The earliest known evidence of peanut farming dates back 7,600 years. With a prevalence of roughly 1%,
peanut allergy is a diagnostic and treatment challenge, but is also a very good model for studying all aspects of
food allergy, including its molecular basis and pathomechanisms. Therefore, the very starting point for elucidating all these aspects is the identification of peanut
allergens with subsequent clearing of their structure and their preparation as pure recombinant and/or natural
allergens. This is the basis for in vitro diagnostic tests as well as the development of immunotherapeutic drugs. With regard to class I
food allergy,
peanut allergy affects by far the largest group of patients. In peanuts, 12
allergens have been identified and their molecular characteristics are described herein.
Ara h 1,
Ara h 3.01 and
Ara h 3.02 (the former
Ara h 4) belong to the cupin superfamily. The conglutins
Ara h 2,
Ara h 6 and
Ara h 7, and the
non-specific lipid transfer protein Ara h 9 belong to the
prolamin superfamily.
Ara h 5 (
profilin) and
Ara h 8 (Bet v 1-homologous
protein) cause class II
food allergies and are associated with inhalation
allergy to pollen via the sequential and/or conformational similarity of molecules. Two peanut oleosins are listed as
Ara h 10 and
Ara h 11 and two
defensins as
Ara h 12 and
Ara h 13 by the WHO/IUIS
Allergen Nomenclature Subcommittee. The effect of the above-specified
allergens has to be considered in the context of their matrix, which is influenced by processing factors and the individual's immune system.