Impact of oligomerization on the allergenicity of allergens

Abstract

Type I hypersensitivity (allergic reaction) is an unsuitable or overreactive immune response to an allergen due to cross-link immunoglobulin E (IgE) antibodies bound to its high-affinity IgE receptors (FcεRIs) on effector cells. It is needless to say that at least two epitopes on allergens are required to the successful and effective cross-linking. There are some reports pointing to small proteins with only one IgE epitope could cross-link FcεRI-bound IgE through homo-oligomerization which provides two same IgE epitopes. Therefore, oligomerization of allergens plays an indisputable role in the allergenic feature and stability of allergens. In this regard, we review the signaling capacity of the B cell receptor (BCR) complex and cross-linking of FcεRI which results in the synthesis of allergen-specific IgE. This review also discusses the protein-protein interactions involved in the oligomerization of allergens and provide some explanations about the oligomerization of some well-known allergens, such as calcium-binding allergens, Alt a 1, Bet v 1, Der p 1, Per a3, and Fel d 1, along with the effects of their concentrations on dimerization.

Mammalian derived lipocalin and secretoglobin respiratory allergens strongly bind ligands with potentially immune modulating properties

“…Ligand binding may also induce the formation of multimeric lipocalin complexes ( 104 ). The dimerization of lipocalin allergens and secrectoglobin Fel d 1 likely impacts their allergenic features and stability ( 105 , 106 ).…”

Subcutaneous Immunotherapy (SCIT) with the New Polymerized Molecular Allergoid Alt a1: A Pilot Study in Children with Allergic Rhinitis Sensitized to Alternaria Alternata

“…Some evidence indicates that the oligomerization of Alt a 1 is an essential prerequisite for its allergenic potential. Indeed, it has been observed that cross-linking of at least two FcεRI-linked IgE by an allergen is required for mast cell and basophil degranulation [ 43 ]. So, allergen concentration is a key factor in the dimerization of monomeric allergens.…”

Oligomerization and tyrosine nitration enhance the allergenic potential of the birch and grass pollen allergens Bet v 1 and Phl p 5

“…Aggregation and adsorption to natural or anthropogenic particles can also lead to the display of multiple epitopes ( 10 ). In addition to repetitive epitope presentation, nitration and dityrosine cross-linking can lead to epitope modification or shielding, or neoepitope formation ( 8 , 10 , 78 , 81 , 82 ).…”