Purification of the major group 1 allergen from bahia grass pollen, Pas n 1
Drew, A.C., Davies, J.M., Dang, T.D., Rolland, J.M., & O'Hehir, R.E. (2011) Purification of the major group 1 allergen from bahia grass pollen, Pas n 1. International Archives of Allergy and Immunology, 154(4), pp. 295-298.
Group 1 grass pollen allergens are glycoproteins of the β-expansin family. They are a predominant component of pollen and are potent allergens with a high frequency of serum IgE reactivity in grass pollen-allergic patients. Bahia grass is distinct from temperate grasses and has a prolonged pollination period and wide distribution in warmer climates. Here we describe the purification of the group 1 pollen allergen, Pas n 1, from Bahia grass (Paspalum notatum), an important subtropical aeroallergen source.
Pas n 1 was purified from an aqueous Bahia grass pollen extract by ammonium sulphate precipitation, hydrophobic interaction and size exclusion chromatography, and assessed by one- and two-dimensional gel electrophoresis, immunoblotting and ELISA.
Pas n 1 was purified to a single 29-kDa protein band containing two dominant isoforms detected by an allergen-specific monoclonal antibody and serum IgE of a Bahia grass pollen-allergic donor. The frequency of serum IgE reactivity with purified Pas n 1 in 51 Bahia grass pollen-allergic patients was 90.6%. Serum IgE reactivity with purified Pas n 1 was highly correlated with serum IgE reactivity with Bahia grass pollen extract and recombinant Pas n 1 (r = 0.821 and 0.913, respectively).
Pas n 1 is a major allergen reactive at high frequency with serum IgE of Bahia grass pollen-allergic patients. Purified natural Pas n 1 has utility for improved specific diagnosis and immunotherapy for Bahia grass pollen allergy.
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|Item Type:||Journal Article|
|Keywords:||Allergen extracts, Allergen isoforms, Allergic rhinitis, Bahia grass pollen, Grass pollen allergens, IgE reactivity, Pas n 1, ammonium sulfate, grass pollen extract, immunoglobulin E antibody, monoclonal antibody, pas n 1 antigen, pollen antigen, unclassified drug, aqueous solution, article, chemical interaction, enzyme linked immunosorbent assay, gel electrophoresis, gel permeation chromatography, grass pollen, human, hydrophobicity, immunoblotting, major clinical study, molecular weight, precipitation, priority journal, protein purification, Allergens, Antigens, Plant, Electrophoresis, Gel, Two-Dimensional, Enzyme-Linked Immunosorbent Assay, Humans, Immunoglobulin E, Paspalum, Plant Proteins, Pollen, Rhinitis, Allergic, Seasonal|
|Divisions:||Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
|Deposited On:||30 Sep 2015 05:12|
|Last Modified:||01 Oct 2015 04:30|
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