PubMed · 15912630
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Sheikh Arshad Saeed. 2005. Hyposensitization.. https://pubmed.ncbi.nlm.nih.gov/15912630/
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Consumption of apples can provoke severe allergic reactions, in susceptible individuals, due to the presence of the allergen Mal d 3, a nonspecific lipid transfer protein, found largely in the fruit skin. Levels of Mal d 3 were determined in peel as a function of apple cultivar, position of the fruit growing on the tree, apple maturity, and postharvest storage by ELISA. As the apples mature, Mal d 3 levels increased, although the rate was dependent on cultivar and tree position. During storage, levels of Mal d 3 decreased in all cultivars (cvs. Cox, Jonagored, and Gala), the rate of overall decrease being greatest under controlled atmosphere conditions. There was no correlation between Mal d 3 levels and total apple peel protein, indicating specific alterations in Mal d 3 expression. Thus pre- and postharvest treatments (i.e., storage) can modify the allergen load in apple peel, the highest levels being found in overly mature and freshly harvested fruits.
We analyzed, from the literature, the balance benefit/risk of a strict avoidance of peanut in children with peanut allergy. The benefits of a strict avoidance diet seem limited: reactions to the low doses and to the peanut oil refined are rare and most often slight. It is not proven that a strict avoidance facilitates the cure of allergy. On the other hand, strict avoidance could induce a worsening of allergy, with deterioration of quality of life, creation of food neophobia. In case of cure of allergy, it is difficult to normalize the diet after a strict avoidance. Outside of the rare sensitive patients to a very low dose of peanut, for which a strict avoidance is counseled, the report benefits risk is in favor of the prescription of adapted avoidance to the eliciting dose. For the majority of the peanut allergic children, it seems to us that the avoidance can and must be limited to the non hidden peanut.
cDNAs encoding the immunodominant allergens tropomyosin and paramyosin were amplified from RNA extracted from the sheep scab mite Psoroptes ovis. The tropomyosin cDNA contained an open reading frame (ORF) of 852 bp which encoded a predicted protein with 98% and 97% identity to the house dust mite allergens Der f 10 and Der p 10 respectively. The complete paramyosin ORF generated by RT-PCR was 2625 bp in length and encoded an 875aa predicted protein of 102.6 kDa with 97%, 95% and 89% identity to the paramyosins of Dermatophagoides pteronyssinus (Der p 11), Sarcoptes scabiei and Blomia tropicalis (Blo t 11) respectively. Full length tropomyosin and truncated and full-length paramyosin were expressed as recombinant proteins. IgG and IgE in sera from sheep with a 6-week duration primary infestation of P. ovis did not detect either full-length or truncated recombinant paramyosin. IgG in both infested and naïve sheep sera detected recombinant tropomyosin, suggesting cross-reactivity to tropomyosin and to other invertebrate species to which the sheep may have been exposed. Staining with antibodies directed against tropomyosin and paramyosin was observed throughout sections of P. ovis. Staining was especially prevalent in the anterior sections of the mites, possibly associated with locomotory muscles in this region.