Ara h 3

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Structures	Swiss-model
Domains	InterPro

Ara h 3
Ara h 3
Identifiers
Organism	Arachis hypogaea (peanut)
Symbol	ara h 3
UniProt	B5TYU1
Structures
Search for
Structures	Swiss-model
Domains	InterPro

Ara h 3 is a seed storage protein from Arachis hypogaea (peanuts).^[1] It is a heat stable 11S legumin-like globulin^[2] with a stable trimeric form that comprises 19% of the total protein in peanut extracts.

Structure edit

Ara h 3 forms homotrimers and has a highly stable structure, mediated through hydrophobic interactions.^{[citation needed]} It has been established as an allergen.^[3]

The trimeric assemblies are stabilized by multiple hydrogen bonds.

Influence of Ara h 3 in peanut allergies edit

The protein Ara h 3 plays an important role in peanut allergic reactions.^[3] Ara h 3 makes up 19% of the total protein in peanut extracts and is classified as a major peanut allergen because it provokes sensitization of patients with this allergy.

This protein is a very potent allergen and it causes a severe reaction. The symptoms can be:

Skin reaction: urticarial, redness or edema.
Itchy reaction: usually around the mouth and throat.
Digestive problems: such as diarrhea, stomach cramps, nausea or vomiting.
Breath problems: it has a relation with the inflammation reaction which causes the blockage of the air passages.
Heart problems: histamine can cause a coronary artery spasm.
Anaphylaxis: a whole-body allergic reaction that causes low blood pressure, suffocation and can bring a person to death.

Treatment edit

No treatment is currently available, avoidance is the only option for peanut-allergic individuals. Unfortunately, consumers can be inadvertently exposed to peanut allergens when food becomes contaminated from processing lines shared with other peanut products. Therefore, there can be labelling mistakes because companies may not include peanuts as ingredients.

In consequence, therapeutic interventions and/or hypoallergenic peanuts are needed to prevent anaphylactic reactions caused by accidental ingestion of peanut-containing products by allergic individuals.

References edit

^ Guo B, Liang X, Chung SY, Maleki SJ (September 2008). "Proteomic screening points to the potential importance of Ara h 3 basic subunit in allergenicity of peanut". Inflammation & Allergy - Drug Targets. 7 (3): 163–6. doi:10.2174/187152808785748182. PMID 18782022.
^ Chruszcz M, Maleki SJ, Majorek KA, Demas M, Bublin M, Solberg R, Hurlburt BK, Ruan S, Mattison CP, Mattisohn CP, Breiteneder H, Minor W (November 2011). "Structural and immunologic characterization of Ara h 1, a major peanut allergen". The Journal of Biological Chemistry. 286 (45): 39318–27. doi:10.1074/jbc.M111.270132. PMC 3234756. PMID 21917921.
^ ^a ^b Jin T, Guo F, Chen YW, Howard A, Zhang YZ (May 2009). "Crystal structure of Ara h 3, a major allergen in peanut". Molecular Immunology. 46 (8–9): 1796–804. doi:10.1016/j.molimm.2009.01.023. PMID 19251323.

[pmid18782022-1] Guo B, Liang X, Chung SY, Maleki SJ (September 2008). "Proteomic screening points to the potential importance of Ara h 3 basic subunit in allergenicity of peanut". Inflammation & Allergy - Drug Targets. 7 (3): 163–6. doi:10.2174/187152808785748182. PMID 18782022.

[pmid21917921-2] Chruszcz M, Maleki SJ, Majorek KA, Demas M, Bublin M, Solberg R, Hurlburt BK, Ruan S, Mattison CP, Mattisohn CP, Breiteneder H, Minor W (November 2011). "Structural and immunologic characterization of Ara h 1, a major peanut allergen". The Journal of Biological Chemistry. 286 (45): 39318–27. doi:10.1074/jbc.M111.270132. PMC 3234756. PMID 21917921.

[crystal_structure-3] Jin T, Guo F, Chen YW, Howard A, Zhang YZ (May 2009). "Crystal structure of Ara h 3, a major allergen in peanut". Molecular Immunology. 46 (8–9): 1796–804. doi:10.1016/j.molimm.2009.01.023. PMID 19251323.

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