Identification of Potential IgE-Binding Epitopes Contributing to the Cross-Reactivity of the Major Cupressaceae Pectate-Lyase Pollen Allergens (Group 1)

• Published in: Allergies 2022-09, Vol.2 (3), p.106-118
• Main Authors: Barre, Annick, Sénéchal, Hélène, Nguyen, Christophe, Granier, Claude, Rougé, Pierre, Poncet, Pascal
• Format: Article
• Language: English
• Subjects: Cryptomeria japonica; cupressaceae; Cupressus sempervirens; Juniperus ashei; Life Sciences; pectate-lyase; pollen
• ISSN: 2313-5786; 2313-5786
• DOI: 10.3390/allergies2030010

Pectate-lyase allergens, the group 1 of allergens from Cupressaceae pollen, consist of glycoproteins exhibiting an extremely well-conserved three-dimensional structure and sequential IgE-binding epitopes. Up to 10 IgE-binding epitopic regions were identified on the molecular surface, which essentially cluster at both extremities of the long, curved β-prism-shaped allergens. Most of these IgE-binding epitopes possess very similar conformations that provide insight into the IgE-binding cross-reactivity and cross-allergenicity commonly observed among Cupressaceae pollen allergens. Some of these epitopic regions coincide with putative N-glycosylation sites that most probably consist of glycotopes or cross-reactive carbohydrate determinants, recognized by the corresponding IgE antibodies from allergic patients. Pectate-lyase allergens of Cupressaceae pollen offer a nice example of structurally conserved allergens that are widely distributed in closely-related plants (Chamæcyparis, Cryptomeria, Cupressus, Hesperocyparis, Juniperus, Thuja) and responsible for frequent cross-allergenicity.