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

Levin, Mattias LU ; Otten, Harm LU ; von Wachenfeldt, Claes LU and Ohlin, Mats LU (2015) In BMC Biotechnology 15.
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.
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
BMC Biotechnology
volume
15
publisher
BioMed Central
external identifiers
  • pmid:26054338
  • wos:000356030500001
  • scopus:84931033092
ISSN
1472-6750
DOI
10.1186/s12896-015-0150-z
language
English
LU publication?
yes
id
ca339a7d-14a0-4c64-a178-18315212c0ef (old id 7487486)
date added to LUP
2015-07-20 10:14:42
date last changed
2017-08-06 04:05:55
@article{ca339a7d-14a0-4c64-a178-18315212c0ef,
  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.},
  articleno    = {52},
  author       = {Levin, Mattias and Otten, Harm and von Wachenfeldt, Claes and Ohlin, Mats},
  issn         = {1472-6750},
  language     = {eng},
  publisher    = {BioMed Central},
  series       = {BMC Biotechnology},
  title        = {A folded and immunogenic IgE-hyporeactive variant of the major allergen Phl p 1 produced in Escherichia coli.},
  url          = {http://dx.doi.org/10.1186/s12896-015-0150-z},
  volume       = {15},
  year         = {2015},
}