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Background: Peach gibberellin-regulated protein (peamaclein) has recently emerged as a relevant food allergen in cypress pollen-hypersensitive patients. Objective: We looked for mono-sensitization to peamaclein among Italian cypress-pollen allergic patients. Material and methods: 835 cypress pollen hypersensitive patients from 28 Italian allergy centers under went thorough interview for food-allergic reactions, and SPT with a commercial peach extracts containing peamaclein. In peach reactors, IgE to rPru p 3 was measured, and those scoring negative were enrolled as potentially mono-sensitized to peamaclein. IgE reactivity to rPru p 7 was evaluated by immunoblot and by an experimental ImmunoCAP with rPru p 7. Results: Peach SPT scored positive in 163 (19.5%) patients but 127 (77,9%) were excluded because Pru p 3 reactors. Twenty-four (14,7%, corresponding to 2.8% of the entire study population) were considered as potentially mono-sensitized to peamaclein. Their distribution did not show any geographic preference. Seventeen/24 (70,8%) had a history of food allergy, in most cases (n=15) to peach. Other offending foods included other Rosaceae, citrus fruits, fig, melon, tree nuts, and kiwi. On peach immunoblot, only 3/18 putative peamaclein allergic subjects reacted to a band at about 7kDa; 4 other patients reacted at about 50-60 kDa. Ten/18 (56%) scored positive for Pru p 7 on ImmunoCAP. Conclusion: Peamaclein allergy and sensitization prevalence seem rare in Italy. Most patients react to peach, albeit other Rosaceae fruits and several citrus fruits may also act as offending foods. Peach and cypress pollen probably share also cross-reacting allergens other than peamaclein.

BACKGROUND: Cypresses play an important role in the urban landscape of the Mediterranean region, releasing a huge amount of allergenic airborne pollen which causes a specific pollinosis in exposed people. OBJECTIVE: The aim of this work is to evaluate, in vivo and in vitro, the potential allergenicity of Cupressus macrocarpa pollen, and to compare it with the allergenicity observed for C. arizonica and C. sempervirens. METHODS: Pollen extracts of the three species were prepared, to determine their protein profile through SDS PAGE analysis and to evaluate their allergenic potential through EAST inhibition assays and SPT. Pollen grain composition was evaluated using a cytochemical approach with optical microscopy. RESULTS: SDS PAGE, EAST inhibition and SPT indicated the higher allergenic potential of C. arizonica compared to C. sempervirens and C. macrocarpa. No significant differences in allergenic potential were found between the latter two species. Cytochemical observations reveal higher ?-glucans and protein content in the intine of C. arizonica during hydration. CONCLUSION: The higher protein content found in C. arizonica pollen grains extract may be due to higher enzyme activity leading to the movement of ?-glucans and pectins from the intine to the partially developed pollen cell wall during hydration. This could explain the higher potential allergenicity of C.arizonica in respect to C. macrocarpa and C. sempervirens.

A case of rice allergy in a patient with bakers asthma is described. On ISAC 112 IgE reactivity to wheat alpha-amylase/trypsin inhibitor (nTri a aA_TI) and lipid tranfer protein (rTri a 14) was found. We hypothesize that the reaction by oral ingestion was elicited by homologous molecules in rice seeds.

Environmental pollutants may affect the allergenicity of pollen and thus the prevalence of allergies. Although a few of studies are available in literature, the connection between pollution and the allergen contentofpollenhasyettobeclearlydefined. Lombardy,ahighlypopulatedItalianregion,isconsideredoneofthemostpollutedareaallovertheworld. Inthisregion,thebehaviorofthealienplantAmbrosiaartemisiifoliaL.isofgreatconcern:ithasrapidly spreadinrecentyearsandithasbecomethesecondcauseofallergyinashorttime. The objective of this work was to evaluate the role of traffic related pollution on the allergenicity of ragweed pollen. The sub‐pollen‐particles release, the whole allergenicity and the allergen pattern were determined in ragweed pollen samples, collected in vegetated areas and along high traffic roads. Concerning sub‐pollen‐particles release, no statistically significant difference was found among samples. Specifically, after hydration, in all samples, regardless to the site of origin, the percentage of pollen releasing cytoplasmic material was very low (

Background. Little is known about the prevalence and clinical relevance of sensitization to shrimp allergens other than tropomyosin. Objective. We detected the prevalence of arginine kinase and sarcoplasmic calcium binding protein sensitization, and identified a high molecular weight allergen that is frequently recognized by Italian shrimp-allergic patients. Methods. Sera from 40 shrimp-allergic patients underwent the detection of IgE specific for arginine kinase (rPen m 2) and sarcoplasmic calcium-binding protein (rPen m 4) by ISAC 112 Microarray platform and immunoblot analysis. A high molecular weight shrimp allergen was identified by N-terminal amino acid sequencing. Results. IgE to rPen m 2 and rPen m 4 were found in 4/40 (10%) and 6/40 (15%) sera, respectively; two sera reacted to both allergens. Clinically, 6/8 Pen m 2 and/or Pen m 4 reactors experienced severe allergies to shrimp. On immunoblot, 4/6 rPen m 4-positive sera showed IgE reactivity at about 20 kDa, whereas no rPen m 2-positive serum reacted at about 40 kDa. Nineteen (47%) sera showed IgE reactivity at molecular weights > 60 kDa. Such profile was not associated with IgE reactivity to rPen m 2 or rPen m 4. N-terminal amino acid sequencing of the high molecular weight allergen led to the identification of hemocyanin. Conclusion. Shrimp arginine kinase and sarcoplasmic calcium-binding protein are minor allergens sensitizing only 10% -15% of Italian shrimp-allergic patients, but are clinically relevant. Hemocyanin is a clinically relevant high molecular weight shrimp allergen possibly cross-reacting to house dust mite.

Sesame seed allergy, a potentially very severe food allergy, seems on the rise worldwide but is still uncommon in Italy. The aim of the present study was to investigate the allergenic profile of Italian sesame seed-allergic patients.Patients with genuine sesame seed allergy diagnosed over one year in a large number of allergy centers scattered through Italy were considered for the study. Their IgE reactivity to sesame seed allergens was characterized by immunoblot analysis.Eleven sesame seed allergic patients were detected and studied. 10/10 patients showed IgE reactivity against a sesame allergen at about 20 kDa, and 7/10 showed an extremely strong reactivity at about 32 kDa. The same 7 sera reacted also against a 28 kDa allergen, although such reactivity was significantly weaker in 6/7 cases. Eight patients showed IgE reactivity at about 48 kDa, and 5 sera reacted against higher m.w. proteins at about 67 kDa. Two sera showed IgE reactivity at about 43 kDa as well. Only one serum appeared to react to 2S-albumin.Italian sesame seed-allergic patients react mostly against allergens other than those described so far as major ones. A large number of recombinant sesame allergens will be needed for a comprehensive component- resolved diagnosis of allergy to this food.