PubMed · 8365166
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E J Klemm. 1993. Patch testing with glyceryl monothioglycolate.. https://doi.org/10.1111/j.1600-0536.1993.tb04551.x
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Bet v 1 is the major birch pollen allergen and therefore the main cause of type I allergies observed in early spring. It is composed of 159 amino acid residues adding up to a molecular mass of 17 kDa. We determined the secondary structure and tertiary fold of full-length Bet v 1 by NMR spectroscopy. Two- and three-dimensional NMR measurements suggest that Bet v 1 is a globular monomer in solution with a high content of well defined secondary structure. Of the total of 159 residues, 135 could be sequentially assigned, using an improved assignment strategy based mainly on heteronuclear experiments. An improved strategy for structure calculation revealed three helices and two beta-sheets as major elements of secondary structure. The globular tertiary structure is mainly stabilized by two antiparallel beta-sheets. The two helices at the C terminus are in accordance with the results from the solution structure of the chemically synthesized peptide Bet v 1-(125-154). This peptide is composed of two helices connected by a hinge. The structural features of Bet v 1 are highly similar to those found in the Ambrosia allergen Amb t V.
Group 1 and 5 allergens of different grasses possess similar physicochemical parameters (molecular weight, pI) and therefore separation with conventional chromatographic methods (gel filtration, ion exchange chromatography) is difficult or impossible to achieve. In this paper we describe the isolation of biologically active group 1 and 5 allergens from extracts of Lolium perenne and Phleum pratense by means of reverse phase chromatography on HPLC. The chromatograms showed very different retention times for group 1 (Rt 19.1-20.5 min) and group 5 (Rt 24.3-26.3 min) containing fractions. In addition, this technique is suitable for the separation of group 5 allergens into 5a and 5b subgroups and for the estimation of the amounts of allergen (groups 1 and 5) in the different extracts.
The role of CD45RA T cells on allergen-dependent lymphocyte functions was analyzed in atopic patients. As compared with age-matched nonatopic controls, atopic patients exhibited a significantly (p < 0.01) increased frequency of CD45RA T cells in peripheral blood. Concentration of serum IgE correlated with increases in this T cell subset. In contrast to nonatopic controls, not only CD45RO but also CD45RA T cells from atopic patients provide help for allergen-stimulated IgE and IgA production, and they act in a synergistic fashion. Transwell coculture experiments revealed that optimal production of IgE and IgA required physical contact of CD45RA T cells with B cells. Freshly prepared and in vitro-activated CD45RO and CD45RA T cells from atopic patients showed an increased expression of CD40 ligand when compared with nonatopic individuals. In addition, CD45RA (and CD45RO) T cells from atopic individuals produced IL-4, IL-5, and IFN-gamma when stimulated with mitogens. Whereas stimulation of normal lymphocytes with tetanus Ag was followed by conversion of the CD45RA to the CD45RO phenotype, T cells from atopic donors did not acquire the CD45RO isoform to the same degree despite T cell activation. In atopic patients, addition of IL-4 to anti-CD3/anti-TCR stimulated CD45RA T cell prevented the shift towards the CD45RO phenotype. These data indicate that a subset of CD45RA T cells plays a unique role as effector T cells regulating IgE and IgA production in atopic patients.