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Characterization of the 41kDa allergen Asp v 13, a subtilisin-like serine protease from Aspergillus versicolor
- Source :
-
Molecular Immunology . Sep2011, Vol. 48 Issue 15/16, p1827-1834. 8p. - Publication Year :
- 2011
-
Abstract
- Abstract: Aspergillus versicolor is common on moldy building materials. Asp v 13, the principal allergen is produced by strains collected from across Canada. In this paper, we report a 1833bp Asp v 13 open reading frame predicted to encode a protein of 403 amino acids in length with three introns. A BLAST search of Asp v 13, a phylogenic tree calculation and alignment with its homologous proteins from other species indicated that Asp v 13 is a secretory, subtilisin-like serine protease widely distributed in Aspergillus species. His-tagged Asp v 13 was over-expressed in Escherichia coli and purified using Ni-NTA columns with a yield of 1mg/L. Based on immuno binding assay of recombinant protein both antibodies developed against the natural protein, and human sera IgE, the recombinant protein was similar to the natural form. Six IgE- and seven IgG-binding epitopes were also identified with selected human sera along the entire amino acid sequence of Asp v 13. Most residues binding these epitopes are exposed on the surface and correspond to charged regions of the molecule. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 01615890
- Volume :
- 48
- Issue :
- 15/16
- Database :
- Academic Search Index
- Journal :
- Molecular Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 65042953
- Full Text :
- https://doi.org/10.1016/j.molimm.2011.05.010