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Crystal structure of the major celery allergen Api g 1 : molecular analysis of cross-reactivity

Schirmer, Tilman and Hoffimann-Sommergrube, Karin and Susani, Markus and Breiteneder, Heimo and Marković-Housley, Zora. (2005) Crystal structure of the major celery allergen Api g 1 : molecular analysis of cross-reactivity. Journal of molecular biology, Vol. 351, H. 5. S. 1101-1109.

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Official URL: http://edoc.unibas.ch/dok/A5258246

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Abstract

Many patients who have been sensitised to pollen, display allergic symptoms after ingestion of certain plant food such as fresh fruit, vegetables and nuts. The cause is the cross-reactivity between structurally very similar major plant allergens. In particular, allergy to celery is very frequently associated with birch and mugwort pollen sensitization, known as to the birch-mugwort-celery syndrome. The crystal structure of the major celery allergen Api g 1, a homologue of the major birch pollen allergen Bet v 1, has been determined to a resolution of 2.9 A. The structure of Api g 1 is very similar to that of Bet v 1 with major differences occurring in the segment comprised of residues 23-45, preceding the well conserved glycine-rich P-loop, as well as in loops beta3-beta4 and beta5-beta6. In particular, Api g 1 lacks E45, which has been shown to be a crucial residue for antibody recognition in the crystal complex of Bet v 1 with the Fab fragment of a murine monoclonal IgG (BV16) antibody. The absence of E45 and the structural differences in the preceding segment suggest that this region of the Api g 1 surface is probably not responsible for the observed cross-reactivity with Bet v 1. A detailed analysis of the molecular surface in combination with sequence alignment revealed three conserved surface patches which may account for cross-reactivity with Bet v 1. Several residues of Bet v 1 which have been shown by mutagenesis studies to be involved in IgE recognition belong to these conserved surface regions. The structure of Api g 1 and the related epitope analysis provides a molecular basis for a better understanding of allergen cross-reactivity and may lead to the development of hypoallergens which would allow a safer immunotherapy.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Schirmer)
UniBasel Contributors:Schirmer, Tilman and Housley-Markovic, Zora
Item Type:Article, refereed
Bibsysno:Link to catalogue
Publisher:Elsevier
ISSN:0022-2836
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:07 Aug 2015 12:05
Deposited On:22 Mar 2012 13:20

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