A folded and immunogenic IgE-hyporeactive variant of the major allergen Phl p 1 produced in Escherichia coli.

Levin, Mattias; Otten, Harm; von Wachenfeldt, Claes; Ohlin, Mats (2015). A folded and immunogenic IgE-hyporeactive variant of the major allergen Phl p 1 produced in Escherichia coli.. BMC Biotechnology, 15,
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DOI:
| Published | English
Authors:
Levin, Mattias ; Otten, Harm ; von Wachenfeldt, Claes ; Ohlin, Mats
Department:
Department of Immunotechnology
MAX IV Laboratory
Molecular Cell Biology
Microbiology Group
Project:
Human IgE repertoires and an anti-allergome resource
Research Group:
Microbiology Group
Abstract:
Group 1 grass pollen allergens are a major cause of allergic disease. Specific immunotherapy involving controlled administration of allergens can be used as a disease-modifying treatment for such disease. Recombinant allergen variants with reduced IgE binding capacity may be used as component in such vaccines, as they may induce fewer treatment side effects than materials currently in use. A mutated variant of the immunodominant C-terminal domain of the group 1 grass pollen allergen Phl p 1 was recently established through an approach that used a set of human monoclonal IgE as a guide to identify mutations that disturbed IgE-allergen interactions. Further analysis of this domain is required to establish its potential for use in treatment.
ISSN:
1472-6750

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