PubMed · 6230327
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K Keczkes. 1984. Does contact sensitivity last?. https://doi.org/10.1111/j.1365-4362.1984.tb05681.x
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The clone FHG22, isolated from a female minus male subtracted cDNA library obtained from the sexually dimorphic Syrian hamster Harderian glands (HG) is 440 bp long with a 95 amino acids ORF, and hybridizes to a female HG-specific 0.6 kb mRNA. The FHG22 nucleotide and amino acid sequences are similar to the subunits from prostatein, uteroglobin, major cat allergen Fel dI (chain 1) and mouse salivary androgen binding proteins (subunit alpha). Therefore I propose that all those polypeptides belong to a common new family. The hamster genome has a single copy of the FHG22 gene, without homologous genes. FHG22 mRNA is also found in male and female parotid (higher levels in females) and submandibular glands, indicating a tissue and sex-dependent control of expression.
This study investigated the ability of an immunogold labeling technique to demonstrate the presence of Fel d 1 (domestic cat) allergens on the surface of particles in samples of airborne house dust. Suspended particulate matter was sampled from ten Norwegian households, five with and five without a domestic cat. The specimens were immunogold labeled and examined in the backscatter electron imaging mode of the scanning electron microscope and in the transmission electron microscope. X-ray microanalysis was also applied to execute element analysis of the suspended particular matter. The gold probe was mainly detected on carbon particles in the suspended particulate matter, both on small (< 1 microns) and larger carbon aggregates (1-10 microns). The present method may be useful in studying the localisation of different allergens on airborne house dust particles of various sizes and composition.
Individuals suffering from immediate hypersensitivity (type-I allergy) to a particular pollen frequently display intolerance to several foods of plant origin. In this respect, individuals sensitized to birch pollen and/or mugwort pollen frequently display type-I allergic symptoms after ingestion of celery. In this study, we expressed the major allergenic protein of celery, Api g 1, which is responsible for the birch-celery syndrome, in the form of a non-fusion protein. The open reading frame of the cDNA of Api g 1 codes for a protein of 153 amino acids with a molecular mass of 16.2 kDa and 40% identity (60% similarity) to the major allergen of birch pollen, Bet v 1. Furthermore, Api g 1 exhibited similar characteristics to (a) two proteins in parsley induced by fungal infection, (b) the major tree pollen allergens and (c) pathogenesis-related and stress-induced proteins in other plant species. The reactivity of recombinant Api g 1 with IgE antibodies present in sera from celery intolerant patients was comparable to that of the natural celery allergen. Cross-reactivity with Bet v 1 was proven by cross-inhibition experiments, which provides further support for the existence of the birch-celery syndrome and for the suggestion that allergies to some vegetable foods are epiphenomena to allergies caused by inhalation of tree pollen.