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This study showed that an iron sulfate free diet in combination with systemic iron repletion prevents the development of chronic ileitis in a murine model of Crohn's disease. Luminal iron may directly affect IEC function or generate a pathological milieu in the intestine that triggers epithelial cell stress-associated apoptosis through changes in microbial homeostasis. These results suggest that oral replacement therapy with iron sulfate may trigger inflammatory processes associated with progression of Crohn's disease-like ileitis.

Approximately 30-50 '6 of individuals who are Key words cross-reactive allergen food allergy, latex allergy Abbreviations used NRL, natural rubber latex, PR protein introduction pathogenesis-related protein. SPT, skin pnck test 'To whom comspondence should be addressed (e-rnail Stefan Wagner@ akh-wien ac at) Allergy to natural rubber latex (NRL) continues to be a feature of allergy practice world-wide. IgE-

Background: Plant profilins are important pan-allergens. They are responsible for a significant percentage of pollen-related allergies. Limited information is available about their involvement in the latex-fruit syndrome and the cross-reactivities between latex and pollen. We aimed to clone and express the Hevea brasiliensis latex profilin to investigate its allergological significance and serological cross-reactivities to profilins from plant foods and pollens. Methods: A DNA complementary to messenger RNA (cDNA) coding for the Hevea latex profilin, Hev b 8, was amplified by polymerase chain reaction from latex RNA. Recombinant (r)Hev b 8 was produced in Escherichia coli and used to screen sera from 50 latex- allergic health care workers (HCWs) with well-documented histories of food and pollen allergy and 34 latex-allergic spina bifida (SB) patients. The cross-reactivity of natural Hev b 8 and rHev b 8 with other plant profilins was determined by ELISA inhibition assays. A three-dimensional homology model of Hev b 8 was constructed based on known profilin structures. Results: The cDNA of Hev b 8 encoded a protein of 131 amino acids with a predicted molecular mass of 14 kD. Twelve of the 50 HCWs and 2 of the 34 SB patients were sensitized to Hev b 8. All Hev b 8-sensitized patients showed allergic symptoms to pollen or plant foods. Cross-reactivities between profilins of latex, pollen and plant food were illustrated by their ability to inhibit IgE binding to rHev b 8. Homology modeling of Hev b 8 yielded a structure highly similar to Bet v 2, the birch pollen profilin, with the most distinct differences located at the N-terminus. Conclusions: We conclude that primary sensitization to latex profilin in the majority of cases takes place via pollen or food profilins. Additionally, pollinosis and food-allergic patients with profilin-specific IgE can be at risk of developing latex allergy.

Kiwifruit is a significant elicitor of allergy both in children and adults. Digestibility of two kiwifruit allergens, actinidin (Act d 1) and thaumatin-like protein (Act d 2), was assessed using an in vitro digestion system that approximates physiological conditions with respect to the passage of food through the stomach into the duodenum. Act d 1 precipitated in simulated gastric fluid at pH 2 and digestion of the aggregated protein proceeded slowly. The residual precipitate redissolved completely in simulated duodenal fluid at pH 6.5 and was partially digested. Forty percent of Act d 2 remained intact during gastric digestion and were cleaved by duodenal proteases into large fragments covalently linked by disulfide bonds. Both digested allergen samples displayed nearly unchanged IgE binding abilities. Circular dichroism spectra were used to analyze heat and acid-induced unfolding. Thermal stability of both allergens was strongly pH dependent. While Act d 1 was irreversibly destabilized in acidic solutions, heat-induced denaturation of Act d 2 at pH 2 was fully reversible. IgE binding to Act d 2 but not Act d 1 was detected in processed food products. The stability of Act d 1 and Act d 2 provides one explanation for the allergenic potency of kiwifruit.

Latex allergy has been studied in detail in Europe and the US over the past two decades, resulting in specific guidelines that succeeded in reducing its incidence in high-risk populations within the medical field. How these developments have affected high-risk populations outside the health care scenario is an important unanswered question. In addition, a second wave of latex allergy may occur in nations that are striving to attain higher economic and technologic standards, including population-dense countries such as China. Therefore, the application of Hevea allergens in novel diagnostic assays and the development of specific latex immunotherapy will provide new opportunities for latex allergy research. In this review, we summarize current knowledge on the immunological properties of the 13 officially accepted Hevea brasiliensis latex allergens.

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IgE-mediated hypersensitivity to latex proteins present in health care products, particularly in latex gloves, has become an important public health problem in recent years. We purified natural Hev b 7, a 43-kDa patatin-like allergen from the latex of Hevea brasiliensis and determined several internal peptide sequences. A heterologous hybridization probe of a patatin gene of potato, to which these peptides could be aligned best, was used to screen a latex cDNA library. The cDNA encoded an acidic protein of 388 amino acids with a molecular mass of 42.9 kDa. The deduced amino acid sequence had 39Ϫ42% identity to patatins from Solanum tuberosum. The purified recombinant Hev b 7 expressed in the yeast Pichia pastoris displayed, similarly to patatins from S. tuberosum, esterase activity. Both natural and recombinant Hev b 7 were recognized by IgE from sera of latex-sensitized allergic individuals. In contrast to patatins from S. tuberosum and Nicotiana tabacum, natural Hev b 7 lacked an N-terminal leader peptide for targeting to the endoplasmatic reticulum and was not glycosylated. These results establish the 43-kDa patatin-like protein as a latex allergen and raise the possibility of different cellular localization and function compared to S. tuberosum patatins.Keywords : latex allergy; Hev b 7; Hevea ; Pichia pastoris; type-I allergy.IgE-mediated hypersensitivity to natural rubber latex (NRL) allergenic potential and therefore potential hazards of latex products. This knowledge will help to make decisions whether to has become a serious medical problem especially among health care workers and patients who have to undergo repeated surger-withhold certain latex products or batches with high allergen content. ies such as patients with spina bifida [1, 2]. The increase in allergic reactions to latex has been partially attributed to the The presence of latex allergens in the 43Ϫ46-kDa range was demonstrated by several investigators [6, 7, 10Ϫ12]. The high enormous increase in the use of latex gloves for protection against HIV and hepatitis B and C [3, 4].prevalence of IgE antibodies against these latex allergens ranging from 23% [12] to 80% [6] and their presence in ammoniIn fresh NRL, the source material for manufactured latex products, a variety of IgE-binding proteins with molecular ated, non-ammoniated latex and manufactured latex products made these allergens especially interesting targets for diagnosis masses ranging over 5Ϫ110 kDa were detected by two-dimensional immunoblotting [5Ϫ7]. In 1993, the first latex allergen of latex allergy and monitoring of allergen content in consumer products. Recently, Beezhold et al. [11,12] reported a 46-kDa was identified at the molecular level as the rubber elongation factor [8]. Since then, a total of eight NRL allergens have re-latex protein that bound IgE from sera of 9/40 (23%) latexallergic health care workers in IgE immunoblots. Two peptide ceived an international nomenclature designation [9]. The full coding sequence is only known for Hev b 1, Hev b 2 (a β-1,3-sequences...