New Findings, Pathophysiology, and Antigen Analysis in Pollen-Food Allergy Syndrome

Akiko Yagami; Motohiro Ebisawa

Disclosures

Curr Opin Allergy Clin Immunol. 2019;19(3):218-223. 

In This Article

Lipid Transfer Protein

LTPs were identified as small 8-to-10-kDa proteins forming the major allergen affecting peach-allergic patients in Spain.[39] LTPs belong to the huge prolamin protein superfamily.[40] These LTPs are considered to contribute to the functional defense against phytopathogens (bacteria, fungi) in plants.

LTPs are considered to be a panallergen that are widespread in different plant foods and pollens.[20,41] Many plant allergen proteins with sequence similarity to LTP, such as Mal d 3 (apple), Pru p3 (peach), Pru av 3 (sweet cherry), Vit v 1 (grape), and Fra a 3 (strawberry), have been identified.[17] As LTPs are extremely resistant to both heat treatment and pepsin digestion, they are likely able to reach the intestinal tract almost as an unmodified form, thereby inducing severe reactions in allergic patients.[42] LTPs are well known as important causes of plant-food allergen in the Mediterranean area.[43] Azofra et al.[44] showed that Pru p 3 (LTP) can be used as a marker allergen for LTP sensitization also in central European patients. Moreover, Deng and Yin[21] reported LTPs as major food allergens for mugwort pollen-related food allergy in China. On the other hand, a pollen LTP was found to elicit rhinitis in sensitized patients.[45] Their findings also suggested that primary sensitization to Pru p 3 can lead to respiratory allergies through cross-reactivity.

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