Citation
A. Malik, . and S. Ahmad, . and Siti Arija M. Arif, . and E. Sunderasan, . (2007) A molecular and in silico characterisation of Hev b 4 a glycosylated latex allergen. [Proceedings Paper]
Abstract
Hev b 4 lecithinase homologue is a highly glycosylated allergenic latex protein with seven attached N-glycan structures comprising of oligomannose and complex type N-glycans. Treatment with a mixture of N-glycosidase A and N-glycosidase F resulted in lowering of the band corresponding to Hev b 4 on SDS-gel from 53-55 kDa to circa 40 kDa this being comparable to the 38.53 kDa mass predicted by its cDNA. In Western-immunoblots the enzymatically deglycosylated Hev b 4 showed negligible binding to sera immunoglobulin E lgE from latex allergic patients; however recognition to anti-Hev b 4 rabbit polyclonal antibody lgG was retained. The results of the Western immunoblots indicated that IgE binding ability of Hev b 4 is essentially determined by its N-glycan moiety presumably by the complex type N-glycans. The complete coverage of the amino acid sequence and the N-glycan structures enabled the construction of a homology based 3D model of He v b 4. Six out of seven N-glycans were already incorporated in the preliminary 3D model of Hev b 4; when completed the model will open the way to the delineation of IgE binding to the glyco-allergen.
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Abstract
Hev b 4 lecithinase homologue is a highly glycosylated allergenic latex protein with seven attached N-glycan structures comprising of oligomannose and complex type N-glycans. Treatment with a mixture of N-glycosidase A and N-glycosidase F resulted in lowering of the band corresponding to Hev b 4 on SDS-gel from 53-55 kDa to circa 40 kDa this being comparable to the 38.53 kDa mass predicted by its cDNA. In Western-immunoblots the enzymatically deglycosylated Hev b 4 showed negligible binding to sera immunoglobulin E lgE from latex allergic patients; however recognition to anti-Hev b 4 rabbit polyclonal antibody lgG was retained. The results of the Western immunoblots indicated that IgE binding ability of Hev b 4 is essentially determined by its N-glycan moiety presumably by the complex type N-glycans. The complete coverage of the amino acid sequence and the N-glycan structures enabled the construction of a homology based 3D model of He v b 4. Six out of seven N-glycans were already incorporated in the preliminary 3D model of Hev b 4; when completed the model will open the way to the delineation of IgE binding to the glyco-allergen.
Additional Metadata
| Item Type: | Proceedings Paper |
|---|---|
| AGROVOC Term: | LATEX |
| AGROVOC Term: | HEVEA BRASILIENSIS |
| AGROVOC Term: | MOLECULAR BIOLOGY |
| AGROVOC Term: | DIALYSIS |
| AGROVOC Term: | ELECTROPHORESIS |
| AGROVOC Term: | ANALYTICAL METHODS |
| AGROVOC Term: | AMINO ACIDS |
| AGROVOC Term: | IMMUNOBLOTTING |
| AGROVOC Term: | IMMUNOGLOBULINS |
| AGROVOC Term: | BIOTECHNOLOGY |
| Geographical Term: | MALAYSIA |
| Depositing User: | Ms. Norfaezah Khomsan |
| Last Modified: | 24 Apr 2025 05:27 |
| URI: | http://webagris.upm.edu.my/id/eprint/15700 |
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