Spectrometry of Proteinous Allergens Inducing Human Diseases

Mass spectrometry of proteinous allergens inducing human diseases 

MARTINA MARCHETTP, JASMIN HIRSCHMANN , ELISABETH EORSTER-WALDL and GUNTER ALLMAIER  

Individuals with latex protein allergy often exhibit reactions to plant-derived food and fresh fruits, such as avocado or banana, too. N-terminal hevein-like domains seem to be responsible for these mediated reactions in the so-called latex-fruit syndrome [12]. 

Besides these hevein-like domains, lipid transfer proteins (LTPs) play an important role in food allergy [13-15] and they have therefore been suggested as model plant food allergens. Only recently, the first citric LTPs were isolated from oranges and lemons with molecular masses of 9610 and 9618 Da, respectively, determined by MALDI-TOF-MS [16]. LTPs have also been identified as the major apricot allergens [17]. The molecular masses of the intact proteins were deduced 

The cross-reactivity between various fruits and different pollen allergens is a well-known fact and has already been studied in the 80s of the last century [19,20] using radioallergosorhent tests (RASTs). One of the first pollen allergens characterized by mass spectrometry is betv 1, the major birch pollen allergen [21]. Plasma desorption mass spectrometry (PD-MS) was used to confirm the primary structures of the intact purified protein, of all potential isoforms and some selected proteolytic peptides and to invesfigate any possible posttranslational modifications. 

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