Authors:
Shen, H. D.; Tam, M. F.; Huang, C. H.; Chou, H.; Tai, H. Y.; Chen, Y. S.; Sheu, S. Y.; Thomas, W. R.
Authors notes:
Immunology and Cell Biology. 2011;89(2):225-30
Keywords:
BPI protein, Der f 7, Der p 7, epitope, modeling structure, odorant-binding protein
Abstract:
The group 7 allergens are important allergenic specificities for mite-sensitive patients and may need to be incorporated into new diagnostic and therapeutic strategies.
However, little is known about their biological and structural features. Position-specific iterative BLAST showed that they had strong ancestral homology to two related families of lipid-binding proteins, namely, the bactericidal permeability-increasing (BPI) proteins and the odorant-binding protein.
A three-dimensional model of Der f 7 made with the Phyre and SWISS-MODEL homology-modeling servers showed a close match with the human BPI coordinates used for its construction. The binding of the monoclonal antibody HD12 known to block IgE binding could be blocked by the linear sequence (46GILDF50) with a critical role for L48 or F50.
These hydrophobic residues were located on a surface loop of the model. The properties of Der f 7 that can be deduced from the model provide avenues for further characterizing these allergens, their IgE binding structures and biological properties that can enhance allergenicity.