Fruit
allergens are
proteins from fruits or pollen that cause
allergy in humans, an increasing food safety concern worldwide. With the globalization of food trade and changing lifestyles and dietary habits, characterization and identification of these
allergens are urgently needed to inform public awareness, diagnosis and treatment of
allergies, drug design, as well as food standards and regulations. This study conducted a phylogenetic reconstruction and
protein clustering among 60 fruit and pollen
allergens from 19 species, and analyzed the clusters, in silico, for cross-reactivity (
IgE), 3D
protein structure prediction, transmembrane and
signal peptides, and conserved domains and motifs. Herein, we wanted to predict the likelihood of their interaction with
antibodies, as well as cross-reactivity between the many
allergens derived from the same
protein families, as the potential for cross-reactivity complicates the management of fruit
allergies. Phylogenetic analysis classified the
allergens into four clusters. The first cluster (n = 9) comprising pollen
allergens showed a high risk of cross-reactivity between eight
allergens, with Bet v1 conserved domain, but lacked a transmembrane helix and
signal peptide. The second (n = 10) cluster similarly suggested a high risk of cross-reactivity among
allergens, with Prolifin conserved domain. However, the group lacked a transmembrane helix and
signal peptide. The third (n = 13) and fourth (n = 29) clusters comprised
allergens with significant sequence diversity, predicted low risk of cross-reactivity, and showed both a transmembrane helix and
signal peptide. These results are critical for treatment and
drug design that mostly use transmembrane
proteins as targets. The prediction of high risk of cross-reactivity indicates that it may be possible to design a
generic drug that will be effective against the wide range of
allergens. Therefore, in the past, we may have avoided the array of fruit species if one was allergic to any one member of the cluster.