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Information on EC 3.4.24.36 - leishmanolysin
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3.4.24.36 leishmanolysinSpecify your search results
Word Map
- 3.4.24.36
- promastigotes
- pneumocystis
- leishmaniasis
- carinii
- donovani
- trypanosoma
- amastigotes
- jirovecii
- mexicana
-
chaga
- pcp
-
guanidinobenzoatase
- infantum
- lipophosphoglycan
-
metacyclic
- braziliensis
-
complement-mediated
-
phagolysosome
- amazonensis
-
rat-derived
-
9-amino
-
tsetse
- viannia
-
leishmanial
- medicine
-
procyclins
- pharmacology
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-/-Leu-Lys-Lys-
Synonyms
major surface glycoprotein, cell surface protease, leishmanolysin, major surface protease, surface protease gp63, glycoprotein gp63, promastigote surface protease, metalloprotease gp63, glycoprotein 63, gp63 protein, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Cell surface protease
-
-
-
-
glycoprotein 63
Glycoprotein gp63
gp63
GP63 protein
-
-
-
-
GP63 surface metalloprotease
GP63 virulence protein
A0A3Q9STI6, A0A3Q9STK3, A0A3Q9STL5, A0A3Q9SVM5, A0A3Q9SVN4, A0A3Q9SVP4, A0A3Q9SYY1, A0A3Q9SYY8, A0A3Q9SYZ2, A0A3Q9SZ12, A0A3Q9SZ15, A0A3Q9SZ21, A0A3Q9SZ22, A0A3Q9SZ29, A0A3Q9SZ30, A0A3Q9SZ36, A0A3Q9SZ41, A0A3Q9SZQ4, A0A3Q9SZR5, A0A3Q9SZS8, A0A3Q9SZT6, A0A3Q9SZX9, A0A3Q9SZY6, A0A3Q9SZZ7, A0A3Q9T1P4, A0A3Q9T1Q3, A0A3T0NKY9, A0A3T0NKZ0, A0A3T0NKZ1, A0A3T0NKZ2, A0A3T0NKZ3, A0A3T0NKZ5, A0A3T0NKZ7, A0A3T0NKZ9, A0A3T0NL00, A0A3T0NL27
-
Leishmania metalloproteinase
-
-
-
-
Leishmania surface metalloprotease
Major surface glycoprotein
-
-
-
-
major surface protease
metalloprotease GP63
A0A3Q9STI6, A0A3Q9STK3, A0A3Q9STL5, A0A3Q9SVM5, A0A3Q9SVN4, A0A3Q9SVP4, A0A3Q9SYY1, A0A3Q9SYY8, A0A3Q9SYZ2, A0A3Q9SZ12, A0A3Q9SZ15, A0A3Q9SZ21, A0A3Q9SZ22, A0A3Q9SZ29, A0A3Q9SZ30, A0A3Q9SZ36, A0A3Q9SZ41, A0A3Q9SZQ4, A0A3Q9SZR5, A0A3Q9SZS8, A0A3Q9SZT6, A0A3Q9SZX9, A0A3Q9SZY6, A0A3Q9SZZ7, A0A3Q9T1P4, A0A3Q9T1Q3, A0A3T0NKY9, A0A3T0NKZ0, A0A3T0NKZ1, A0A3T0NKZ2, A0A3T0NKZ3, A0A3T0NKZ5, A0A3T0NKZ7, A0A3T0NKZ9, A0A3T0NL00, A0A3T0NL27
-
MSP
Promastigote surface endopeptidase
-
-
-
-
Surface acid proteinase
-
-
-
-
surface proteinase GP63
virulence factor major surface protease
Glycoprotein gp63
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-/-Leu-Lys-Lys-
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
161052-06-8
-
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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
Dansyl-Ala-Tyr-Leu-Lys-Lys-Trp-Val-NH2 + H2O
Dansyl-Ala-Tyr + ?
-
cleavage site: Tyr-Leu
-
?
protein-tyrosine phosphatase-PEST + H2O
?
-
fibroblast protein cleaved upon infection by Leishmania major. cleavage augments its catalytic activity. Cleavage occurs likely near its C-terminal nuclear localization signal. Removal of the nuclear localization signal could allow the phosphatase to access additional substrates and also enhance its catalytic activity
-
-
?
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
-
i.e. synthetic peptide derived from leishmanolysin
-
-
?
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
-
i.e. synthetic peptide derived from leishmanolysin
-
?
Ala-Arg-Ser-Val-Val-Arg-Asp-Val-Asn + H2O
Ala-Arg-Ser-Val + Val-Arg-Asp-Val-Asn
-
covers the last 4 amino acids of the prosequence and the first 5 amino acids of the native Leishmanolysin, cleavage site: Val-Val
-
?
casein + H2O
?
fluorescein isothiocyanate-labeled casein
-
-
?
casein + H2O
?
fluorescein isothiocyanate-labeled casein
-
-
?
Glucagon + H2O
?
-
major cleavage sites: Tyr10-Ser11, Asp15-Ser16, minor site: Trp25-Leu26
-
-
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
-
from horse cytochrome
-
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
-
from horse cytochrome
-
-
?
Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr + H2O
Leu-Ile-Ala-Tyr + ?
-
model peptide cytochrome c(94-102)L, cleavage site: Tyr97-Leu98
-
-
?
Leu-Ile-Ala-Tyr-Ser-Lys-Lys-Ala-Thr + H2O
?
-
model peptide cytochrome c(94-102)S, cleavage site: Tyr97-Ser98
-
-
?
myristoylated alanine-rich C kinase substrate MARCKS + H2O
?
-
-
-
?
Oxidized insulin B-chain + H2O
?
-
major cleavage site: Gly8-Ser9, minor site: Tyr16-Leu17
-
-
?
Peptide 170-182 from CW-3 HLA antigen + H2O
?
-
major cleavage site: Lys75-Asn76, minor site: Tyr73-Leu74
-
-
?
Peptide 83-94 from beta-chain of HLA DO + H2O
?
-
cleavage site: Arg84-Leu85
-
-
?
Peptides from horse cytochrome c + H2O
?
-
i.e. peptides 1-25, 39-53 and 81-104
-
-
?
Peptides from horse cytochrome c + H2O
?
-
peptide 81-104 cleavage sites: Gly84-Ile85 and Tyr97-Leu98
-
-
?
Peptides from horse cytochrome c + H2O
?
-
i.e. peptides 1-25, 39-53 and 81-104
-
-
?
protein tyrosine phosphatase PTP1B + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The PTP1B cleavage fragments are enzymatically active. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63
-
-
?
protein tyrosine phosphatase PTP1B + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages
-
-
?
protein tyrosine phosphatase SHP-1 + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The SHP-1 cleavage fragments are enzymatically active
-
-
?
protein tyrosine phosphatase SHP-1 + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages
-
-
?
protein tyrosine phosphatase TCPTP + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The TCPTP cleavage fragments are enzymatically active
-
-
?
protein tyrosine phosphatase TCPTP + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
role of enzyme in promastigote multiplication connected with its fibronectin-like properties
-
-
?
additional information
?
-
-
specificity is defined by P'-subsites of the substrates
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
-
enzyme plays a significant role in association with other surface molecules, especially lipophosphoglycan. Overexpression of enzyme can compensate lipophosphoglycan defect in the vertebrate host but in sand flies both molecules fulfill quite different functions
-
-
?
additional information
?
-
-
the major surface-metalloprotease is a virulence factor which contributes to a variety of functions including evasion of complement-mediated parasite-killing and host intramacrophage survival, the protozoan enzyme protects the parasite against antimicrobial peptide-induced apoptotic killing by the host cell, overview
-
-
?
additional information
?
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
Leishmania mexicana pifanoi
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
preferentially cleaves at amino side when hydrophobic residues are in P1'-site, basic amino acids in P2' and P3' and commonly Tyr at P1
-
-
?
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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
protein tyrosine phosphatase PTP1B + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The PTP1B cleavage fragments are enzymatically active. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63
-
-
?
protein tyrosine phosphatase SHP-1 + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The SHP-1 cleavage fragments are enzymatically active
-
-
?
protein tyrosine phosphatase TCPTP + H2O
?
-
activation and posttranslationally modification of host enzymes in infected macrophages. The TCPTP cleavage fragments are enzymatically active
-
-
?
additional information
?
-
-
the enzyme shows a broad substrate spectrum and ability to degrade albumin,hemoglobin, IgG, mucin, casein, and gut proteins obtained from Aedes aegypti
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
major surface protease is a virulence factor of Leishmania spp. protozoan, virulent Leishmania chagasi undergoes a growth-associated lengthening in the t1/2 of surface-localized MSP, but this does not occur in the attenuated L5 strain, surface-localized MSP isoforms are differently regulated in attenuated and virulent strains, overview
-
-
?
additional information
?
-
-
role of enzyme in promastigote multiplication connected with its fibronectin-like properties
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
-
enzyme plays a significant role in association with other surface molecules, especially lipophosphoglycan. Overexpression of enzyme can compensate lipophosphoglycan defect in the vertebrate host but in sand flies both molecules fulfill quite different functions
-
-
?
additional information
?
-
-
the major surface-metalloprotease is a virulence factor which contributes to a variety of functions including evasion of complement-mediated parasite-killing and host intramacrophage survival, the protozoan enzyme protects the parasite against antimicrobial peptide-induced apoptotic killing by the host cell, overview
-
-
?
additional information
?
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is an important agent for suppression of natural killer cells during Leishmain infection. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
-
-
?
additional information
?
-
-
gp63 is the principal catalyst of proteolysis during infection. It plays a central role in a number of host cell molecular events that likely contribute to the infectivity of Leishmania
-
-
?
additional information
?
-
-
Leishmania promastigotes reside in the midgut of the phlebotomine sand fly and invade host macrophages during a sand fly bite, infection may result in leishmanolysin-dependent hydrolysis of MRP, a major protein kinase C substrate in macrophages
-
?
additional information
?
-
Leishmania mexicana pifanoi
-
protects parasite membrane from cytosolic damage during their survival, differentiation and multiplication in the phagolysosomes of macrophages
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zinc
Zn2+
additional information
Zinc
-
amino acid sequence between 161-173 and 304-308 shows strong homology to zinc-binding sites with the histidine ligands and the glutamate ligand of other metalloproteinases
Zn2+
-
required, induces the enzyme, uptake during growth phase, the zinc content of the medium regulates the enzyme activity and expression, increased zinc content leads to reduced infectivity of promastigotes, therefor the infectivity of the parasites is increased in stationary phase, overview
additional information
-
MSP of Trypanosoma rangeli presents the typical characteristics of metalloproteases, such as the presence of the HEXXH motif, which corresponds to a region previously associated with the catalytic site of the enzyme
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2,2'-bipyridyl
-
strong, Zn2+ reverses, bovine serum albumin as substrate
2-mercaptoethylamine
-
Zn2+ reverses, bovine serum albumin as substrate
Benzyloxycarbonyl-Tyr-Leu-NHOH
-
i.e. hydroxamate-derivatized dipeptide, strong, azocasein as substrate
1,10-phenanthroline
-
inactivation by dialysis against 1,10-phenanthroline, reactivation of apoenzyme by Zn2+, partially by Cu2+, Co2+, Cd2+ or Ni2+, not by Hg2+, Ca2+, Fe2+, Pb2+, Ba2+, Sn2+, Mg2+, Mn2+, Fe3+ or Ag+; strong, 1 mM, Zn2+ reverses, bovine serum albumin as substrate
additional information
-
degradation of MARCKS-related protein MRP is inhibited by protein kinase C-dependent phosphorylation of MRP
-
additional information
-
the cathelicidin bovine myeloid antimicrobial peptide 28, BMAP-28, has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. BMAP-28 isomers,i.e. the D-amino acid form D-BMAP-28 and the retro-inverso form RI-BMAP-28, are resistant against GP63 protease activity and act as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages, overview
-
additional information
-
no inhibition by carboxymethyl derivative of Phe-Leu or hydroxamate derivatives of Leu or Tyr
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0037
casein
fluorogenic substrate, pH 7.2, 37°C, wild-type enzyme
0.005
casein
fluorogenic substrate, pH 7.2, 37°C, mutant F448V
0.0052
casein
fluorogenic substrate, pH 7.2, 37°C, mutant F448Y
0.0053
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA542
0.0054
casein
fluorogenic substrate, pH 7.2, 37°C, mutant S446T
0.0055
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA484
0.0098
casein
fluorogenic substrate, pH 7.2, 37°C, mutant S446A
0.0104
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA389
0.011
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA420
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.1
casein
fluorogenic substrate, pH 7.2, 37°C, mutant S446A
3.5
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA389
3.7
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA420
11.1
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA484
11.8
casein
fluorogenic substrate, pH 7.2, 37°C, mutant F448Y
11.8
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA542
11.9
casein
fluorogenic substrate, pH 7.2, 37°C, mutant S446T
12
casein
fluorogenic substrate, pH 7.2, 37°C, wild-type enzyme
12.7
casein
fluorogenic substrate, pH 7.2, 37°C, mutant F448V
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
300
casein
fluorogenic substrate, pH 7.2, 37°C, mutant S446A
300
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA389
300
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA420
2000
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA484
2200
casein
fluorogenic substrate, pH 7.2, 37°C, mutant F448Y
2200
casein
fluorogenic substrate, pH 7.2, 37°C, mutant S446T
2200
casein
fluorogenic substrate, pH 7.2, 37°C, truncated mutant DELTA542
2500
casein
fluorogenic substrate, pH 7.2, 37°C, mutant F448V
3200
casein
fluorogenic substrate, pH 7.2, 37°C, wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
additional information
-
isoelectric pattern, microheterogeneity in MW and charge
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.7 - 11.7
-
about half-maximal activity at pH 4.7 and 11.7, azocasein as substrate
5.3 - 9.5
-
about half-maximal activity at pH 5.3 and 9.5, Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr as substrate
additional information
-
the surface metallopeptidase is active at a broad spectrum of pH
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
60
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
pI-values of isoforms from stationary phase are 5.2 to 6.1
additional information
-
pI-values of isoforms from stationary phase are 5.2 to 6.1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
A0A3Q9STI6, A0A3Q9STK3, A0A3Q9STL5, A0A3Q9SVM5, A0A3Q9SVN4, A0A3Q9SVP4, A0A3Q9SYY1, A0A3Q9SYY8, A0A3Q9SYZ2, A0A3Q9SZ12, A0A3Q9SZ15, A0A3Q9SZ21, A0A3Q9SZ22, A0A3Q9SZ29, A0A3Q9SZ30, A0A3Q9SZ36, A0A3Q9SZ41, A0A3Q9SZQ4, A0A3Q9SZR5, A0A3Q9SZS8, A0A3Q9SZT6, A0A3Q9SZX9, A0A3Q9SZY6, A0A3Q9SZZ7, A0A3Q9T1P4, A0A3Q9T1Q3, A0A3T0NKY9, A0A3T0NKZ0, A0A3T0NKZ1, A0A3T0NKZ2, A0A3T0NKZ3, A0A3T0NKZ5, A0A3T0NKZ7, A0A3T0NKZ9, A0A3T0NL00, A0A3T0NL27
UniProt
brenda
at least 18 genes coding for enzyme, being differentially expressed or differentially processed during parasite growth. In stationary phase, there exist more than 10 isoforms
Uniprot
brenda
three genes encoding the enzyme: MSPS, MSPL, and MSPC
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comparison of enzyme in different strains. Considerable variability in amount and proteolytical activity of enzyme among the strains. Attenuated LV561/AV line shows low amount and low enzymatic activity. Strains L119, Neal defective in lipophosphoglycan exhibit enzyme overexpression
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
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enzymes from promastigotes and amastigotes are not identical but immunologically related
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enzymes from promastigotes and amastigotes are not identical but immunologically related
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isolated from the spleens of infected hamsters and transformed to promastigotes at 26°C
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isolated from the spleens of infected hamsters and transformed to promastigotes at 26°C
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Leishmania mexicana pifanoi
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enzymes from promastigotes and amastigotes are not identical but immunologically related
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Leishmania mexicana pifanoi
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axenic amastigotes from Leishmania mexicana pifanoi grown under macrophage-free conditions
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enzymes from promastigotes and amastigotes are not identical but immunologically related
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enzymes from promastigotes and amastigotes are not identical but immunologically related
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expresses the genes MSPS, MSPL, and two forms of MSPC
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expresses the genes MSPS, MSPL, and two forms of MSPC
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proteins from exosomes released by Leishmania infantum promastigotes
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lipophosphoglycan-deficient stationary phase promastigote
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proteins from exosomes released by Leishmania infantum promastigotes
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Leishmania mexicana pifanoi
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enzymes from promastigotes and amastigotes are not identical but immunologically related
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Leishmania mexicana U1103
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proteins from exosomes released by Leishmania infantum promastigotes
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additional information
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MSP multiple forms expression analysis during parasite life stages, overview
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additional information
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MSP multiple forms expression analysis during parasite life stages, overview
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GP63 is able to act on its substrate proteins within the nucleus of its host cell
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the host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole
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additional information
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surface molecules are glycosylphosphatidylinositol-anchored
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about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Surface-localized enzyme is released at different rates from logarithmic and stationary phase virulent promastigotes. Major mechanism regulating enzyme abundance is the rate of loss of surface-localized enzyme from promastigote surface
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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GP63 is able to act on its substrate proteins within the nucleus of its host cell
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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Leishmania mexicana U1103
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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-
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metacyclic promastigote exosomes contain the highest, and logarithmic exosomes have the lowest abundance of total major surface protease GP63. Among the major surface protease classes, major surface protease C class has the greatest variety of isoforms, but is least abundant in all exosomes. All major surface protease classes are present at higher levels in exosomes released from stationary or metacyclic promastigotes than logarithmic promastigotes
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the enzyme is secreted. The zinc-metallopeptidase inhibitor 1,10-phenanthroline is able to restrain the secretion of the metallopeptidase in a dose-dependent manner, while the phospholipase C inhibitor 4-chloromercuriphenylsulfonic acid does not alter the secretion pattern
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promastigote MSP is shed extracellularly, whereas MSPs from axenic amastigotes are not shed
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promastigote MSP is shed extracellularly, whereas MSPs from axenic amastigotes are not shed
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the host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole. The enzyme is released from the parasite surface following phagocytosis and is redistributed to the endoplasmic reticulum of macrophages
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket
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about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Internal enzyme is stable without detectable decrease in abundance up to 6 days after biosynthesis
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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most MSPs in promastigotes are membrane-associated, whereas most MSPs in amastigotes are cytosolic
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additional information
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leishmanolysin-like molecules are distributed in different cellular compartments, immunocytochemic analysis, overview. The expression of leishmanolysin-like molecules is not modulated during either temperature- or dimethylsulfoxide-elicited differentiation
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additional information
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three pools of MSP, located either internally within the parasite, anchored to the surface membrane, or released into the extracellular environment, promastigotes incubation with Matrigel matrix, a soluble basement membrane extract of Engelbreth-Holm-Swarm tumor cells, stimulates the release of internal MSP but not of surface-located MSP, at 37°C, overview
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additional information
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three pools of MSP, located either internally within the parasite, anchored to the surface membrane, or released into the extracellular environment, promastigotes incubation with Matrigel matrix, a soluble basement membrane extract of Engelbreth-Holm-Swarm tumor cells, stimulates the release of internal MSP but not of surface-located MSP, at 37°C, overview
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additional information
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GP63 is located in punctuated structures along the cell periphery in infected macrophages, with partial colocalization with the lipid raft marker cholera toxin B
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
GP63 belongs to the metzincin class, encoded by a series of tandemly linked genes usually in a single chromosome that are highly sequence-conserved among different species of Leishmania
evolution
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GP63 belongs to the metzincin class, encoded by a series of tandemly linked genes usually in a single chromosome that are highly sequence-conserved among different species of Leishmania
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malfunction
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a leishmanolysin knockout strain of Leishmania major Seidman strain lacks the GP63 surface metalloprotease
malfunction
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a leishmanolysin knockout strain of Leishmania major Seidman strain lacks the GP63 surface metalloprotease
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physiological function
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GP63 is a key Leishmania virulence factor. Leishmania GP63 alters the profile of protein tyrosine phosphatases associated with JAK-2 at the host cell plasma membrane
physiological function
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Leishmania-induced inactivation of the macrophage transcription factor AP-1 is mediated by the parasite metalloprotease GP63 at the cell surface, overview. GP63 but not LPG is highly involved in the mechanism responsible for the inactivation of AP-1 transcription factor. GP63 action requires macrophage lipid raft and is not dependent on parasite phagocytosis
physiological function
A0A3Q9STI6, A0A3Q9STK3, A0A3Q9STL5, A0A3Q9SVM5, A0A3Q9SVN4, A0A3Q9SVP4, A0A3Q9SYY1, A0A3Q9SYY8, A0A3Q9SYZ2, A0A3Q9SZ12, A0A3Q9SZ15, A0A3Q9SZ21, A0A3Q9SZ22, A0A3Q9SZ29, A0A3Q9SZ30, A0A3Q9SZ36, A0A3Q9SZ41, A0A3Q9SZQ4, A0A3Q9SZR5, A0A3Q9SZS8, A0A3Q9SZT6, A0A3Q9SZX9, A0A3Q9SZY6, A0A3Q9SZZ7, A0A3Q9T1P4, A0A3Q9T1Q3, A0A3T0NKY9, A0A3T0NKZ0, A0A3T0NKZ1, A0A3T0NKZ2, A0A3T0NKZ3, A0A3T0NKZ5, A0A3T0NKZ7, A0A3T0NKZ9, A0A3T0NL00, A0A3T0NL27
metalloprotease GP63 is the major Leishmania surface antigen. It has multiple functions required for the survival of the parasite. Metalloprotease GP63 is encoded by multiple genes and their copy numbers vary considerably between different species. A greater role for the sequence variation found among the chromosome 10 GP63 genes is possibly related to the pathogenesis of Leishmania braziliensis and closely related species within the mammalian host
physiological function
the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the host's immune functions, allowing the survival of the parasite and its dissemination
physiological function
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the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the host's immune functions, allowing the survival of the parasite and its dissemination
physiological function
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the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination
physiological function
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the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination
physiological function
the enzyme is involved in the degradation and cleavage of many biological molecules as kappa-B nuclear factor, fibronectin, tyrosine phosphatases. GP63 is capable of inhibiting the activity of the complement system and reduces the immune functions of the host, allowing the survival of the parasite and its dissemination
additional information
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Herpetomonas samuelpessoai cells are able to colonize the gut of Aedes aegypti, but the pretreatment of gut cells with purified leishmanolysin-like protein drastically diminishes the adhesion, overview. The expression of surface leishmanolysin in Herpetomonas samuelpessoai cells is drastically enhanced after passage in Aedes aegypti
additional information
homology modeling and structure-function relationship of GP63, overview
additional information
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the cathelicidin bovine myeloid antimicrobial peptide 28, BMAP-28, has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. BMAP-28 isomers,i.e. the D-amino acid form D-BMAP-28 and the retro-inverso form RI-BMAP-28, are resistant against GP63 protease activity and act as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages, overview
additional information
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homology modeling and structure-function relationship of GP63, overview
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additional information
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the cathelicidin bovine myeloid antimicrobial peptide 28, BMAP-28, has broad antimicrobial activities and confers protection in animal models of bacterial infection or sepsis. BMAP-28 isomers,i.e. the D-amino acid form D-BMAP-28 and the retro-inverso form RI-BMAP-28, are resistant against GP63 protease activity and act as anti-leishmanial agents against the promastigote and amastigote intracellular Leishmania major lifecycle stages, overview
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Show AA Sequence and Transmembrane Helices (559 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51674
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
51689
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
52000
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x * 52000, Leishmania major, deglycosylated enzyme, x * 53200, Leishmania major, deglycosylated enzyme, SDS-PAGE
52570
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Leishmania major, calculated from nucleotide sequence plus carbohydrate core of GPI anchor
53200
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x * 52000, Leishmania major, deglycosylated enzyme, x * 53200, Leishmania major, deglycosylated enzyme, SDS-PAGE
59177
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
?
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x * 59177, MSPC, sequence calculation, x * 51689, MSPS, sequence calculation, x * 51674, MSPL, sequence calculation
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?
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x * 52000, Leishmania major, deglycosylated enzyme, x * 53200, Leishmania major, deglycosylated enzyme, SDS-PAGE
additional information
masses of isoforms from stationary phase are 58000 to 63000 Da, SDS-PAGE
additional information
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masses of isoforms from stationary phase are 58000 to 63000 Da, SDS-PAGE
additional information
gp63 contains a 590 amino acids precursor protein consisting of an NH2-terminal signal peptide of 39 amino acids for membrane targeting, a pro region of 48 amino acids, the mature protein of 478 amino acids containing glycosylation and putative catalytic sites, and a COOH-terminal signal peptide of 25 amino acids for GPI attachment
additional information
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gp63 contains a 590 amino acids precursor protein consisting of an NH2-terminal signal peptide of 39 amino acids for membrane targeting, a pro region of 48 amino acids, the mature protein of 478 amino acids containing glycosylation and putative catalytic sites, and a COOH-terminal signal peptide of 25 amino acids for GPI attachment
additional information
homology modeling and structure-function relationship of GP63, overview
additional information
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homology modeling and structure-function relationship of GP63, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
phosphoprotein
posttranslational modifications of enzyme isoforms include N-glycosylation, GPI anchor addition and phosphorylation
glycoprotein
posttranslational modifications of enzyme isoforms include N-glycosylation, GPI anchor addition and phosphorylation
glycoprotein
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most MSPs in promastigotes are N-glycosylated, while in amastigotes they are not
glycoprotein
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most MSPs in promastigotes are N-glycosylated, while in amastigotes they are not
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
homology modeling based on the structure of Leishmania major gp63. The protein consists of the N-terminal, central and C-terminal domain
molecular dynamics simulation of enzyme in water. Upon solvation, enzyme undergoes a sharp structural relaxation with respect to the crystal structure. Fingerprint fluctuations of enzyme are characterized by the motion of a large part of the N-terminal domain, which is also involved in substrate recognition and proenzyme activation. Residues involved in interdomain binding are highly conserved
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monoclinic crystals, space group C2 with a : 107.2 A, b : 90.6 A, c : 70.6 A, and tetragonal crystals, space group P4(1)2(1)2(1), a : b : 63.6 A, c : 251.4 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F448V
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F448Y
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
S446A
site-directed mutagenesis, the mutant shows 50% reduced activity and altered kinetics compared to the wild-type enzyme
S446T
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
F448V
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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F448Y
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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S446A
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site-directed mutagenesis, the mutant shows 50% reduced activity and altered kinetics compared to the wild-type enzyme
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S446T
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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additional information
additional information
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preparation of active enzyme immobilized by glutaraldehyde
additional information
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enzyme-deficient transfectants due to expression of enzyme antisense mRNA show increased generation time, altered cell morphology, accumulation of cells in G2/M phase of cell cycle, and increased numbers of binucleate cells with one or two kinetoplasts. Growth of transfectants can be stimulated by addition of a fusion protein containing the fibronectin-like SRYD motif and the zinc-binding domain of enzyme
additional information
construction of several truncation mutants, deletion of about 180-211 amino acids, DELTA420 and DELTA389, from the C-terminal region results in approximately 50% reduction in residual activitycompared to the wild-type enzyme
additional information
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construction of several truncation mutants, deletion of about 180-211 amino acids, DELTA420 and DELTA389, from the C-terminal region results in approximately 50% reduction in residual activitycompared to the wild-type enzyme
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additional information
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leishmanolysin-knock out mutants show a substantially higher sensitivity to inhibitors and their antileishmanial activity, such as members of the alpha- and phi-defensins, magainins and cathelicidins, pexiganan-treatment of knock out mutants induces disruption of surface-membrane permeability and expression of features of apoptosis including smaller cell size, loss of mitochondrial membrane potential, exposure of surface phosphatidyl serine as well as induction of caspase 3/7 activity, phenotype and pexiganan cleavage products generated by leishmanolysin degradation, overview
additional information
Leishmaina major gp63ko strain has all seven gp63 genes deleted. In general these ko parasites show a decreased virulence, but are still able to cause significant footpad swelling. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
additional information
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Leishmaina major gp63ko strain has all seven gp63 genes deleted. In general these ko parasites show a decreased virulence, but are still able to cause significant footpad swelling. Proliferation of interleukin-2-activated purified natural killer cells is suppressed after exposure to the wild-type but not to gp63ko promastigotes. gp63ko Leishmaina major induces no natural killer cell proliferation when natural killer cells are co-cultured with peripheral blood mononuclear cells populations such as CD14+ monocytes or T cells
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 mg enzyme/ml, in 10 mM Tris-HCl buffer, pH 8, 0.02% w/v NaN3, prolonged periods of time
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 (DE3) pLysS by nickel affinity chromatography and ultrafiltration
recombinant His-tagged full-length gp63 from Escherichia coli BL21 (DE3) by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of full-length gp63 gene in mammalian pcDNA3.1 (2/2) expression vector, expression in CHO cells and of His-tagged protein in Escherichia coli BL21 (DE3) pLysS
DNA and amino acid sequence determination, analysis and comparison, overexpression in Escherichia coli strain BL21 (DE3) pLysS
genes gp63, DNA and amino acid sequence determination and analysis, sequence analysis and identification of homologues of major surface protease genes and sequence comparisons, phylogenetic analysis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
pharmacology
medicine
enzyme plays a key role during infection of humans with Leishmania parasites, inhibitors may aid the development of drugs
medicine
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parasite virulence is not simply correlated with the activity of enzyme. Enzyme plays a significant role in association with other surface molecules, especially lipophosphoglycan. Overexpression of enzyme can compensate lipophosphoglycan defect in the vertebrate host but in sand flies both molecules fulfill quite different functions
medicine
DNA/DNA, DNA/protein and protein/protein based vaccination using gp63 against Leishmania donovani inducing immune responses and conferred protection against challenge infection, humural responses, quantitative overview
medicine
the endoplasmic reticulum and the Golgi hinderes the exit of GP63 metalloprotease from the parasitophorous vacuole and dampens the cleavage of host proteins by GP63
medicine
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the monitoring of host MMPs levels and GP63 in Leishmania isolated from host samples can be used on the laboratory routine to predict the prognostic and treatment efficacy of American tegumentary leishmaniasis
medicine
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the monitoring of host MMPs levels and GP63 in Leishmania isolated from host samples can be used on the laboratory routine to predict the prognostic and treatment efficacy of American tegumentary leishmaniasis
medicine
the monitoring of host MMPs levels and GP63 in Leishmania isolated from host samples can be used on the laboratory routine to predict the prognostic and treatment efficacy of American tegumentary leishmaniasis
medicine
the monitoring of host MMPs levels and GP63 in Leishmania isolated from host samples can be used on the laboratory routine to predict the prognostic and treatment efficacy of American tegumentary leishmaniasis
medicine
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the monitoring of host MMPs levels and GP63 in Leishmania isolated from host samples can be used on the laboratory routine to predict the prognostic and treatment efficacy of American tegumentary leishmaniasis
medicine
-
enzyme plays a key role during infection of humans with Leishmania parasites, inhibitors may aid the development of drugs
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pharmacology
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cationic distearoyl phosphatidylcholine liposomes, used as vaccine adjuvant with the immunodominant 63 kDa glycoprotein of promastigotes, induce significant protection against progressive visceral leishmaniasis in susceptible BALB/c mice. gp63 used without adjuvant elicits partial protection but in association with liposomes exhibits marked resistance in both the livers and spleens of the mice challenged 10 days after the last vaccination. The protective efficacy of liposomal gp63 vaccination is dose dependent, with 2.5 microg of protein showing optimal protection. Mice challenged 12 weeks after immunization are still protected, and a mixed Th1/Th2 response has been induced following immunization
pharmacology
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immunization of female BALB/c mice with negatively, positively charged or neutral liposomes encapsulated with rgp63, rgp63 in soluble form. The group of mice immunized with recombinant gp63 encapsulated in neutral liposomes shows a significantly smaller footpad swelling upon challenge with Leishmania major compared with positively or negatively charged liposomes. The mice immunized with neutral liposomes show the lowest splenic parasite burden, the highest IgG2a/IgG1 ratio and IFN-gamma production and the lowest IL-4 level compared to the other groups. The results indicate that a Th1 type of immune response is induced in mice immunized with neutral liposomes more efficiently than positively charged liposomes and conversely negatively charged liposomes induce a Th2 type of immune response
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chaudhuri, G.; Chaudhuri, M.; Pan, A.; Chang, K.P.
Surface acid proteinase (gp63) of Leishmania mexicana. A metalloenzyme capable of protecting liposome-encapsulated proteins from phagolysosomal degradation by macrophages
J. Biol. Chem.
264
7483-7489
1989
Leishmania amazonensis, Leishmania mexicana pifanoi, Leishmania amazonensis LV78
brenda
Bouvier, J.; Schneider, P.; Etges, R.; Bordier, C.
Peptide substrate specificity of the membrane-bound metalloprotease of Leishmania
Biochemistry
29
10113-10119
1990
Leishmania sp.
brenda
Schlagenhauf, E.; Etges, R.; Metcalf, P.
Crystallization and preliminary X-ray diffraction studies of leishmanolysin, the major surface metalloproteinase from Leishmania major
Proteins Struct. Funct. Genet.
22
58-66
1995
Leishmania major
brenda
Bouvier, J.; Schneider, P.; Etges, R.
Leishmanolysin: surface metalloproteinase of Leishmania
Methods Enzymol.
248
614-633
1995
Leishmania amazonensis, Leishmania infantum, Leishmania major
brenda
Corradin, S.; Ransijn, A.; Corradin, G.; Roggero, M.A.; Schmitz, A.A.; Schneider, P.; Mauel, J.; Vergeres, G.
MARCKS-related protein (MRP) is a substrate for the Leishmania major surface protease leishmanolysin (gp63)
J. Biol. Chem.
274
25411-25418
1999
Leishmania major, Leishmania major LV39
brenda
Schlagenhauf, E.; Etges, R.; Metcalf, P.
The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)
Structure
6
1035-1046
1998
Leishmania major (P08148), Leishmania major, Leishmania major LRC-L119 (P08148)
brenda
Sadlova, J.; Volf, P.; Victoir, K.; Dujardin, J.C.; Votypka, J.
Virulent and attenuated lines of Leishmania major: DNA karyotypes and differences in metalloproteinase GP63
Folia Parasitol.
53
81-90
2006
Leishmania major
brenda
Pandey, S.; Chakraborti, P.; Sharma, R.; Bandyopadhyay, S.; Sarkar, D.; Adhya, S.
Involvement of Leishmania donovani major surface glycoprotein gp63 in promastigote multiplication
J. Biosci.
29
15-22
2004
Leishmania donovani
brenda
Yao, C.; Luo, J.; Storlie, P.; Donelson, J.E.; Wilson, M.E.
Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family
Mol. Biochem. Parasitol.
135
171-183
2004
Leishmania chagasi (P15706), Leishmania chagasi
brenda
Yao, C.; Luo, J.; Hsiao, C.; Donelson, J.E.; Wilson, M.E.
Internal and surface subpopulations of the major surface protease (MSP) of Leishmania chagasi
Mol. Biochem. Parasitol.
139
173-183
2005
Leishmania chagasi
brenda
Bianchini, G.; Bocedi, A.; Ascenzi, P.; Gavuzzo, E.; Mazza, F.; Aschi, M.
Molecular dynamics simulation of Leishmania major surface metalloprotease GP63 (leishmanolysin)
Proteins
64
385-390
2006
Leishmania major
brenda
Porter-Kelley, J.; Seay, M.; Singh, P.K.; Chaudhuri, G.
Bio-available Zn2+ in the growth medium as a cue for Leishmania to express its protective surface protease
Ann. Trop. Med. Parasitol.
101
89-93
2007
Leishmania amazonensis
brenda
Yao, C.; Donelson, J.E.; Wilson, M.E.
Internal and surface-localized major surface proteases of Leishmania spp. and their differential release from promastigotes
Eukaryot. Cell
6
1905-1912
2007
Leishmania chagasi, Leishmania chagasi MHOM/BR/00/1669
brenda
Hsiao, C.C.; Yao, C.; Storlie, P.; Donelson, J.E.; Wilson, M.E.
The major surface protease (MSP or GP63) in the intracellular amastigote stage of Leishmania chagasi
Mol. Biochem. Parasitol.
157
148-159
2008
Leishmania chagasi, Leishmania chagasi MHOM/BR/00/1669
brenda
Kulkarni, M.M.; McMaster, W.R.; Kamysz, E.; Kamysz, W.; Engman, D.M.; McGwire, B.S.
The major surface-metalloprotease of the parasitic protozoan, Leishmania, protects against antimicrobial peptide-induced apoptotic killing
Mol. Microbiol.
62
1484-1497
2006
Leishmania major
brenda
Razzazan, A.; Saberi, M.R.; Jaafari, M.R.
Insights from the analysis of a predicted model of gp63 in Leishmania donovani
Bioinformation
3
114-118
2008
Leishmania donovani (P23223), Leishmania donovani
brenda
Lieke, T.; Nylen, S.; Eidsmo, L.; McMaster, W.R.; Mohammadi, A.M.; Khamesipour, A.; Berg, L.; Akuffo, H.
Leishmania surface protein gp63 binds directly to human natural killer cells and inhibits proliferation
Clin. Exp. Immunol.
153
221-230
2008
Leishmania major (P08148), Leishmania major
brenda
Badiee, A.; Jaafari, M.R.; Khamesipour, A.; Samiei, A.; Soroush, D.; Kheiri, M.T.; Barkhordari, F.; McMaster, W.R.; Mahboudi, F.
The role of liposome charge on immune response generated in BALB/c mice immunized with recombinant major surface glycoprotein of Leishmania (rgp63)
Exp. Parasitol.
121
362-369
2009
Leishmania major
brenda
Bhowmick, S.; Ravindran, R.; Ali, N.
gp63 in stable cationic liposomes confers sustained vaccine immunity to susceptible BALB/c mice infected with Leishmania donovani
Infect. Immun.
76
1003-1015
2008
Leishmania donovani
brenda
Halle, M.; Gomez, M.A.; Stuible, M.; Shimizu, H.; McMaster, W.R.; Olivier, M.; Tremblay, M.L.
The Leishmania surface protease GP63 cleaves multiple intracellular proteins and actively participates in p38 mitogen-activated protein kinase inactivation
J. Biol. Chem.
284
6893-6908
2009
Leishmania major
brenda
Pereira, F.M.; Dias, F.A.; Elias, C.G.; dAvila-Levy, C.M.; Silva, C.S.; Santos-Mallet, J.R.; Branquinha, M.H.; Santos, A.L.
Leishmanolysin-like molecules in Herpetomonas samuelpessoai mediate hydrolysis of protein substrates and interaction with insect
Protist
161
589-602
2010
Herpetomonas pessoai
brenda
Gomez, M.A.; Contreras, I.; Halle, M.; Tremblay, M.L.; McMaster, R.W.; Olivier, M.
Leishmania GP63 alters host signaling through cleavage-activated protein tyrosine phosphatases
Sci. Signal.
2
ra58
2009
Leishmania sp.
brenda
Ferreira, K.A.; Ruiz, J.C.; Dias, F.C.; Lages-Silva, E.; Tosi, L.R.; Ramirez, L.E.; Pedrosa, A.L.
Genome survey sequence analysis and identification of homologs of major surface protease (gp63) genes in Trypanosoma rangeli
Vector Borne Zoonotic Dis.
10
847-853
2010
Trypanosoma rangeli, Trypanosoma rangeli P07
brenda
Mazumder, S.; Ganguly, A.; Ali, N.
The effect of C-terminal domain deletion on the catalytic activity of Leishmania donovani surface proteinase GP63: Role of Ser446 in proteolysis
Biochimie
92
1876-1885
2010
Leishmania donovani donovani (C7EX18), Leishmania donovani donovani MHOM/IN/1983/AG83 (C7EX18)
brenda
Lynn, M.A.; Kindrachuk, J.; Marr, A.K.; Jenssen, H.; Pante, N.; Elliott, M.R.; Napper, S.; Hancock, R.E.; McMaster, W.R.
Effect of BMAP-28 antimicrobial peptides on Leishmania major promastigote and amastigote growth: role of leishmanolysin in parasite survival
PLoS Negl. Trop. Dis.
5
e1141
2011
Leishmania major, Leishmania major MHOM/IL/80/Friedlin
brenda
Mazumder, S.; Maji, M.; Das, A.; Ali, N.
Potency, efficacy and durability of DNA/DNA, DNA/protein and protein/protein based vaccination using gp63 against Leishmania donovani in BALB/c mice
PLoS ONE
6
e14644
2011
Leishmania donovani (C7EX18)
brenda
Contreras, I.; Gomez, M.; Nguyen, O.; Shio, M.; McMaster, R.; Olivier, M.
Leishmania-induced inactivation of the macrophage transcription factor AP-1 is mediated by the parasite metalloprotease GP63
PLoS Pathog.
6
e1001148
2010
Leishmania donovani
brenda
Castro Neto, A.L.; Brito, A.N.A.L.M.; Rezende, A.M.; Magalhaes, F.B.; de Melo Neto, O.P.
In silico characterization of multiple genes encoding the GP63 virulence protein from Leishmania braziliensis identification of sources of variation and putative roles in immune evasion
BMC Genomics
20
118
2019
Leishmania braziliensis (A0A3Q9STI6), Leishmania braziliensis (A0A3Q9STK3), Leishmania braziliensis (A0A3Q9STL5), Leishmania braziliensis (A0A3Q9SVM5), Leishmania braziliensis (A0A3Q9SVN4), Leishmania braziliensis (A0A3Q9SVP4), Leishmania braziliensis (A0A3Q9SYY1), Leishmania braziliensis (A0A3Q9SYY8), Leishmania braziliensis (A0A3Q9SYZ2), Leishmania braziliensis (A0A3Q9SZ12), Leishmania braziliensis (A0A3Q9SZ15), Leishmania braziliensis (A0A3Q9SZ21), Leishmania braziliensis (A0A3Q9SZ22), Leishmania braziliensis (A0A3Q9SZ29), Leishmania braziliensis (A0A3Q9SZ30), Leishmania braziliensis (A0A3Q9SZ36), Leishmania braziliensis (A0A3Q9SZ41), Leishmania braziliensis (A0A3Q9SZQ4), Leishmania braziliensis (A0A3Q9SZR5), Leishmania braziliensis (A0A3Q9SZS8), Leishmania braziliensis (A0A3Q9SZT6), Leishmania braziliensis (A0A3Q9SZX9), Leishmania braziliensis (A0A3Q9SZY6), Leishmania braziliensis (A0A3Q9SZZ7), Leishmania braziliensis (A0A3Q9T1P4), Leishmania braziliensis (A0A3Q9T1Q3), Leishmania braziliensis (A0A3T0NKY9), Leishmania braziliensis (A0A3T0NKZ0), Leishmania braziliensis (A0A3T0NKZ1), Leishmania braziliensis (A0A3T0NKZ2), Leishmania braziliensis (A0A3T0NKZ3), Leishmania braziliensis (A0A3T0NKZ5), Leishmania braziliensis (A0A3T0NKZ7), Leishmania braziliensis (A0A3T0NKZ9), Leishmania braziliensis (A0A3T0NL00), Leishmania braziliensis (A0A3T0NL27), Leishmania braziliensis
brenda
Marshall, S.; Kelly, P.H.; Singh, B.K.; Pope, R.M.; Kim, P.; Zhanbolat, B.; Wilson, M.E.; Yao, C.
Extracellular release of virulence factor major surface protease via exosomes in Leishmania infantum promastigotes
Parasit. Vectors
11
355
2018
Leishmania infantum (A4HUF6), Leishmania infantum (A4HUF9), Leishmania infantum (A4HUG0), Leishmania infantum (E9AHH5), Leishmania infantum, Leishmania mexicana (E9AN53), Leishmania mexicana (P43150), Leishmania donovani donovani (F0V646), Leishmania donovani donovani (F0V651), Leishmania major (P08148), Leishmania chagasi (P15706), Leishmania donovani (P23223), Leishmania donovani (Q25274), Leishmania donovani (Q967C0), Leishmania donovani (Q967C2), Leishmania amazonensis (Q27673), Leishmania tropica (Q8MNZ1), Leishmania mexicana U1103 (E9AN53)
brenda
Murase, L.S.; de Souza, J.V.P.; de Lima Neto, Q.A.; de Mello, T.F.P.; Cardoso, B.M.; Lera-Nonose, D.S.S.L.; Teixeira, J.J.V.; Lonardoni, M.V.C.; Demarchi, I.G.
The role of metalloproteases in Leishmania species infection in the New World a systematic review
Parasitology
145
1499-1509
2018
Leishmania braziliensis, Leishmania panamensis, Leishmania mexicana venezuelensis, Leishmania mexicana (P43150), Leishmania guyanensis (Q00689)
brenda
Arango Duque, G.; Jardim, A.; Gagnon, E.; Fukuda, M.; Descoteaux, A.
The host cell secretory pathway mediates the export of Leishmania virulence factors out of the parasitophorous vacuole
PLoS Pathog.
15
e1007982
2019
Leishmania major (P08148)
brenda
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