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Oral allergy syndrome (OAS) is an IgE-mediated immediate food allergy that is localized to the oral mucosa. Pollen food allergy syndrome (PFAS), a pollinosis-associated OAS, is caused by cross-reactivity between food and pollen allergens. However, we need to more precisely understand the underlying pathogenesis of OAS/PFAS. In the present study, we developed a method to comprehensively identify cross-reactive allergens by using murine model of OAS and protein microarray technology. We focused on lip angioedema, which is one of the most common symptoms of OAS, and confirmed that mast cells reside in the tissues inside the lower lip of the mice. Interestingly, when the food allergen ovalbumin (OVA) was injected inside the lower lip of mice with high levels of OVA-specific IgE followed by an intravenous injection of the Evans blue dye, we found immediate dye extravasation in the skin of the neck in a mast cell-dependent manner. In addition, the degree of mast cell degranulation in the oral cavity, reflecting the severity of oral allergic responses, can be estimated by measuring the amount of extravasated dye in the skin. Therefore, we used this model of OAS to examine IgE cross-reactive allergens in vivo. Protein microarray analysis showed that serum IgE from mice intraperitoneally sensitized with ragweed pollen, one of the major pollens causing pollinosis, bound highly to protein extracts from several edible plants including black peppercorn and fennel. We confirmed that the levels of black pepper-specific IgE and fennel-specific IgE were significantly higher in the serum from ragweed pollen-sensitized mice than in the serum from non-sensitized control mice. Importantly, analysis of murine model of OAS showed that the injection of black pepper or fennel extract induced apparent oral allergic responses in ragweed pollen-sensitized mice. These results indicate IgE cross-reactivity of ragweed pollen with black pepper and fennel. In conclusion, we developed mouse model of OAS to identify IgE cross-reactive pollen and food allergens, which will help understand the pathogenesis of OAS/PFAS.

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N ucleotide-binding domain leucine-rich repeat (LRR)-containing protein family pyrin domain (PYD)-containing protein 1 (NLRP1) forms an inflammasome complex with apoptosis-associated speck-like protein containing a caspase recruitment domain and caspase-1. Inflammasome-activated caspase-1 cleaves pro-IL-1β or pro-IL-18 to produce its mature form and induces a type of cell death called pyroptosis through gasdermin D activation. NLRP1 undergoes autoproteolysis within its function-to-find domain (FIIND) to generate N-and C-terminal fragments that remain associated; the liberated C-terminal fragment, including caspase activation and recruitment domain (CARD), triggers inflammasome activation. NLRP1-associated autoinflammatory diseases are caused by genetic alterations of NLRP1, including a FIIND mutation in one case. (1,2) Case PresentationWe previously reported on an atypical case of Papillon-Lefèvre syndrome in an 11-year-old girl with an episode of palmoplantar keratosis and periodontitis; however, she also had liver cirrhosis as one of its unusual symptoms. Any mutation in the cathepsin C gene was not present. (3) Because of Abbreviations: CK-18, cytokeratin 18; FIIND, function-to-find domain; LRR, leucine-rich repeat; NLRP1, nucleotide-binding domain LRRcontaining protein family PYD-containing protein 1; NLRP3, nucleotide-binding domain LRR-containing protein family PYD-containing protein 3; PYD, pyrin domain; SNPs, single-nucleotide polymorphisms.

et al. High-fat diet exacerbates early psoriatic skin inflammation independent of obesity: saturated fatty acids as key players.