3.4.24.36: leishmanolysin
This is an abbreviated version!
For detailed information about leishmanolysin, go to the full flat file.
Reaction
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
66 kDa surface metallopeptidase, Cell surface protease, glycoprotein 63, Glycoprotein gp63, gp63, GP63 metalloprotease, GP63 protein, GP63 surface metalloprotease, GP63 virulence protein, Leishmania metalloproteinase, Leishmania surface metalloprotease, leishmanolysin-like molecule, Major surface glycoprotein, major surface protease, major surface-metalloprotease, metalloprotease GP63, MSP, Promastigote surface endopeptidase, Promastigote surface protease, protective surface protease, Surface acid proteinase, surface leishmanolysin-like molecule, surface protease GP63, surface protein GP63, surface proteinase GP63, virulence factor major surface protease
ECTree
Application
Application on EC 3.4.24.36 - leishmanolysin
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
medicine
enzyme plays a key role during infection of humans with Leishmania parasites, inhibitors may aid the development of drugs
medicine
-
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
-
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
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
-
enzyme plays a key role during infection of humans with Leishmania parasites, inhibitors may aid the development of drugs
-
pharmacology
-
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
-
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