Background: Albumins are multifunctional proteins present in the blood serum of animals. They can bind and transport a wide variety of ligands which they accommodate due to their conformational flexibility. Serum albumins are highly conserved both in amino acid sequence and three-dimensional structure. Several mammalian and avian serum albumins (SAs) are also allergens. Sensitization to one of the SAs coupled with the high degree of conservation between SAs may result in cross-reactive antibodies in allergic individuals. Sensitivity to SA generally begins with exposure to an aeroallergen, which can then lead to cross-sensitization to serum albumins present in food.
Scope of review: This review focuses on the allergenicity of SAs presented in a structural context.
Major conclusions: SA allergenicity is unusual taking into account the high sequence identity and similarity between SA from different species and human serum albumin. Cross-reactivity of human antibodies towards different SAs is one of the most important characteristics of these allergens.
General significance: Establishing a relationship between sequence and structure of different SAs and their interactions with antibodies is crucial for understanding the mechanisms of cross-sensitization of atopic individuals. Structural information can also lead to better design and production of recombinant SAs to replace natural proteins in allergy testing and desensitization. Therefore, structural analyses are important for diagnostic and treatment purposes. This article is part of a Special Issue entitled Serum Albumin.
Keywords: Allergen; Antibody; BSA; Cross-reactive; Cross-sensitization; FSA; HSA; IgE; IgG; MMR; MMRV; PSA; SA; Serum albumin; bovine serum albumin; feline serum albumin; human serum albumin; immunoglobulin E; immunoglobulin G; measles–mumps–rubella; measles–mumps–rubella–varicella; porcine serum albumin; serum albumin.
© 2013.