Streptococcus mitis, Streptococcus mitis SK564, Streptococcus mitis SK597, Streptococcus mitis SK599, Streptococcus oralis, Streptococcus oralis SK10, Streptococcus pneumoniae, Streptococcus pneumoniae SK690, Streptococcus sanguinis, Streptococcus sanguinis SK1, Streptococcus sanguinis SK4, Streptococcus sanguinis SK49
Mistry, D.; Stockley, R.A.
IgA1 protease
Int. J. Biochem. Cell Biol.
38
1244-1248
2006
Streptococcus pneumoniae, Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
Fernaays, M.M.; Lesse, A.J.; Cai, X.; Murphy, T.F.
Characterization of igaB, a second immunoglobulin A1 protease gene in nontypeable Haemophilus influenzae
Infect. Immun.
74
5860-5870
2006
Haemophilus influenzae
Lamm, M.E.; Emancipator, S.N.; Robinson, J.K.; Yamashita, M.; Fujioka, H.; Qiu, J.; Plaut, A.G.
Microbial IgA protease removes IgA immune complexes from mouse glomeruli in vivo: potential therapy for IgA nephropathy
Am. J. Pathol.
172
31-36
2008
Haemophilus influenzae
Hotomi, M.; Kono, M.; Togawa, A.; Arai, J.; Takei, S.; Ikeda, Y.; Ogami, M.; Murphy, T.F.; Yamanaka, N.
Haemophilus influenzae and Haemophilus haemolyticus in tonsillar cultures of adults with acute pharyngotonsillitis
Auris Nasus Larynx
37
594-600
2010
Haemophilus influenzae, no activity in Haemophilus haemolyticus
Johnson, T.A.; Qiu, J.; Plaut, A.G.; Holyoak, T.
Active-site gating regulates substrate selectivity in a chymotrypsin-like serine protease the structure of Haemophilus influenzae IgA1 protease
J. Mol. Biol.
389
559-574
2009
Haemophilus influenzae (P44969), Haemophilus influenzae
Long, S.; Phan, E.; Vellard, M.C.
The expression of soluble and active recombinant Haemophilus influenzae IgA1 protease in E. coli
J. Biomed. Biotechnol.
2010
253983
2010
Haemophilus influenzae (P44969), Haemophilus influenzae
Xie, L.S.; Huang, J.; Qin, W.; Fan, J.M.
Immunoglobulin A1 protease: a new therapeutic candidate for immunoglobulin A nephropathy
Nephrology
15
584-586
2010
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis
Murphy, T.; Lesse, A.; Kirkham, C.; Zhong, H.; Sethi, S.; Munson Jr., R.
A clonal group of nontypeable Haemophilus influenzae with two IgA proteases is adapted to infection in chronic obstructive pulmonary disease
PLoS ONE
6
e25923
2011
Haemophilus influenzae
Mullins, M.A.; Register, K.B.; Bayles, D.O.; Butler, J.E.
Haemophilus parasuis exhibits IgA protease activity but lacks homologs of the IgA protease genes of Haemophilus influenzae
Vet. Microbiol.
153
407-412
2011
Haemophilus influenzae (P44969), Haemophilus influenzae
Mistry, D.V.; Stockley, R.A.
The cleavage specificity of an IgA1 protease from Haemophilus influenzae
Virulence
2
103-110
2011
Haemophilus influenzae (P44969), Haemophilus influenzae
Murphy, T.F.; Kirkham, C.; Jones, M.M.; Sethi, S.; Kong, Y.; Pettigrew, M.M.
Expression of IgA proteases by Haemophilus influenzae in the respiratory tract of adults with chronic obstructive pulmonary disease
J. Infect. Dis.
212
1798-1805
2015
Haemophilus influenzae (N0BM78), Haemophilus influenzae (Q19V48), Haemophilus influenzae, Haemophilus influenzae 124P3H1 (Q19V48), Haemophilus influenzae RD (N0BM78)
Lechner, S.M.; Abbad, L.; Boedec, E.; Papista, C.; Le Stang, M.B.; Moal, C.; Maillard, J.; Jamin, A.; Bex-Coudrat, J.; Wang, Y.; Li, A.; Martini, P.G.; Monteiro, R.C.; Berthelot, L.
IgA1 protease treatment reverses mesangial deposits and hematuria in a model of IgA nephropathy
J. Am. Soc. Nephrol.
27
2622-2629
2016
Haemophilus influenzae
Wang, H.; Zhong, X.; Li, J.; Zhu, M.; Wang, L.; Ji, X.; Fan, J.; Wang, L.
Cloning and expression of H. influenzae 49247 IgA protease in E. coli
Mol. Biotechnol.
60
134-140
2018
Haemophilus influenzae, Haemophilus influenzae ATCC 49247
Wang, L.; Li, X.; Shen, H.; Mao, N.; Wang, H.; Cui, L.; Cheng, Y.; Fan, J.
Bacterial IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes as a potential therapy for IgA nephropathy
Sci. Rep.
6
30964
2016
Haemophilus influenzae, Neisseria gonorrhoeae, Neisseria meningitidis, Neisseria gonorrhoeae ATCC 49226, Haemophilus influenzae ATCC 10211, Haemophilus influenzae ATCC 49247, Neisseria meningitidis ATCC 13090
EXTERNAL LINKS (specific for EC-Number 3.4.21.72)
Transporter Classification Database (TCDB): 1.B.12.3.1
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