One Disappointing Misconception About CAPNS1 Exposed

Results:? Peanut symptoms were reported in 87% of the children with IgE reactivity to any of the peanut allergens Ara h 1, 2 or 3 but not to Ara h 8 (n?=?46) vs 17% of children with IgE reactivity to Ara h 8 but not to Ara h 1, 2 or 3 (n?=?23), P?Talazoparib research buy of severe symptoms and those likely to have milder or no symptoms to peanut if sensitized to pollen allergens and their peanut homologue allergens. Peanut allergy has a prevalence between 0.6% and 1.8% (1, 2); it can be fatal (3�C5) and is rarely outgrown (6). Therefore, the condition is not merely a diagnostic and therapeutic issue, but is also associated with decreased quality of life (7). However, many people who exhibit IgE antibodies to peanut report no symptoms at exposure (8). When such individuals are tested for peanut sensitization as part of a routine work up for other underlying allergic diseases, the presence of peanut-specific IgE antibodies may Microbiology inhibitor be confusing. Recently, we showed that Swedish children at school age with concomitant peanut and birch pollen sensitization reported CAPNS1 fewer symptoms to peanuts than children with sensitization to peanut only (9). Peanut sensitization without associated symptoms has recently been observed among grass-sensitized individuals (10). We, therefore, wondered if this could be explained by differences in IgE reactivity to peanut allergen components within different groups of peanut-sensitized children. The major peanut allergens Ara h 1, Ara h 2 and Ara h 3 are proteins considered responsible for the original sensitization to peanut in susceptible individuals (11). Ara h 2 is considered the most clinically important peanut allergen (12�C15). Other peanut allergens show extensive IgE cross-reactivity between homologous allergens from various sources. Ara h 8 is homologous to the major birch pollen allergen Bet v 1 and may contribute substantially to birch pollen�Cpeanut cross-reactivity (16). The profilins, exemplified by Ara h 5, are often involved in extensive IgE antibody cross-reactivity between various pollens and plant-derived foods (17, 18). Recently, a role for carbohydrate cross-reactive determinant (CCD) in the cross-reactivity between grass pollen and peanut has been implicated (10). Furthermore, IgE cross-reactivity between lipid transfer proteins (LTPs) in plant-derived foods (e.g. Ara h 9 in peanut and Pru p 3 in peach) has been reported (19).