The major pollen allergen Aln g 1 is derived from the alder tree (Alnus glutinosa), which is widespread in North America and Central and Northern Europe . Aln g 1 belongs to the PR-10 (Pathogenesis-Related class 10) protein family, which includes several clinically relevant allergens known for their ability to bind hydrophobic ligands .
Aln g 1 is a glycosylated polypeptide with a calculated molecular mass of approximately 18,710 Daltons . The recombinant form of Aln g 1 is often expressed with a 10xHis tag at the N-terminus to facilitate purification through chromatographic techniques . The protein’s structure is characterized by a conserved fold typical of PR-10 proteins, which includes a seven-stranded antiparallel β-sheet and three α-helices .
Aln g 1 is a potent allergen that can act as a true sensitizer of the immune system . It has been shown to upregulate alarmins in epithelial cells, playing a crucial role in the sensitization process . The allergenicity of Aln g 1 is partly due to its ability to bind IgE antibodies from allergic patients . However, thermal denaturation of Aln g 1 can lead to a decrease in its IgE-binding capacity, suggesting that its structural integrity is essential for its allergenic properties .
Recombinant Aln g 1 is produced using various expression systems, including insect cells (SF9), to ensure proper glycosylation and folding . The recombinant protein is used in research to study the structural and immunological features of Aln g 1 and to develop hypoallergenic variants for allergen-specific immunotherapy .
Recent studies have focused on understanding the allergenic and structural features of Aln g 1 through techniques such as qPCR, CD-spectroscopy, and ELISA assays . Site-directed mutagenesis has been employed to identify key residues involved in IgE binding and ligand interactions . These insights are crucial for developing hypoallergenic variants of Aln g 1, which could be used in allergen-specific immunotherapy to treat patients with alder pollen allergies .