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PMID:24696276
Citation |
'Chang, SH, Chen, KY and Wang, LC (2014) Identification and characterization of an asparaginyl endopeptidase from Angiostrongylus cantonensis. Parasitol. Res. ' |
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Abstract |
Asparaginyl endopeptidase, also known as legumain, is a family of cysteine proteases in many organisms. In this study, an asparaginyl endopeptidase (Ac-AEP) was identified from the cDNA library of Angiostrongylus cantonensis. The full-length of Ac-AEP was determined to be 1,472 bp with an open reading frame of 1,341 bp encoding a putative protein with 446 amino acids. This putative protein was determined to have 37-65 % identity in the amino acid sequences of the asparaginyl endopeptidases of other parasitic helminths. By real-time quantitative PCR analysis, Ac-AEP was revealed to be more abundantly expressed in the female adult worms than in other development stages. A recombinant asparaginyl endopeptidase (rAc-AEP) was then produced by a Pichia pastoris expression system. Posttranslational modification was shown to occur via N-linked glycosylation in this recombinant enzyme. The proteolytic activity of rAc-AEP was inhibited by iodoacetamide but not affected by E64, pepatain A, AEBSF, and EDTA. Moreover, the purified rAc-AEP was recognized by IgG in serum samples from BALB/c or ICR mice with A. cantonensis infection and patients with eosinophilic meningitis. These findings indicate that the rAc-AEP may have the potential for detecting A. cantonensis infection. |
Links |
PubMed Online version:10.1007/s00436-014-3866-0 |
Keywords |
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Significance
Annotations
Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
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GO:0004197: cysteine-type endopeptidase activity |
ECO:0000314: |
F |
Figure 5 shows the proteolytic activity of a recombinant asparaginyl endopeptidase revealed by zymography with gelatin as a substrate |
complete | ||||
enables |
GO:0004197: cysteine-type endopeptidase activity |
ECO:0000314: direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
See also
References
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