Allergenic molecules
A study on plantain pollen‘s IgE binding protein profile showed several molecular bands ranging from 70kDa to 13 kDa. The 1D gel electrophoresis showed 8 prominent groups of IgE-reactive allergens. The mass spectroscopy revealed several peptides, among these 2 immunoreactive proteins of around 39 kDa and 37 kDa, corresponding to fructose-bisphosphate aldolase and glyceraldehyde-3-phosphate dehydrogenase, respectively. Proteomic analysis revealed that these two peptides are known to work together in metabolic pathways such as glycolysis and were also recognized as IgE-binding proteins in ryegrass (Lolium perenne) pollen extracts. Another peptide Glyceraldehyde-3-phosphate dehydrogenase was also found to be a wheat (Triticum aestivum) food allergen. Other identified peptide is α-1,4-glucan-protein synthase is known to be involved in the synthesis of cellulose and shows allergenic activity in date palm (Phoenix dactylifera) pollen aldolase(9).
Allergen Pla l 1 in plantain pollen has been identified and purified. Other allergens identified as specific to plantain include a cytochrome c protein and a calcium-binding protein. (9).
Pla l 2 is the second allergen found in plantain. Pla l 2 is a profilin, with a molecular weight of 12-15 kDa, a small actin-binding protein. It is responsible for polysensitization. From its purified form, a total of four peptides are recognized which have similarities ranging from 73% to 86% with other pollen profilin. In a profilin diagnostic study, around 87.5% percent of the serum samples identified Pla l 2. (16)
Biomarkers of severity
Pla l 1 constitutes the only indicative marker allergen for the diagnosis of genuine plantain pollen sensitization. Without considering Pla l 1 as a marker molecule for genuine sensitization, most of the patients would have been diagnosed positive solely because of cross-reactivity to grass, olive, birch, or ash allergens. (17) The allergenic significance of Pla l 1 has been studied in vitro with sera of allergic patients sensitized to plantain. Of the 22 sera analyzed, 19 had IgE antibodies to Pla l 1. In addition, Pla l 1 was responsible for 80% of the total IgE-binding capacity of the whole extract, which was determined by competitive ELISA.(4).
Cross-reactivity
Patients with a true monosensitization to plantain are rarely found. The vast majority of the plantain pollen-sensitized patients show concomitant sensitizations and allergies to other pollen allergen sources, such as grass, birch, ash, or olive pollen. Recent studies showed a lack of IgE cross-reactivity of Pla l 1 with homologous allergens. However, plantain pollen also contains the panallergens such as profilin and polcalcin which are present in other pollen sources. (17).