Ara h1
Ara h 1
Ara h 1 is a major allergen found in peanuts (Arachis hypogaea), which are a common cause of food allergies worldwide. It is a glycoprotein that belongs to the vicilin family of seed storage proteins. Ara h 1 is known for its role in triggering immune system responses in individuals with peanut allergies.
Structure and Function
Ara h 1 is a trimeric protein, meaning it is composed of three identical subunits. Each subunit is approximately 63 kDa in size. The protein is characterized by its cupin domain, which is a conserved beta-barrel structure. This domain is responsible for the protein's stability and resistance to proteolysis, which contributes to its allergenic properties.
The primary function of Ara h 1 in peanuts is as a seed storage protein, providing a source of nitrogen and carbon for the developing seedling. However, in allergic individuals, Ara h 1 is recognized as a foreign antigen by the immune system, leading to the production of IgE antibodies and the release of histamine and other mediators from mast cells and basophils.
Allergenic Properties
Ara h 1 is one of the most potent peanut allergens, along with Ara h 2 and Ara h 3. It is recognized by the IgE antibodies of over 90% of individuals with peanut allergies. The protein's resistance to digestion and its ability to bind IgE make it a significant contributor to the severity of peanut allergic reactions.
The allergenic epitopes of Ara h 1 are primarily located on the surface of the protein, allowing them to be easily recognized by the immune system. These epitopes are often conformational, meaning they depend on the protein's three-dimensional structure.
Clinical Implications
Understanding the structure and function of Ara h 1 is crucial for developing diagnostic and therapeutic strategies for peanut allergies. Allergy testing often includes measuring IgE levels specific to Ara h 1 to assess the risk of allergic reactions. Additionally, research into immunotherapy aims to desensitize individuals to Ara h 1 and other peanut allergens.
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Contributors: Prab R. Tumpati, MD