EC Number   |
Application |
Reference |
|---|
   3.4.21.72 | 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 |
665220 |
| 3.4.21.72 | analysis |
the ability of IgA1 protease to cleave exclusively IgA1 without affecting IgA2 molecules allows a more economical and reliable method for determination of these antibody subclasses in human sera based on recombinant Neisseria meningitidis IgA1 protease. Estimation of IgA1 and IgA2 content in human serum and of IgA subclass levels and IgA1/IgA2 ratio using recombinant active and inactive forms of IgA1 protease from Neisseria meningitidis, method evaluation, overview |
-, 753051 |
| 3.4.21.72 | 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 |
665220 |
| 3.4.21.72 | medicine |
causing agent of gonorrhoea |
-, 651233 |
| 3.4.21.72 | medicine |
IgA protease-mediated degradation of agIgA1 and agIgA1 immune complexes is a potential therapy for IgA nephropathy |
-, 755437 |
| 3.4.21.72 | 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 |
718166 |
| 3.4.21.72 | medicine |
immunization of animals with IgA1pr MA28-P1004LEH6 or proteins I, II, III provides the formation of immunological memory and can protect against both meningococcal and a number of pneumococcal fatal infections. Protective properties of meningococcal IgA1pr MA28-P1004LEH6 and proteins I, II, III against pneumococci may be attributed to their conformational epitopes close in structure to epitopes of pneumococcal surface proteins. In the model of passive animal protection, sera from rabbits immunized with Streptococcus pneumoniae of different serotypes are shown to be capable of animal protection from infection with Neisseria meningitidis, at least serogroup B. Pneumococcal and meningococcal infections can cause a crossprotective effect. This makes meningococcal IgA1 proteases and their recombinant derivatives the potential components of polyvalent vaccines |
-, 754644 |
| 3.4.21.72 | medicine |
inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces |
665220 |
| 3.4.21.72 | 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 |
717879 |
| 3.4.21.72 | medicine |
the inactive mutant E1605A can be considered as a candidate vaccine component |
666834 |
