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Characterization of the human T cell response to antigen 5 from Vespula vulgaris (Ves v 5) (2005)

Bohle, B. ; Zwölfer, B. ; Fischer, G. F. ; [et al.]

Oxford, UK : Blackwell Science Ltd

Clinical & experimental allergy 35 (2005), S. 0

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ISSN: 1365-2222

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: Background The T cell reactivity to the major allergen of bee venom, phospholipase A2, has been thoroughly characterized. In contrast, only little is known about the human cellular response to major allergens from wasp venom.Objective To characterize the human T cell response to antigen 5 from Vespula vulgaris, Ves v 5.Methods Recombinant Ves v 5 was used to establish allergen-specific T cell lines (TCL) and T cell clones (TCC) from the peripheral blood of vespid-allergic and non-allergic individuals. Ves v 5-specific TCL were mapped for T cell epitopes using overlapping synthetic peptides representing the complete amino acid sequence of Ves v 5. Ves v 5-specific TCC were analysed for antigen-induced secretion of IL-4, IFN-γ and IL-10.Results Seventeen distinct T cell epitopes were recognized by allergic individuals among which Ves v 5181–192 was identified as a dominant T cell epitope. Partially different epitopes were observed in TCL from non-allergic subjects and the dominant epitope Ves v 5181–192 was not prevalent in these cultures. Ves v 5-specific TCC isolated from allergic individuals did not show the typical T helper type 2 (Th2)-like cytokine profile in response to specific stimulation, i.e. high amounts of IL-4 and low IFN-γ. TCC from non-allergic individuals showed a Th1-like cytokine pattern.Conclusions Our findings provide evidence that the allergic T cell response to Ves v 5 is not Th2-dominated and that different immunogenic sites on this major wasp venom allergen are recognized by allergic and non-allergic individuals.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1365-2222.2005.02180.x

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Internal symmetry of the molecular chaperone cpn60 (GroEL) determined by X-ray crystallography (1994)

Spangfort, M. D. ; Surin, B. P. ; Dixon, N. E. ; [et al.]

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 50 (1994), S. 591-595

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: The Escherichia coli molecular chaperone cpn60 oligomer, [cpn60]14, also called GroEL, has been crystallized and examined by X-ray crystallography and self-rotation function calculations. The crystals show unit-cell dimensions a = 143.3, b = 154.6 and c = 265 Å, with α = 82, β = 95 and γ = 107°. The space group is P1 and crystals diffract to 7 Å. X-ray analysis shows that the oligomer has one sevenfold symmetry axis and seven twofold axes that are all perpendicular to the sevenfold. The symmetry suggests that [cpn60]24 consists of two heptamers, [cpn60]7, stacked on top of each other. The orientations of the symmetry axes of the two independent [cpn60]14 oligomers in the triclinic unit cell have been determined relative to the crystallographic axes. The two oligomers in the unit cell are arranged side-by- side, but the second oligomer is rotated 26° around the sevenfold axis relative to the first oligomer.