نتایج جستجو برای: ige binding proteins

تعداد نتایج: 865783  

Journal: :The Journal of allergy and clinical immunology 1997
J Schuurman G J Perdok T E Lourens P W Parren M D Chapman R C Aalberse

A chimeric human IgE monoclonal antibody was developed against the house dust mite allergen Der p 2. This chimeric antibody (hIgE-Dp2A) was composed of the heavy-chain variable domains and light chains of the original murine monoclonal antibody retaining its binding characteristics, whereas the heavy-chain constant domains were exchanged with the human IgE heavy chain. The chimeric IgE expressi...

Journal: :The Journal of biological chemistry 1993
M W Robertson

The high affinity IgE receptor is a multisubunit complex that participates in IgE-dependent activation of mast cells and basophils. The IgE-binding portion of the receptor resides exclusively in the alpha-subunit and specifically within the 180 residues of the mature extracytoplasmic portion. In this study the contiguous two-domain human alpha-subunit has been displayed on the surface of a fila...

2015
Marta F. Gabriel Purificación González-Delgado Idoia Postigo Javier Fernández Victor Soriano Begoña Cueva Jorge Martínez

We report a case of a 38-year-old mold-allergic patient who developed episodes of generalized urticaria and systemic anaphylactic shock immediately after ingesting button mushrooms. A manganese-dependent superoxide dismutase (MnSOD) and a NADP-dependent mannitol dehydrogenase (MtDH) from Agaricus bisporus mushroom were identified as patient-specific IgE-binding proteins. Cross-reactivity betwee...

Journal: :Molecular medicine reports 2015
Chung-Ryul Kim Kyoung Yong Jeong Myung-Hee Yi Hyoung-Pyo Kim Ho-Joon Shin Tai-Soon Yong

Group-5 and group-21 allergens, produced by house dust mites and storage mites are 36.6-55.8% identical in their sequences and are recognized by at least 50% of immunoglobulin (Ig)E from the sera of individuals allergic to dust mites. In the present study, recombinant group-5 and ‑21 allergens from three mite species, Dermatophagoides farinae (rDer f 5 and 21), Tyrophagus putrescentiae (rTyr p ...

Objective(s): New generation of allergy vaccines is capable of promoting the development of protective IgG and blocking the functionality of allergen-specific IgE. We incorporated universal and powerful T-cell epitopes from tetanus and diphtheria toxoids (TD epitope) into recombinant Che a 2, the well-known allergic profilin of Chenopodium album, to determine its immun...

2014
Greg Plunkett Domingo Barber Eliseo M Villalobos Joshua S Jacobs Jeffrey S Hallett Tara Mostofi Agustin Galan Nieto Tricia Moore

Background Panallergens like profilin are proteins that have very similar sequences and structure. People can develop IgE specific to these highly cross reactive panallergens. The purpose of this study was to determine the prevalence of profilin sensitivity and the contribution to multiple allergen skin test responses. Sensitivity to profilin was established by IgE binding to purified profilins...

2013
C Pekar H Berkner L Vogel M Gubesch L Meisel S Randow L Ries T Holzhauser J Lidholm S Vieths P Rösch O Hartl-Spiegelhauer D Schiller

Background Millions of patients with allergy to tree pollen are sensitized to the major allergen of birch (Betula verrucosa) pollen, Bet v 1. Bet v 1-specific IgE cross-reacts with Bet v 1-homologous proteins from plant foods. Only little information on functional IgE epitopes of Bet v 1 and Bet v 1-like allergens in foods is available. We sought to generate a synthetic protein tool to identify...

2009
A. Ahuva Nissim

To map precisely the binding site of the high affinity receptor (FcεRI) on IgE we have constructed and expressed recombinant human and mouse IgE genes with anti-NIP specificity. Various mutated and chi-meric molecules thus prepared were studied for their ability to bind to rat mast cells or transfected fibro-blasts expressing human FcεRI α chain. To avoid destruction of the FcεRI binding site d...

Journal: :The Journal of Experimental Medicine 1999
Christina Mayer Ulrich Appenzeller Heike Seelbach Gernot Achatz Hannes Oberkofler Michael Breitenbach Kurt Blaser Reto Crameri

A panel of cDNAs encoding allergenic proteins was isolated from an Aspergillus fumigatus cDNA library displayed on the surface of filamentous phage. Solid phase-immobilized serum immunoglobulin E (IgE) from A. fumigatus-allergic individuals was used to enrich phage displaying IgE-binding molecules. One of the cDNAs encoded a 11.1-kD protein that was identified as acidic ribosomal phosphoprotein...

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